[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). PubMed=6319097 [NCBI, ExPASy, EBI, Israel, Japan] Bollen A., Herzog A., Cravador A., Herion P., Chuchana P., van der Straten A., Loriau R., Jacobs P., van Elsen A.; "Cloning and expression in Escherichia coli of full-length complementary DNA coding for human alpha 1-antitrypsin."; DNA 2:255-264(1983).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1021/bi00316a003; PubMed=6093867 [NCBI, ExPASy, EBI, Israel, Japan] Long G.L., Chandra T., Woo S.L.C., Davie E.W., Kurachi K.; "Complete sequence of the cDNA for human alpha 1-antitrypsin and the gene for the S variant."; Biochemistry 23:4828-4837(1984).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF MET-382. DOI=10.1038/312077a0; PubMed=6387509 [NCBI, ExPASy, EBI, Israel, Japan] Rosenberg S., Barr P.J., Najarian R.C., Hallewell R.A.; "Synthesis in yeast of a functional oxidation-resistant mutant of human alpha-antitrypsin."; Nature 312:77-80(1984).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1016/S0092-8674(85)80026-X; PubMed=2985281 [NCBI, ExPASy, EBI, Israel, Japan] Ciliberto G., Dente L., Cortese R.; "Cell-specific expression of a transfected human alpha 1-antitrypsin gene."; Cell 41:531-540(1985).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION OF VARIANT Z. PubMed=3491072 [NCBI, ExPASy, EBI, Israel, Japan] Nukiwa T., Satoh K., Brantly M.L., Ogushi F., Fells G.A., Courtney M., Crystal R.G.; "Identification of a second mutation in the protein-coding sequence of the Z type alpha 1-antitrypsin gene."; J. Biol. Chem. 261:15989-15994(1986).
[6]	ERRATUM. Nukiwa T., Satoh K., Brantly M.L., Ogushi F., Fells G.A., Courtney M., Crystal R.G.; J. Biol. Chem. 262:10412-10412(1987).
[7]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-237 AND ASP-400. TISSUE=Liver; PubMed=17650587 [NCBI, ExPASy, EBI, Israel, Japan] Shasany A.K., Shukla A.K., Darokar M.P., Saraiya M., Chaturvedi N., Tewari L., Khanuja S.P.; "An alpha-1 antitrypsin genetic variant from India."; Indian J. Biochem. Biophys. 44:176-178(2007).
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-172; ALA-237 AND LYS-366. TISSUE=Lymphocyte; Balduyck M., Porchet N., Aubert J.-P., Zerimech F., Douchain F., Verchain S.; "Characterization of a new variant of alpha1 antitrypsin M Lille (p.Gly148Trp)."; Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Fetal liver; Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhou W., Bi J., Zhang Y., Liu M., He F.; "Functional prediction of the coding sequences of 32 new genes deduced by analysis of cDNA clones from human fetal liver."; Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[10]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). TISSUE=Fetal liver, and Placenta; Li W.B., Gruber C., Jessee J., Polayes D.; "Full-length cDNA libraries and normalization."; Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[11]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Synovium; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[12]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-237. Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.; "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[13]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Colon, and Ovary; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[14]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67; 196-255 AND 387-418. DOI=10.1038/297655a0; PubMed=6979715 [NCBI, ExPASy, EBI, Israel, Japan] Leicht M., Long G.L., Chandra T., Kurachi K., Kidd V.J., Mace M. Jr., Davie E.W., Woo S.L.C.; "Sequence homology and structural comparison between the chromosomal human alpha 1-antitrypsin and chicken ovalbumin genes."; Nature 297:655-659(1982).
[15]	PRELIMINARY PROTEIN SEQUENCE OF 25-418 (ISOFORM 1). Chan S.K.; "The covalent structure of human alpha1-protease inhibitor."; Fed. Proc. 41:1016-1016(1982).
[16]	PROTEIN SEQUENCE OF 25-418 (ISOFORM 1). DOI=10.1038/298329a0; PubMed=7045697 [NCBI, ExPASy, EBI, Israel, Japan] Carrell R.W., Jeppsson J.-O., Laurell C.-B., Brennan S.O., Owen M.C., Vaughan L., Boswell D.R.; "Structure and variation of human alpha 1-antitrypsin."; Nature 298:329-334(1982).
[17]	PROTEIN SEQUENCE OF 25-418 (ISOFORM 1), VARIANTS ABERRANT FORM 190-GLY--ARG-198 AND VAL-288, AND FUNCTION. TISSUE=Blood; Sinha A.K., Girish G.V.; "Appearance of an aberrant form of alpha-antitrypsin in the circulation of chronic cigarette smokers and its effect on the insulin induced NO synthesis in blood platelets."; Submitted (AUG-2007) to UniProtKB.
[18]	PROTEIN SEQUENCE OF 25-39, AND FUNCTION. TISSUE=Ascites; PubMed=1906855 [NCBI, ExPASy, EBI, Israel, Japan] Tanaka N., Sekiya S., Takamizawa H., Kato N., Moriyama Y., Fujimura S.; "Characterization of a 54 kDa, alpha 1-antitrypsin-like protein isolated from ascitic fluid of an endometrial cancer patient."; Jpn. J. Cancer Res. 82:693-700(1991).
