[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Liver; DOI=10.1021/bi00291a001; PubMed=6606438 [NCBI, ExPASy, EBI, Israel, Japan] Chandra T., Stackhouse R., Kidd V.J., Robson K.J.H., Woo S.L.C.; "Sequence homology between human alpha 1-antichymotrypsin, alpha 1-antitrypsin, and antithrombin III."; Biochemistry 22:5055-5061(1983).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN COPD, AND VARIANTS BOCHUM-1 PRO-78 AND BONN-1 ALA-252. DOI=10.1006/geno.1993.1396; PubMed=8244391 [NCBI, ExPASy, EBI, Israel, Japan] Poller W., Faber J.-P., Weidinger S., Tief K., Scholz S., Fischer M., Olek K., Kirchgesser M., Heidtmann H.-H.; "A leucine-to-proline substitution causes a defective alpha 1-antichymotrypsin allele associated with familial obstructive lung disease."; Genomics 17:740-743(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-9. Kim J.W.; "Identification of a human cell growth inhibiting gene."; Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-9. TISSUE=Urinary bladder; 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).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-9. TISSUE=Brain; Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.; Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS THR-9 AND ARG-267. TISSUE=Brain, Liver, and Skin; 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).
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-46, AND TISSUE SPECIFICITY. TISSUE=Liver; DOI=10.1016/0092-8674(88)90462-X; PubMed=3257719 [NCBI, ExPASy, EBI, Israel, Japan] Abraham C.R., Selkoe D.J., Potter H.; "Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease."; Cell 52:487-501(1988).
[8]	NUCLEOTIDE SEQUENCE [MRNA] OF 17-423 (ISOFORM 1), AND TISSUE SPECIFICITY. TISSUE=Hippocampus; DOI=10.1074/jbc.274.3.1821; PubMed=9880565 [NCBI, ExPASy, EBI, Israel, Japan] Hwang S.-R., Steineckert B., Kohn A., Palkovits M., Hook V.Y.H.; "Molecular studies define the primary structure of alpha1-antichymotrypsin (ACT) protease inhibitor in Alzheimer's disease brains. Comparison of act in hippocampus and liver."; J. Biol. Chem. 274:1821-1827(1999).
[9]	NUCLEOTIDE SEQUENCE [MRNA] OF 22-86 AND 130-423 (ISOFORM 1). Rubin H.; Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases.
[10]	PROTEIN SEQUENCE OF 24-34. DOI=10.1016/0167-4838(89)90139-8; PubMed=2787670 [NCBI, ExPASy, EBI, Israel, Japan] Lindmark B., Hilja H., Alan R., Eriksson S.; "The microheterogeneity of desialylated alpha 1-antichymotrypsin: the occurrence of two amino-terminal isoforms, one lacking a His-Pro dipeptide."; Biochim. Biophys. Acta 997:90-95(1989).
[11]	NUCLEOTIDE SEQUENCE [MRNA] OF 36-45. PubMed=7521171 [NCBI, ExPASy, EBI, Israel, Japan] Korzus E., Luisetti M., Travis J.; "Interactions of alpha-1-antichymotrypsin, alpha-1-proteinase inhibitor, and alpha-2-macroglobulin with the fungal enzyme, seaprose."; Biol. Chem. Hoppe-Seyler 375:335-341(1994).
[12]	PROTEIN SEQUENCE OF 41-60. DOI=10.1016/0006-291X(83)90325-X; PubMed=6687683 [NCBI, ExPASy, EBI, Israel, Japan] Morii M., Travis J.; "Structural alterations in alpha 1-antichymotrypsin from normal and acute phase human plasma."; Biochem. Biophys. Res. Commun. 111:438-443(1983).
[13]	PROTEIN SEQUENCE OF 48-68 (ISOFORMS 1/2). DOI=10.1002/(SICI)1097-0215(19960529)66:5<636::AID-IJC10>3.0.CO;2-2; PubMed=8647626 [NCBI, ExPASy, EBI, Israel, Japan] Pinczower G.D., Williams R.P.W., Gianello R.D., Robinson H.C., Preston B.N., Linnane A.W.; "Characterisation of the tumour-associated carbohydrate epitope recognised by monoclonal antibody 4D3."; Int. J. Cancer 66:636-644(1996).
[14]	NUCLEOTIDE SEQUENCE [MRNA] OF 87-129 (ISOFORMS 1/2), AND FUNCTION. TISSUE=Liver; PubMed=2404007 [NCBI, ExPASy, EBI, Israel, Japan] Rubin H., Wang Z., Nickbarg E.B., McLarney S., Naidoo N., Schoenberger O.L., Johnson J.L., Cooperman B.S.; "Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins."; J. Biol. Chem. 265:1199-1207(1990).