[19]	PROTEIN SEQUENCE OF 30-48 AND 248-257 (ISOFORMS 1/2/3), GLYCOSYLATION AT ASN-70; ASN-107 AND ASN-271, STRUCTURE OF CARBOHYDRATES, CYSTEINE BINDING, AND MASS SPECTROMETRY. DOI=10.1002/pmic.200500751; PubMed=16622833 [NCBI, ExPASy, EBI, Israel, Japan] Kolarich D., Weber A., Turecek P.L., Schwarz H.P., Altmann F.; "Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms."; Proteomics 6:3369-3380(2006).
[20]	PROTEIN SEQUENCE OF 47-66. TISSUE=Urine; DOI=10.1006/bbrc.1993.1731; PubMed=8323530 [NCBI, ExPASy, EBI, Israel, Japan] Umekawa T., Kohri K., Amasaki N., Yamate T., Yoshida K., Yamamoto K., Suzuki Y., Sinohara H., Kurita T.; "Sequencing of a urinary stone protein, identical to alpha-one antitrypsin, which lacks 22 amino acids."; Biochem. Biophys. Res. Commun. 193:1049-1053(1993).
[21]	PROTEIN SEQUENCE OF 50-63 AND 161-178 (ISOFORMS 1/2/3), AND MASS SPECTROMETRY. TISSUE=Brain, and Cajal-Retzius cell; Lubec G., Afjehi-Sadat L.; Submitted (MAR-2007) to UniProtKB.
[22]	NUCLEOTIDE SEQUENCE [MRNA] OF 292-418 (ISOFORM 1). DOI=10.1016/0014-5793(85)81056-5; PubMed=3876243 [NCBI, ExPASy, EBI, Israel, Japan] Riley J.H., Bathurst I.C., Edbrooke M.R., Carrell R.W., Craig R.K.; "Alpha 1-antitrypsin and serum albumin mRNA accumulation in normal, acute phase and ZZ human liver."; FEBS Lett. 189:361-366(1985).
[23]	NUCLEOTIDE SEQUENCE [MRNA] OF 350-418 (ISOFORM 1). DOI=10.1073/pnas.78.11.6826; PubMed=7031661 [NCBI, ExPASy, EBI, Israel, Japan] Kurachi K., Chandra T., Friezner Degen S.J., White T.T., Marchioro T.L., Woo S.L.C., Davie E.W.; "Cloning and sequence of cDNA coding for alpha 1-antitrypsin."; Proc. Natl. Acad. Sci. U.S.A. 78:6826-6830(1981).
[24]	PROTEIN SEQUENCE OF 375-414, IDENTIFICATION OF SPAAT, FUNCTION, AND SUBCELLULAR LOCATION. TISSUE=Placenta; PubMed=1406456 [NCBI, ExPASy, EBI, Israel, Japan] Niemann M.A., Narkates A.J., Miller E.J.; "Isolation and serine protease inhibitory activity of the 44-residue, C-terminal fragment of alpha 1-antitrypsin from human placenta."; Matrix 12:233-241(1992).
[25]	NUCLEOTIDE SEQUENCE [MRNA] OF 387-418 (ISOFORM 1). PubMed=3873938 [NCBI, ExPASy, EBI, Israel, Japan] Coutelle C., Speer A., Rogers J., Kalsheker N., Humphries S., Williamson R.; "Construction and partial characterization of a human liver cDNA library."; Biomed. Biochim. Acta 44:421-431(1985).
[26]	GLYCOSYLATION AT ASN-70 AND ASN-271. DOI=10.1038/nbt827; PubMed=12754519 [NCBI, ExPASy, EBI, Israel, Japan] Zhang H., Li X.-J., Martin D.B., Aebersold R.; "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."; Nat. Biotechnol. 21:660-666(2003).
[27]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-271, AND MASS SPECTROMETRY. TISSUE=Bile; DOI=10.1074/mcp.M400015-MCP200; PubMed=15084671 [NCBI, ExPASy, EBI, Israel, Japan] Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; "A proteomic analysis of human bile."; Mol. Cell. Proteomics 3:715-728(2004).
[28]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-271, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1002/pmic.200300556; PubMed=14760718 [NCBI, ExPASy, EBI, Israel, Japan] Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."; Proteomics 4:454-465(2004).
[29]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan] Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.; "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."; J. Proteome Res. 4:2070-2080(2005).
[30]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1074/mcp.M500324-MCP200; PubMed=16263699 [NCBI, ExPASy, EBI, Israel, Japan] Lewandrowski U., Moebius J., Walter U., Sickmann A.; "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."; Mol. Cell. Proteomics 5:226-233(2006).
[31]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[32]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan] Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."; J. Proteome Res. 8:651-661(2009).
[33]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). DOI=10.1016/0022-2836(84)90298-5; PubMed=6332197 [NCBI, ExPASy, EBI, Israel, Japan] Loebermann H., Tokuoka R., Deisenhofer J., Huber R.; "Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function."; J. Mol. Biol. 177:531-556(1984).
[34]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). DOI=10.1093/protein/2.6.407; PubMed=2785270 [NCBI, ExPASy, EBI, Israel, Japan] Engh R., Loebermann H., Schneider M., Wiegand G., Huber R., Laurell C.-B.; "The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism."; Protein Eng. 2:407-415(1989).
[35]	X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 25-418. DOI=10.1016/0014-5793(95)01331-8; PubMed=8543039 [NCBI, ExPASy, EBI, Israel, Japan] Song H.K., Lee K.N., Kwon K.-S., Yu M.-H., Suh S.W.; "Crystal structure of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop."; FEBS Lett. 377:150-154(1995).
[36]	X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-418. DOI=10.1038/nsb0896-676; PubMed=8756325 [NCBI, ExPASy, EBI, Israel, Japan] Elliott P.R., Lomas D.A., Carrell R.W., Abrahams J.P.; "Inhibitory conformation of the reactive loop of alpha 1-antitrypsin."; Nat. Struct. Biol. 3:676-681(1996).
[37]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 45-418. DOI=10.1016/S0969-2126(96)00126-8; PubMed=8939743 [NCBI, ExPASy, EBI, Israel, Japan] Ryu S.-E., Choi H.-J., Kwon K.-S., Lee K.N., Yu M.-H.; "The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: crystal structure of an uncleaved alpha1-antitrypsin at 2.7 A."; Structure 4:1181-1192(1996).
[38]	X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-418. DOI=10.1006/jmbi.1997.1458; PubMed=9466920 [NCBI, ExPASy, EBI, Israel, Japan] Elliott P.R., Abrahams J.P., Lomas D.A.; "Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation."; J. Mol. Biol. 275:419-425(1998).
[39]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 48-418 IN COMPLEX WITH BOVINE TRYPSIN. DOI=10.1038/35038119; PubMed=11057674 [NCBI, ExPASy, EBI, Israel, Japan] Huntington J.A., Read R.J., Carrell R.W.; "Structure of a serpin-protease complex shows inhibition by deformation."; Nature 407:923-926(2000).
[40]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 44-418. PubMed=10716194 [NCBI, ExPASy, EBI, Israel, Japan] Dunstone M.A., Dai W., Whisstock J.C., Rossjohn J., Pike R.N., Feil S.C., Le Bonniec B.F., Parker M.W., Bottomley S.P.; "Cleaved antitrypsin polymers at atomic resolution."; Protein Sci. 9:417-420(2000).
[41]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). PubMed=10933492 [NCBI, ExPASy, EBI, Israel, Japan] Elliott P.R., Pei X.Y., Dafforn T.R., Lomas D.A.; "Topography of a 2.0 A structure of alpha1-antitrypsin reveals targets for rational drug design to prevent conformational disease."; Protein Sci. 9:1274-1281(2000).
[42]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-418. DOI=10.1006/jmbi.2000.4357; PubMed=11178897 [NCBI, ExPASy, EBI, Israel, Japan] Kim S.-J., Woo J.-R., Seo E.J., Yu M.-H., Ryu S.-E.; "A 2.1 A resolution structure of an uncleaved alpha(1)-antitrypsin shows variability of the reactive center and other loops."; J. Mol. Biol. 306:109-119(2001).
[43]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-418. DOI=10.1074/jbc.M207682200; PubMed=12244055 [NCBI, ExPASy, EBI, Israel, Japan] Im H., Woo M.-S., Hwang K.Y., Yu M.-H.; "Interactions causing the kinetic trap in serpin protein folding."; J. Biol. Chem. 277:46347-46354(2002).
[44]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-418 OF VARIANT PITTSBURGH ARG-382. DOI=10.1074/jbc.M305195200; PubMed=12860985 [NCBI, ExPASy, EBI, Israel, Japan] Dementiev A., Simonovic M., Volz K., Gettins P.G.; "Canonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinases."; J. Biol. Chem. 278:37881-37887(2003).
[45]	REVIEW. DOI=10.1007/BF01115992; PubMed=2669992 [NCBI, ExPASy, EBI, Israel, Japan] Kalsheker N.; "Alpha 1-antitrypsin: structure, function and molecular biology of the gene."; Biosci. Rep. 9:129-138(1989).
[46]	REVIEW. DOI=10.1002/bies.950130404; PubMed=1859394 [NCBI, ExPASy, EBI, Israel, Japan] Wu Y., Foreman R.C.; "The molecular genetics of alpha 1 antitrypsin deficiency."; Bioessays 13:163-169(1991).
[47]	CHARACTERIZATION OF VARIANT M2. PubMed=2901226 [NCBI, ExPASy, EBI, Israel, Japan] Nukiwa T., Brantly M.L., Ogushi F., Fells G.A., Crystal R.G.; "Characterization of the gene and protein of the common alpha 1-antitrypsin normal M2 allele."; Am. J. Hum. Genet. 43:322-330(1988).
[48]	VARIANT M3 ASP-400. DOI=10.1007/BF00206766; PubMed=2394452 [NCBI, ExPASy, EBI, Israel, Japan] Graham A., Hayes K., Weidinger S., Newton C.R., Markham A.F., Kalsheker N.A.; "Characterisation of the alpha-1-antitrypsin M3 gene, a normal variant."; Hum. Genet. 85:381-382(1990).
[49]	VARIANT F CYS-247. PubMed=2035534 [NCBI, ExPASy, EBI, Israel, Japan] Okayama H., Brantly M., Holmes M., Crystal R.G.; "Characterization of the molecular basis of the alpha 1-antitrypsin F allele."; Am. J. Hum. Genet. 48:1154-1158(1991).
[50]	VARIANT M-HEERLEN LEU-393. DOI=10.1007/BF00279001; PubMed=2784123 [NCBI, ExPASy, EBI, Israel, Japan] Hofker M.H., Nukiwa T., van Paassen H.M.B., Nelen M., Kramps J.A., Klasen E.C., Frants R.R., Crystal R.G.; "A Pro-->Leu substitution in codon 369 of the alpha-1-antitrypsin deficiency variant PI M-Heerlen."; Hum. Genet. 81:264-268(1989).
[51]	VARIANT M-MALTON PHE-75 DEL. PubMed=2786335 [NCBI, ExPASy, EBI, Israel, Japan] Fraizer G.C., Harrold T.R., Hofker M.H., Cox D.W.; "In-frame single codon deletion in the M-Malton deficiency allele of alpha 1-antitrypsin."; Am. J. Hum. Genet. 44:894-902(1989).
[52]	VARIANT M-MINERAL SPRINGS GLU-91. PubMed=1967187 [NCBI, ExPASy, EBI, Israel, Japan] Curiel D.T., Vogelmeier C., Hubbard R.C., Stier L.E., Crystal R.G.; "Molecular basis of alpha 1-antitrypsin deficiency and emphysema associated with the alpha 1-antitrypsin M-Mineral springs allele."; Mol. Cell. Biol. 10:47-56(1990).
[53]	VARIANT M-NICHINAN PHE-75 DEL. PubMed=2309708 [NCBI, ExPASy, EBI, Israel, Japan] Matsunaga E., Shiokawa S., Nakamura H., Maruyama T., Tsuda K., Fukumaki Y.; "Molecular analysis of the gene of the alpha 1-antitrypsin deficiency variant, M-Nichinan."; Am. J. Hum. Genet. 46:602-612(1990).