[15]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-423. DOI=10.1038/311175a0; PubMed=6547997 [NCBI, ExPASy, EBI, Israel, Japan] Hill R.E., Shaw P.H., Boyd P.A., Baumann H., Hastie N.D.; "Plasma protease inhibitors in mouse and man: divergence within the reactive centre regions."; Nature 311:175-177(1984).
[16]	ACTIVE SITE. PubMed=6556193 [NCBI, ExPASy, EBI, Israel, Japan] Morii M., Travis J.; "Amino acid sequence at the reactive site of human alpha 1-antichymotrypsin."; J. Biol. Chem. 258:12749-12752(1983).
[17]	GLYCOSYLATION AT ASN-93 AND ASN-106. 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).
[18]	INTERACTION WITH DNAJC1. DOI=10.1074/jbc.M310903200; PubMed=14668352 [NCBI, ExPASy, EBI, Israel, Japan] Kroczynska B., Evangelista C.M., Samant S.S., Elguindi E.C., Blond S.Y.; "The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity."; J. Biol. Chem. 279:11432-11443(2004).
[19]	REGION RCL. DOI=10.1007/s00239-004-2640-9; PubMed=15638460 [NCBI, ExPASy, EBI, Israel, Japan] Horvath A.J., Forsyth S.L., Coughlin P.B.; "Expression patterns of murine antichymotrypsin-like genes reflect evolutionary divergence at the Serpina3 locus."; J. Mol. Evol. 59:488-497(2004).
[20]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93, 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).
[21]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-93; ASN-106; ASN-127; ASN-186 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).
[22]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93; ASN-106; ASN-127 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).
[23]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-423. DOI=10.1016/0022-2836(91)90704-A; PubMed=2016749 [NCBI, ExPASy, EBI, Israel, Japan] Baumann U., Huber R., Bode W., Grosse D., Lesjak M., Laurell C.-B.; "Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7-A resolution and its comparison with other serpins."; J. Mol. Biol. 218:595-606(1991).
[24]	X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370 AND ARG-372. DOI=10.1038/nsb1096-888; PubMed=8836107 [NCBI, ExPASy, EBI, Israel, Japan] Lukacs C.M., Zhong J.Q., Plotnick M.I., Rubin H., Cooperman B.S., Christianson D.W.; "Arginine substitutions in the hinge region of antichymotrypsin affect serpin beta-sheet rearrangement."; Nat. Struct. Biol. 3:888-893(1996).
[25]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370; ARG-372 AND ARG-374. DOI=10.1021/bi972359e; PubMed=9521649 [NCBI, ExPASy, EBI, Israel, Japan] Lukacs C.M., Rubin H., Christianson D.W.; "Engineering an anion-binding cavity in antichymotrypsin modulates the 'spring-loaded' serpin-protease interaction."; Biochemistry 37:3297-3304(1998).
[26]	X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 26-423. DOI=10.1073/pnas.97.1.67; PubMed=10618372 [NCBI, ExPASy, EBI, Israel, Japan] Gooptu B., Hazes B., Chang W.-S.W., Dafforn T.R., Carrell R.W., Read R.J., Lomas D.A.; "Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease."; Proc. Natl. Acad. Sci. U.S.A. 97:67-72(2000).
[27]	VARIANT ISEHARA-1 VAL-401. DOI=10.1016/0014-5793(92)80590-D; PubMed=1618300 [NCBI, ExPASy, EBI, Israel, Japan] Tsuda M., Sei Y., Yamamura M., Yamamoto M., Shinohara Y.; "Detection of a new mutant alpha-1-antichymotrypsin in patients with occlusive-cerebrovascular disease."; FEBS Lett. 304:66-68(1992).
[28]	VARIANT BONN-1 ALA-252. DOI=10.1016/0140-6736(92)91301-N; PubMed=1351206 [NCBI, ExPASy, EBI, Israel, Japan] Poller W., Faber J.-P., Scholz S., Weindinger S., Bartholome K., Olek K., Eriksson S.; "Mis-sense mutation of alpha 1-antichymotrypsin gene associated with chronic lung disease."; Lancet 339:1538-1538(1992).
[29]	VARIANT VAL-401. DOI=10.1007/s100380170125; PubMed=11289720 [NCBI, ExPASy, EBI, Israel, Japan] Tachikawa H., Tsuda M., Onoe K., Ueno M., Takagi S., Shinohara Y.; "Alpha-1-antichymotrypsin gene A1252G variant (ACT Isehara-1) is associated with a lacunar type of ischemic cerebrovascular disease."; J. Hum. Genet. 46:45-47(2001).