[54]	VARIANT M-PROCIDA PRO-65. PubMed=3262617 [NCBI, ExPASy, EBI, Israel, Japan] Takahashi H., Nukiwa T., Satoh K., Ogushi F., Brantly M., Fells G., Stier L., Courtney M., Crystal R.G.; "Characterization of the gene and protein of the alpha 1-antitrypsin 'deficiency' allele M-Procida."; J. Biol. Chem. 263:15528-15534(1988).
[55]	VARIANT P-DUARTE VAL-280. DOI=10.1002/humu.1380020311; PubMed=8364590 [NCBI, ExPASy, EBI, Israel, Japan] Hildesheim J., Kinsley G., Bissell M., Pierce J., Brantly M.; "Genetic diversity from a limited repertoire of mutations on different common allelic backgrounds: alpha 1-antitrypsin deficiency variant P-Duarte."; Hum. Mutat. 2:221-228(1993).
[56]	VARIANT PITTSBURGH ARG-382. PubMed=6604220 [NCBI, ExPASy, EBI, Israel, Japan] Owen M.C., Brennan S.O., Lewis J.H., Carrell R.W.; "Mutation of antitrypsin to antithrombin. Alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder."; N. Engl. J. Med. 309:694-698(1983).
[57]	VARIANT S-IIYAMA PHE-77. PubMed=1905728 [NCBI, ExPASy, EBI, Israel, Japan] Seyama K., Nukiwa T., Takabe K., Takahashi H., Miyake K., Kira S.; "Siiyama (serine 53 (TCC) to phenylalanine 53 (TTC)). A new alpha 1-antitrypsin-deficient variant with mutation on a predicted conserved residue of the serpin backbone."; J. Biol. Chem. 266:12627-12632(1991).
[58]	VARIANT V-MUNICH ALA-26. PubMed=2316526 [NCBI, ExPASy, EBI, Israel, Japan] Holmes M.D., Brantly M.L., Curiel D.T., Weidinger S., Crystal R.G.; "Characterization of the normal alpha 1-antitrypsin allele V-Munich: a variant associated with a unique protein isoelectric focusing pattern."; Am. J. Hum. Genet. 46:810-816(1990).
[59]	VARIANT W-BETHESDA THR-360. DOI=10.1016/0006-291X(90)90493-7; PubMed=2390072 [NCBI, ExPASy, EBI, Israel, Japan] Holmes M.D., Brantly M.L., Fells G.A., Crystal R.G.; "Alpha 1-antitrypsin W-Bethesda: molecular basis of an unusual alpha 1-antitrypsin deficiency variant."; Biochem. Biophys. Res. Commun. 170:1013-1020(1990).
[60]	VARIANT Z-AUGSBURG LYS-366. PubMed=2339709 [NCBI, ExPASy, EBI, Israel, Japan] Faber J.-P., Weidinger S., Olek K.; "Sequence data of the rare deficient alpha 1-antitrypsin variant PI Zaugsburg."; Am. J. Hum. Genet. 46:1158-1162(1990).
[61]	VARIANTS Z-WREXHAM LEU-4 AND Q0-NEWPORT SER-139. DOI=10.1007/BF00194233; PubMed=2227940 [NCBI, ExPASy, EBI, Israel, Japan] Graham A., Kalsheker N.A., Bamforth F.J., Newton C.R., Markham A.F.; "Molecular characterisation of two alpha-1-antitrypsin deficiency variants: proteinase inhibitor (Pi) Null(Newport) (Gly115-->Ser) and (Pi) Z Wrexham (Ser-19-->Leu)."; Hum. Genet. 85:537-540(1990).
[62]	VARIANTS P-CARDIFF VAL-280; I CYS-63 AND M-MALTON PHE-75 DEL. DOI=10.1007/BF00210671; PubMed=2606478 [NCBI, ExPASy, EBI, Israel, Japan] Graham A., Kalsheker N.A., Newton C.R., Bamforth F.J., Powell S.J., Markham A.F.; "Molecular characterisation of three alpha-1-antitrypsin deficiency variants: proteinase inhibitor (Pi) nullcardiff (Asp256-->Val); PiM-Malton (Phe51-->deletion) and PiI (Arg39-->Cys)."; Hum. Genet. 84:55-58(1989).
[63]	VARIANT QO-LUDWIGSHAFEN ASN-116. PubMed=2254451 [NCBI, ExPASy, EBI, Israel, Japan] Fraizer G.C., Siewertsen M.A., Hofker M.H., Brubacher M.G., Cox D.W.; "A null deficiency allele of alpha 1-antitrypsin, QO-Ludwigshafen, with altered tertiary structure."; J. Clin. Invest. 86:1878-1884(1990).
[64]	VARIANTS. PubMed=7977369 [NCBI, ExPASy, EBI, Israel, Japan] Faber J.-P., Poller W., Weidinger S., Kirchgesser M., Schwaab R., Bidlingmaier F., Olek K.; "Identification and DNA sequence analysis of 15 new alpha 1-antitrypsin variants, including two PIQ0 alleles and one deficient PIM allele."; Am. J. Hum. Genet. 55:1113-1121(1994).
[65]	VARIANT Z-BRISTOL MET-109. DOI=10.1017/S0003480097006404; PubMed=9459000 [NCBI, ExPASy, EBI, Israel, Japan] Lovegrove J.U., Jeremiah S., Gillett G.T., Temple I.K., Povey S., Whitehouse D.B.; "A new alpha 1-antitrypsin mutation, Thr-Met 85, (PI ZBristol) associated with novel electrophoretic properties."; Ann. Hum. Genet. 61:385-391(1997).
[66]	VARIANTS Y-BARCELONA VAL-280 AND HIS-415. PubMed=10651487 [NCBI, ExPASy, EBI, Israel, Japan] Jardi R., Rodriguez F., Miravitlles M., Vidal R., Cotrina M., Quer J., Pascual C., Weidinger S.; "Identification and molecular charaterization of the new alpha-1-antitrypsin deficient allele PI YBarcelona (Asp256Val and Pro391His)."; Hum. Mutat. 12:213-213(1998).
[67]	VARIANT SAO TOME HIS-386. Seixas S., Trovoada M.J., Santos M.T., Rocha J.; "A novel alpha-1-antitrypsin P362H variant found in a population sample from Sao Tome e Principe (Gulf of Guinea, West Africa)."; Hum. Mutat. 13:414-414(1999).
[68]	VARIANT BASQUE ARG-305 DEL. DOI=10.1002/(SICI)1098-1004(200001)15:1<121::AID-HUMU37>3.0.CO;2-U; PubMed=10612848 [NCBI, ExPASy, EBI, Israel, Japan] Seixas S., Garcia O., Amorim A., Rocha J.; "A novel alpha-1-antitrypsin r281del variant found in a population sample from the Basque country."; Hum. Mutat. 15:121-122(2000).