Comments

FUNCTION: Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2.
SUBUNIT: Interacts with DNAJC1.
SUBCELLULAR LOCATION: Secreted.

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

Name	1
Isoform ID	P01011-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P01011-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_014227, VSP_014228.

Name	3
Isoform ID	P01011-3
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_014225, VSP_014226.

TISSUE SPECIFICITY: Plasma. Synthesized in the liver. Like the related alpha-1-antitrypsin, its concentration increases in the acute phase of inflammation or infection. Found in the myloid plaques from the hippocampus of Alzheimer's disease brains.
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.
DISEASE: Defects in SERPINA3 may be a cause of chronic obstructive pulmonary disease (COPD) [MIM:107280].
MISCELLANEOUS: Alpha-1-antichymotrypsin can bind DNA.
SIMILARITY: Belongs to the serpin family.
CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
SEQUENCE CAUTION:
- Sequence=AAA51543.1; Type=Frameshift; Positions=101, 106, 111, 117, 123, 129, 421;
- Sequence=AAT08029.1; Type=Erroneous initiation; Note=Translation N-terminally shortened
- Sequence=AAT08029.1; Type=Frameshift; Positions=4;
WEB RESOURCE: Name=Wikipedia; Note=Alpha-1 antichymotrypsin entry; URL="http://en.wikipedia.org/wiki/Alpha_1-antichymotrypsin";.

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

K01500; AAA51543.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X68733; CAA48671.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X68734; CAA48671.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X68735; CAA48671.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X68736; CAA48671.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X68737; CAA48671.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY513275; AAT08028.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY513276; AAT08029.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK123091; BAG53869.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB209060; BAD92297.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003559; AAH03559.3; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010530; AAH10530.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013189; AAH13189.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC034554; AAH34554.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC070265; AAH70265.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18906; AAA51559.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF089747; AAD08810.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J05176; AAA51560.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X00947; CAA25459.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00550991; -.
IPI00607870; -.
IPI00847635; -.

PIR

A90475; ITHUC.
S62374; S62374.

RefSeq

NP_001076.2; -.

UniGene

Hs.534293

3D structure databases

PDB

1AS4; X-ray; 2.10 A; A=43-383, B=387-423.	[ExPASy / RCSB / EBI]
1QMN; X-ray; 2.27 A; A=26-423.	[ExPASy / RCSB / EBI]
2ACH; X-ray; 2.70 A; A=24-383, B=384-423.	[ExPASy / RCSB / EBI]
3CAA; X-ray; 2.40 A; A=43-383, B=387-423.	[ExPASy / RCSB / EBI]
4CAA; X-ray; 2.90 A; A=43-383, B=387-423.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AS4; -.
1QMN; -.
2ACH; -.
3CAA; -.
4CAA; -.