Comments

FUNCTION: Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.
FUNCTION: Short peptide from AAT (SPAAT) is a reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin.
INTERACTION:
P00760:- (xeno); NbExp=1; IntAct=EBI-986224, EBI-986385;
P00772:ELA1 (xeno); NbExp=1; IntAct=EBI-986224, EBI-986248;
SUBCELLULAR LOCATION: Secreted.
SUBCELLULAR LOCATION: Short peptide from AAT: Secreted, extracellular space, extracellular matrix.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	P01009-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P01009-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_028889.

Name	3
Isoform ID	P01009-3
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_028890.

TISSUE SPECIFICITY: Plasma.
DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
PTM: Several isomers are observed, resulting from the combination of different N-linked glycan structures and mature N-terminus. N-linked glycan at Asn-107 is alternatively di-antennary, tri-antennary or tetra-antennary, whereas glycan at Asn-70 is di-antennary with trace amounts of tri-antennary, and glycan at Asn-271 is exclusively di-antennary. The structure of the antennas is Neu5Ac(alpha1-6)Gal(beta1-4)GlcNAc attached to the core structure Man(alpha1-6)[Man(alpha1-3)]Man(beta1-4)GlcNAc(beta1-4)GlcNAc. Some antennas are fucosylated, which forms a Lewis-X determinant.
PTM: Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418.
POLYMORPHISM: The sequence shown is that of the M1V allele which is the most common form of PI (44 to 49%). Other frequent alleles are: M1A 20 to 23%; M2 10 to 11%; M3 14 to 19%.
DISEASE: The major physiological function of AAT is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE). A hereditary deficiency of AAT, is associated with a 20-30 fold increased risk of developing chronic obstructive pulmonary disease.
DISEASE: Deficiency of the normal inhibitor in individuals homozygous for allele Z or M-Malton can result in the development of chronic emphysema or infantile liver cirrhosis.
DISEASE: Variant Pittsburgh is the cause of bleeding diathesis.
MISCELLANEOUS: The aberrant form is found in the plasma of chronic smokers, and persists after smoking is ceased. It can still be found ten years after smoking has ceased.
SIMILARITY: Belongs to the serpin family.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=SERPINA1";.
WEB RESOURCE: Name=Wikipedia; Note=Alpha-1 antitrypsin entry; URL="http://en.wikipedia.org/wiki/Alpha_1-antitrypsin";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

K01396; AAB59375.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
K02212; AAB59495.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X01683; CAA25838.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11465; AAA51546.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J02619; AAA51547.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ682455; ABG73380.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AM048838; CAJ15161.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF113676; AAF29581.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF130068; AAG35496.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX161449; CAD61914.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX247968; CAD62306.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX248002; CAD62334.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX248257; CAD62585.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK315637; BAG38005.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019455; AAV38262.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011991; AAH11991.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015642; AAH15642.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J00064; AAB59369.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J00066; AAB59370.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J00065; AAB59370.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J00067; AAB59371.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02920; CAA26677.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
V00496; CAA23755.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26123; AAA51545.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00553177; -.
IPI00790784; -.
IPI00869004; -.