ModBase

P01011.

Protein-protein interaction databases

IntAct

P01011; 1.

Protein family/group databases

MEROPS

I04.002; -.

PTM databases

GlycoSuiteDB

P01011; -.

PhosphoSite

P01011; -.

2D gel databases

SWISS-2DPAGE

P01011; -.

DOSAC-COBS-2DPAGE

P01011; -.

Siena-2DPAGE

P01011; -.

Organism-specific databases

GeneCards

GC14P094148; -.

H-InvDB

HIX0011931; -.
HIX0079611; -.

HGNC:16; SERPINA3.

CAB016647; -.
HPA002560; -.

MIM

107280; gene. [NCBI / EBI]

PharmGKB

PA35020; -.

Gene expression databases

ArrayExpress

P01011; -.

Bgee

P01011; -.

GermOnline

ENSG00000196136; Homo sapiens.

Ontologies

GO:0005576;	Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0005634;	Cellular component: nucleus (traceable author statement from UniProtKB).
GO:0003677;	Molecular function: DNA binding (traceable author statement from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004867;	Molecular function: serine-type endopeptidase inhibitor activity (traceable author statement from UniProtKB).
GO:0006953;	Biological process: acute-phase response (inferred from electronic annotation from UniProtKB-KW).
GO:0019216;	Biological process: regulation of lipid metabolic process (non-traceable author statement from UniProtKB).
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.

Proteomic databases

PRIDE

P01011; -.

Genome annotation databases

Ensembl

ENSG00000196136; Homo sapiens. [Contig view]

GeneID

12; -.

KEGG

hsa:12; -.

Phylogenomic databases

HOVERGEN

P01011; -.

Other

NextBio

23; -.

PMAP-CutDB

P01011; -.

SOURCE

SERPINA3; Homo sapiens.

ProtoNet

P01011.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`
`CHAIN`	`24 423`	`400`	`Alpha-1-antichymotrypsin.`	`PRO_0000032411`
`CHAIN`	`26 423`	`398`	`Alpha-1-antichymotrypsin His-Pro-less.`	`PRO_0000032412`
`DNA_BIND`	`235 237`	`3`
`REGION`	`369 394`	`26`	`RCL.`
`SITE`	`383 384`	`2`	`Reactive bond.`
`CARBOHYD`	`33 33`		`N-linked (GlcNAc...).`
`CARBOHYD`	`93 93`		`N-linked (GlcNAc...).`
`CARBOHYD`	`106 106`		`N-linked (GlcNAc...).`
`CARBOHYD`	`127 127`		`N-linked (GlcNAc...).`
`CARBOHYD`	`186 186`		`N-linked (GlcNAc...).`
`CARBOHYD`	`271 271`		`N-linked (GlcNAc...).`
`VAR_SEQ`	`64 95`		`LVLKAPDKNVIFSPLSISTALAFLSLGAHNTT -> SPRWSIRLCLMYLRRAQKHLLPQQSKSPSFLH (in isoform 3).`	`VSP_014225`
`VAR_SEQ`	`96 423`		`Missing (in isoform 3).`	`VSP_014226`
`VAR_SEQ`	`215 216`		`AK -> ER (in isoform 2).`	`VSP_014227`
`VAR_SEQ`	`217 423`		`Missing (in isoform 2).`	`VSP_014228`
`VARIANT`	`9 9`	`1`	`A -> T (in dbSNP:rs4934 [NCBI]).`	`VAR_006973`
`VARIANT`	`78 78`	`1`	`L -> P (in COPD; Bochum-1; dbSNP:rs1800463 [NCBI]).`	`VAR_006974`
`VARIANT`	`167 167`	`1`	`A -> G.`	`VAR_006975`
`VARIANT`	`252 252`	`1`	`P -> A (in COPD; Bonn-1; dbSNP:rs17473 [NCBI]).`	`VAR_006976`
`VARIANT`	`267 267`	`1`	`K -> R (in dbSNP:rs17853314 [NCBI]).`	`VAR_037902`
`VARIANT`	`401 401`	`1`	`M -> V (associated with occlusive-cerebrovascular disease; Isehara-1).`	`VAR_006977 [3D]`
`VARIANT`	`407 407`	`1`	`D -> G (in dbSNP:rs10956 [NCBI]).`	`VAR_011742 [3D]`
`CONFLICT`	`55 55`		`D -> S (in Ref. 12; AA sequence).`
`CONFLICT`	`69 69`		`P -> L (in Ref. 1; AAA51543).`
`CONFLICT`	`101 101`		`K -> R (in Ref. 5; BAD92297).`
`CONFLICT`	`106 106`		`N -> Y (in Ref. 3; AAT08028).`
`CONFLICT`	`198 198`		`D -> N (in Ref. 3; AAT08029).`
`CONFLICT`	`199 199`		`L -> P (in Ref. 1; AAA51543).`
`CONFLICT`	`234 234`		`S -> N (in Ref. 3; AAT08029).`
`CONFLICT`	`339 339`		`S -> G (in Ref. 3; AAT08028).`
`CONFLICT`	`346 346`		`I -> S (in Ref. 3; AAT08028).`
`CONFLICT`	`361 363`		`AVL -> VVS (in Ref. 1; AAA51543).`
`HELIX`	`49 67`	`19`
`STRAND`	`73 75`	`3`
`HELIX`	`77 88`	`12`
`HELIX`	`93 102`	`10`
`TURN`	`107 109`	`3`
`HELIX`	`112 126`	`15`
`STRAND`	`134 144`	`11`
`HELIX`	`151 161`	`11`
`STRAND`	`164 168`	`5`
`HELIX`	`173 187`	`15`
`TURN`	`188 190`	`3`
`STRAND`	`203 219`	`17`
`HELIX`	`223 225`	`3`
`STRAND`	`227 234`	`8`
`STRAND`	`237 256`	`20`
`TURN`	`257 260`	`4`
`STRAND`	`261 279`	`19`
`HELIX`	`284 289`	`6`
`HELIX`	`293 302`	`10`
`STRAND`	`304 314`	`11`
`STRAND`	`316 323`	`8`
`HELIX`	`325 330`	`6`
`HELIX`	`335 337`	`3`
`HELIX`	`344 347`	`4`
`STRAND`	`348 350`	`3`
`STRAND`	`352 365`	`14`
`STRAND`	`367 382`	`16`
`STRAND`	`391 394`	`4`
`STRAND`	`399 405`	`7`
`STRAND`	`412 418`	`7`

Sequence information

Length: 423 AA [This is the length of the unprocessed precursor]

Molecular weight: 47651 Da [This is the MW of the unprocessed precursor]

CRC64: B002F946C86A8951 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MERMLPLLAL GLLAAGFCPA VLCHPNSPLD EENLTQENQD RGTHVDLGLA SANVDFAFSL 

        70         80         90        100        110        120 
YKQLVLKAPD KNVIFSPLSI STALAFLSLG AHNTTLTEIL KGLKFNLTET SEAEIHQSFQ 

       130        140        150        160        170        180 
HLLRTLNQSS DELQLSMGNA MFVKEQLSLL DRFTEDAKRL YGSEAFATDF QDSAAAKKLI 

       190        200        210        220        230        240 
NDYVKNGTRG KITDLIKDLD SQTMMVLVNY IFFKAKWEMP FDPQDTHQSR FYLSKKKWVM 

       250        260        270        280        290        300 
VPMMSLHHLT IPYFRDEELS CTVVELKYTG NASALFILPD QDKMEEVEAM LLPETLKRWR 

       310        320        330        340        350        360 
DSLEFREIGE LYLPKFSISR DYNLNDILLQ LGIEEAFTSK ADLSGITGAR NLAVSQVVHK 

       370        380        390        400        410        420 
AVLDVFEEGT EASAATAVKI TLLSALVETR TIVRFNRPFL MIIVPTDTQN IFFMSKVTNP 


KQA

P01011 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