PIR

A21853; ITHU.
A61391; A61391.

RefSeq

NP_000286.3; -.
NP_001002235.1; -.
NP_001002236.1; -.
NP_001121172.1; -.
NP_001121173.1; -.
NP_001121174.1; -.
NP_001121175.1; -.
NP_001121176.1; -.
NP_001121177.1; -.
NP_001121178.1; -.
NP_001121179.1; -.

UniGene

Hs.525557

3D structure databases

PDB

1ATU; X-ray; 2.70 A; A=45-418.	[ExPASy / RCSB / EBI]
1D5S; X-ray; 3.00 A; A=44-377, B=378-418.	[ExPASy / RCSB / EBI]
1EZX; X-ray; 2.60 A; A=48-382, B=383-418.	[ExPASy / RCSB / EBI]
1HP7; X-ray; 2.10 A; A=25-418.	[ExPASy / RCSB / EBI]
1IZ2; X-ray; 2.20 A; A=25-418.	[ExPASy / RCSB / EBI]
1KCT; X-ray; 3.46 A; A=25-418.	[ExPASy / RCSB / EBI]
1OO8; X-ray; 2.65 A; A=26-418.	[ExPASy / RCSB / EBI]
1OPH; X-ray; 2.30 A; A=26-418.	[ExPASy / RCSB / EBI]
1PSI; X-ray; 2.92 A; A=26-418.	[ExPASy / RCSB / EBI]
1QLP; X-ray; 2.00 A; A=26-418.	[ExPASy / RCSB / EBI]
1QMB; X-ray; 2.60 A; A=49-376, B=377-418.	[ExPASy / RCSB / EBI]
2D26; X-ray; 3.30 A; A=26-382, B=383-418.	[ExPASy / RCSB / EBI]
2QUG; X-ray; 2.00 A; A=25-418.	[ExPASy / RCSB / EBI]
3CWL; X-ray; 2.44 A; A=25-418.	[ExPASy / RCSB / EBI]
3CWM; X-ray; 2.51 A; A=25-418.	[ExPASy / RCSB / EBI]
3DRM; X-ray; 2.20 A; A=26-418.	[ExPASy / RCSB / EBI]
3DRU; X-ray; 3.20 A; A/B/C=26-418.	[ExPASy / RCSB / EBI]
7API; X-ray; 3.00 A; A=36-382, B=383-418.	[ExPASy / RCSB / EBI]
8API; X-ray; 3.10 A; A=36-382, B=383-418.	[ExPASy / RCSB / EBI]
9API; X-ray; 3.00 A; A=36-382, B=383-418.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1ATU; -.
1D5S; -.
1EZX; -.
1HP7; -.
1IZ2; -.
1KCT; -.
1OO8; -.
1OPH; -.
1PSI; -.
1QLP; -.
1QMB; -.
2D26; -.
2QUG; -.
3CWL; -.
3CWM; -.
3DRM; -.
3DRU; -.
7API; -.
8API; -.
9API; -.

ModBase

P01009.

Protein-protein interaction databases

IntAct

P01009; 6.

Protein family/group databases

MEROPS

I04.001; -.

PTM databases

GlycoSuiteDB

P01009; -.

PhosphoSite

P01009; -.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3apathway; FOXA1 transcription factor network.

Reactome

REACT_604; Hemostasis.

2D gel databases

P01009; -.

P01009; -.

P01009; -.

P01009; -.

P01009; -.

IPI00553177; -.
P01009; -.

Siena-2DPAGE

P01009; -.

Organism-specific databases

GC14M093914; -.

HIX0011929; -.

HGNC:8941; SERPINA1.

CAB013211; -.
CAB016648; -.
HPA000927; -.
HPA001292; -.

MIM

107400; gene+phenotype. [NCBI / EBI]

Orphanet

60; Alpha-1 antitrypsin deficiency.

PharmGKB

PA35509; -.

Gene expression databases

ArrayExpress

P01009; -.

Bgee

P01009; -.

GermOnline

ENSG00000197249; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (inferred from mutant phenotype from UniProtKB).
GO:0005730;	Cellular component: nucleolus (inferred from direct assay from HPA).
GO:0031093;	Cellular component: platelet alpha granule lumen (inferred from experiment from Reactome).
GO:0005578;	Cellular component: proteinaceous extracellular matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0008233;	Molecular function: peptidase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0002020;	Molecular function: protease binding (inferred from physical interaction from UniProtKB).
GO:0004867;	Molecular function: serine-type endopeptidase inhibitor activity (non-traceable author statement from UniProtKB).
GO:0006953;	Biological process: acute-phase response (inferred from electronic annotation from UniProtKB-KW).
GO:0007596;	Biological process: blood coagulation (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000215; Protease_inhib_I4_serpin.
Graphical view of domain structure.

PANTHER

PTHR11461; Prot_inh_serpin; 1.

Pfam

PF00079; Serpin; 1.
Pfam graphical view of domain structure.

SMART

SM00093; SERPIN; 1.
SMART graphical view of domain structure.

PROSITE

PS00284; SERPIN; 1.

Other

SWISS-3DIMAGE

P01009.

Proteomic databases

PRIDE

P01009; -.

Genome annotation databases

Ensembl

ENSG00000197249; Homo sapiens. [Contig view]

GeneID

5265; -.

KEGG

hsa:5265; -.

Phylogenomic databases

HOGENOM

P01009; -.

HOVERGEN

P01009; -.

OMA

P01009; AGAMFLE.

Other

DrugBank

DB00058; Alpha-1-proteinase inhibitor.

NextBio

20336; -.

PMAP-CutDB

P01009; -.

SOURCE

SERPINA1; Homo sapiens.

ProtoNet

P01009.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acute phase; Alternative splicing; Blood coagulation; Direct protein sequencing; Disease mutation; Extracellular matrix; Glycoprotein; Hydrolase; Polymorphism; Protease; Protease inhibitor; Secreted; Serine protease inhibitor; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`
`CHAIN`	`25 418`	`394`	`Alpha-1-antitrypsin.`	`PRO_0000032377`
`PEPTIDE`	`375 418`	`44`	`Short peptide from AAT.`	`PRO_0000364030`
`REGION`	`368 392`	`25`	`RCL.`
`BINDING`	`256 256`		`Cysteine (covalent).`
`SITE`	`382 383`	`2`	`Reactive bond.`
`CARBOHYD`	`70 70`		`N-linked (GlcNAc...).`
`CARBOHYD`	`107 107`		`N-linked (GlcNAc...).`
`CARBOHYD`	`271 271`		`N-linked (GlcNAc...).`
`VAR_SEQ`	`307 418`		`Missing (in isoform 3).`	`VSP_028890`
`VAR_SEQ`	`356 418`		`AVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFV` `FLMIEQNTKSPLFMGKVVNPTQK -> VRSP (in isoform 2).`	`VSP_028889`
`VARIANT`	`4 4`	`1`	`S -> L (in Z-Wrexham).`	`VAR_006978`
`VARIANT`	`26 26`	`1`	`D -> A (in V-Munich).`	`VAR_006979`
`VARIANT`	`37 37`	`1`	`T -> A (in dbSNP:rs11558262 [NCBI]).`	`VAR_051938`
`VARIANT`	`58 58`	`1`	`A -> T (in M5-Karlsruhe).`	`VAR_006980 [3D]`
`VARIANT`	`63 63`	`1`	`R -> C (in I).`	`VAR_006981 [3D]`
`VARIANT`	`65 65`	`1`	`L -> P (in M-Procida).`	`VAR_006982 [3D]`
`VARIANT`	`69 69`	`1`	`S -> F (in M6-Bonn).`	`VAR_006983 [3D]`
`VARIANT`	`75 75`	`1`	`Missing (in M-Malton, M-Nichinan and M-Palermo; associated with very low serum levels of AAT).`	`VAR_006984`
`VARIANT`	`77 77`	`1`	`S -> F (in S-Iiyama).`	`VAR_006985 [3D]`
`VARIANT`	`84 84`	`1`	`A -> T (in M6-Passau).`	`VAR_006986 [3D]`
`VARIANT`	`91 91`	`1`	`G -> E (in M-Mineral springs; causes reduced AAT secretion).`	`VAR_006987 [3D]`
`VARIANT`	`92 92`	`1`	`T -> I (in QO-Lisbon; deficient AAT with very low serum levels).`	`VAR_006988 [3D]`
`VARIANT`	`109 109`	`1`	`T -> M (in Z-Bristol; deficient AA; disrupts the N-glycosylation site N-107).`	`VAR_011620 [3D]`
`VARIANT`	`112 112`	`1`	`P -> T (in M5-Berlin).`	`VAR_006989 [3D]`
`VARIANT`	`116 116`	`1`	`I -> N (in QO-Ludwigshafen).`	`VAR_006990 [3D]`
`VARIANT`	`125 125`	`1`	`R -> H (in M2; associated with D-400; dbSNP:rs709932 [NCBI]).`	`VAR_006991 [3D]`
`VARIANT`	`139 139`	`1`	`G -> S (in QO-Newport; dbSNP:rs11558261 [NCBI]).`	`VAR_006992 [3D]`
`VARIANT`	`172 172`	`1`	`G -> R (in V and M-Nichinan).`	`VAR_006993 [3D]`
`VARIANT`	`172 172`	`1`	`G -> W (in M2-Obernburg).`	`VAR_006994 [3D]`
`VARIANT`	`180 180`	`1`	`Q -> E (in L-Frankfurt).`	`VAR_006995 [3D]`
`VARIANT`	`190 198`	`9`	`QGKIVDLVK -> GFQNAILVR (in Aberrant form).`	`VAR_036746`
`VARIANT`	`228 228`	`1`	`E -> K (in X).`	`VAR_006996 [3D]`
`VARIANT`	`237 237`	`1`	`V -> A (in M1A and Z; associated with K-366 in Z; dbSNP:rs6647 [NCBI]).`	`VAR_006997 [3D]`
`VARIANT`	`247 247`	`1`	`R -> C (in F).`	`VAR_006998 [3D]`
`VARIANT`	`280 280`	`1`	`D -> V (in P-Duarte/P-Cardiff/P-Lowell; associated with H-415 in Y-Barcelona).`	`VAR_006999 [3D]`
`VARIANT`	`288 288`	`1`	`E -> V (in S and T; dbSNP:rs17580 [NCBI]).`	`VAR_007000 [3D]`
`VARIANT`	`305 305`	`1`	`Missing (in Basque).`	`VAR_009216`
`VARIANT`	`354 354`	`1`	`S -> F (in S-Munich).`	`VAR_007001 [3D]`
`VARIANT`	`360 360`	`1`	`A -> T (in W-Bethesda; dbSNP:rs1802959 [NCBI]).`	`VAR_007002 [3D]`
`VARIANT`	`365 365`	`1`	`D -> N (in P-St.Albans/P-Donauwoerth).`	`VAR_007003 [3D]`
`VARIANT`	`366 366`	`1`	`E -> K (in Z/Z-Augsburg/Z-Tun; associated with A-237 in Z).`	`VAR_007004 [3D]`
`VARIANT`	`382 382`	`1`	`M -> R (in Pittsburgh; has antithrombin activity).`	`VAR_007005 [3D]`
`VARIANT`	`386 386`	`1`	`P -> H (in Sao Tome).`	`VAR_007006 [3D]`
`VARIANT`	`386 386`	`1`	`P -> T (in L-Offenbach).`	`VAR_007007 [3D]`
`VARIANT`	`387 387`	`1`	`E -> K (in Christchurch).`	`VAR_007008 [3D]`
`VARIANT`	`393 393`	`1`	`P -> L (in M-Heerlen).`	`VAR_007009 [3D]`
`VARIANT`	`400 400`	`1`	`E -> D (in M2 and M3; associated with H-125 in M2; dbSNP:rs1303 [NCBI]).`	`VAR_007010 [3D]`
`VARIANT`	`415 415`	`1`	`P -> H (in Y-Barcelona; associated with V-280).`	`VAR_007011 [3D]`
`MUTAGEN`	`382 382`		`M->V: Oxidation-resistant inhibitor of therapeutic importance.`
`CONFLICT`	`12 12`		`Missing (in Ref. 4; AAA51546).`
`CONFLICT`	`23 23`		`L -> P (in Ref. 11; BAG38005).`
`CONFLICT`	`26 26`		`D -> H (in Ref. 18; AA sequence).`
`CONFLICT`	`39 39`		`H -> L (in Ref. 18; AA sequence).`
`CONFLICT`	`61 61`		`L -> P (in Ref. 9; AAF29581).`
`CONFLICT`	`96 96`		`T -> A (in Ref. 7; ABG73380).`
`CONFLICT`	`139 140`		`GN -> DG (in Ref. 1; AAB59375).`
`CONFLICT`	`174 174`		`T -> H (in Ref. 4; AAA51546).`
`CONFLICT`	`229 229`		`E -> D (in Ref. 4; AAA51546).`
`CONFLICT`	`273 273`		`T -> N (in Ref. 1; AAB59375).`
`CONFLICT`	`280 280`		`D -> G (in Ref. 7; ABG73380).`
`CONFLICT`	`326 326`		`V -> I (in Ref. 3; CAA25838).`
`CONFLICT`	`410 410`		`G -> L (in Ref. 24; AA sequence).`
`CONFLICT`	`414 414`		`N -> S (in Ref. 24; AA sequence).`
`TURN`	`48 50`	`3`
`HELIX`	`51 68`	`18`
`STRAND`	`70 72`	`3`
`STRAND`	`74 76`	`3`
`HELIX`	`78 89`	`12`
`HELIX`	`94 103`	`10`
`TURN`	`108 110`	`3`
`HELIX`	`113 127`	`15`
`STRAND`	`135 145`	`11`
`HELIX`	`152 160`	`9`
`STRAND`	`165 169`	`5`
`HELIX`	`174 188`	`15`
`TURN`	`189 191`	`3`
`STRAND`	`206 215`	`10`
`STRAND`	`218 220`	`3`
`HELIX`	`224 226`	`3`
`STRAND`	`228 237`	`10`
`STRAND`	`239 256`	`18`
`TURN`	`257 260`	`4`
`STRAND`	`261 268`	`8`
`TURN`	`269 271`	`3`
`STRAND`	`272 279`	`8`
`HELIX`	`284 290`	`7`
`HELIX`	`293 299`	`7`
`STRAND`	`306 313`	`8`
`STRAND`	`315 322`	`8`
`HELIX`	`323 329`	`7`
`HELIX`	`334 336`	`3`
`TURN`	`343 345`	`3`
`STRAND`	`346 349`	`4`
`STRAND`	`355 364`	`10`
`STRAND`	`387 389`	`3`
`STRAND`	`394 400`	`7`
`TURN`	`401 403`	`3`
`STRAND`	`406 413`	`8`

Sequence information

Length: 418 AA [This is the length of the unprocessed precursor]

Molecular weight: 46737 Da [This is the MW of the unprocessed precursor]

CRC64: 7016555F273B7F16 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPSSVSWGIL LLAGLCCLVP VSLAEDPQGD AAQKTDTSHH DQDHPTFNKI TPNLAEFAFS 

        70         80         90        100        110        120 
LYRQLAHQSN STNIFFSPVS IATAFAMLSL GTKADTHDEI LEGLNFNLTE IPEAQIHEGF 

       130        140        150        160        170        180 
QELLRTLNQP DSQLQLTTGN GLFLSEGLKL VDKFLEDVKK LYHSEAFTVN FGDTEEAKKQ 

       190        200        210        220        230        240 
INDYVEKGTQ GKIVDLVKEL DRDTVFALVN YIFFKGKWER PFEVKDTEEE DFHVDQVTTV 

       250        260        270        280        290        300 
KVPMMKRLGM FNIQHCKKLS SWVLLMKYLG NATAIFFLPD EGKLQHLENE LTHDIITKFL 

       310        320        330        340        350        360 
ENEDRRSASL HLPKLSITGT YDLKSVLGQL GITKVFSNGA DLSGVTEEAP LKLSKAVHKA 

       370        380        390        400        410 
VLTIDEKGTE AAGAMFLEAI PMSIPPEVKF NKPFVFLMIE QNTKSPLFMG KVVNPTQK

P01009 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools