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UniProtKB/Swiss-Prot entry P02771


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FETA_HUMAN
Primary accession number P02771
Secondary accession number B2RBU3
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 103)
Name and origin of the protein
Protein name Alpha-fetoprotein [Precursor]
Synonyms Alpha-1-fetoprotein
Alpha-fetoglobulin
Gene name
Name: AFP
Synonyms: HPAFP
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.80.15.4604; PubMed=6192439 [NCBI, ExPASy, EBI, Israel, Japan]
Morinaga T., Sakai M., Wegmann T.G., Tamaoki T.;
"Primary structures of human alpha-fetoprotein and its mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 80:4604-4608(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1021/bi00379a020; PubMed=2436661 [NCBI, ExPASy, EBI, Israel, Japan]
Gibbs P.E.M., Zielinski R., Boyd C., Dugaiczyk A.;
"Structure, polymorphism, and novel repeated DNA elements revealed by a complete sequence of the human alpha-fetoprotein gene.";
Biochemistry 26:1332-1343(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-570.
TISSUE=Heart;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
DOI=10.1093/hmg/2.4.379; PubMed=7684942 [NCBI, ExPASy, EBI, Israel, Japan]
McVey J.H., Michaelides K., Hansen L.P., Ferguson-Smith M., Tilghman S., Krumlauf R., Tuddenham E.G.D.;
"A G-->A substitution in an HNF I binding site in the human alpha-fetoprotein gene is associated with hereditary persistence of alpha-fetoprotein (HPAFP).";
Hum. Mol. Genet. 2:379-384(1993).
[6]
PROTEIN SEQUENCE OF 311-332; 348-372 AND 422-437, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 429-556.
DOI=10.1016/0378-1119(82)90210-4; PubMed=6187626 [NCBI, ExPASy, EBI, Israel, Japan]
Beattie W.G., Dugaiczyk A.;
"Structure and evolution of human alpha-fetoprotein deduced from partial sequence of cloned cDNA.";
Gene 20:415-422(1982).
[8]
PARTIAL PROTEIN SEQUENCE OF 19-609.
DOI=10.1021/bi00234a032; PubMed=1709810 [NCBI, ExPASy, EBI, Israel, Japan]
Pucci P., Siciliano R., Malorni A., Marino G., Tecce M.F., Ceccarini C., Terrana B.;
"Human alpha-fetoprotein primary structure: a mass spectrometric study.";
Biochemistry 30:5061-5066(1991).
[9]
PRELIMINARY PROTEIN SEQUENCE OF 19-35.
DOI=10.1016/0005-2795(77)90198-2; PubMed=70228 [NCBI, ExPASy, EBI, Israel, Japan]
Yachnin S., Hsu R., Heinrikson R.L., Miller J.B.;
"Studies on human alpha-fetoprotein. Isolation and characterization of monomeric and polymeric forms and amino-terminal sequence analysis.";
Biochim. Biophys. Acta 493:418-428(1977).
[10]
PRELIMINARY PROTEIN SEQUENCE OF 19-38.
PubMed=71198 [NCBI, ExPASy, EBI, Israel, Japan]
Aoyagi Y., Ikenaka T., Ichida F.;
"Comparative chemical structures of human alpha-fetoproteins from fetal serum and from ascites fluid of a patient with hepatoma.";
Cancer Res. 37:3663-3667(1977).
[11]
PRELIMINARY PROTEIN SEQUENCE OF 19-39.
PubMed=4138095 [NCBI, ExPASy, EBI, Israel, Japan]
Ruoslahti E., Pihko H., Vaheri A., Seppala M., Virolainen M., Konttinen A.;
"Alpha fetoprotein: structure and expression in man and inbred mouse strains under normal conditions and liver injury.";
Johns Hopkins Med. J. Suppl. 3:249-255(1974).
[12]
GENE STRUCTURE.
PubMed=2580830 [NCBI, ExPASy, EBI, Israel, Japan]
Sakai M., Morinaga T., Urano Y., Watanabe K., Wegmann T.G., Tamaoki T.;
"The human alpha-fetoprotein gene. Sequence organization and the 5' flanking region.";
J. Biol. Chem. 260:5055-5060(1985).
[13]
METAL-BINDING.
PubMed=80265 [NCBI, ExPASy, EBI, Israel, Japan]
Aoyagi Y., Ikenaka T., Ichida F.;
"Copper(II)-binding ability of human alpha-fetoprotein.";
Cancer Res. 38:3483-3486(1978).
[14]
BILIRUBIN-BINDING.
PubMed=89900 [NCBI, ExPASy, EBI, Israel, Japan]
Aoyagi Y., Ikenaka T., Ichida F.;
"Alpha-fetoprotein as a carrier protein in plasma and its bilirubin-binding ability.";
Cancer Res. 39:3571-3574(1979).
[15]
SULFATION.
DOI=10.1073/pnas.82.21.7160; PubMed=2414772 [NCBI, ExPASy, EBI, Israel, Japan]
Liu M.C., Yu S., Sy J., Redman C.M., Lipmann F.;
"Tyrosine sulfation of proteins from the human hepatoma cell line HepG2.";
Proc. Natl. Acad. Sci. U.S.A. 82:7160-7164(1985).
Comments
  • FUNCTION: Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin. Only a small percentage (less than 2%) of the human AFP shows estrogen-binding properties.
  • SUBUNIT: Dimeric and trimeric forms have been found in addition to the monomeric form.
  • SUBCELLULAR LOCATION: Secreted.
  • TISSUE SPECIFICITY: Plasma. Synthesized by the fetal liver and yolk sac.
  • DEVELOPMENTAL STAGE: Occurs in the plasma of fetuses more than 4 weeks old, reaches the highest levels during the 12th-16th week of gestation, and drops to trace amounts after birth. The serum level in adults is usually less than 40 ng/ml. AFP occurs also at high levels in the plasma and ascitic fluid of adults with hepatoma.
  • PTM: Independent studies suggest heterogeneity of the N-terminal sequence of the mature protein and of the cleavage site of the signal sequence.
  • PTM: Sulfated.
  • SIMILARITY: Belongs to the ALB/AFP/VDB family.
  • SIMILARITY: Contains 3 albumin domains.
  • WEB RESOURCE: Name=Wikipedia; Note=Alpha-fetoprotein entry; URL="http://en.wikipedia.org/wiki/Alpha-fetoprotein";.
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
M10949; AAA51674.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M10950; AAA51675.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V01514; CAA24758.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16110; AAB58754.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK314817; BAG37340.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027881; AAH27881.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z19532; CAA79592.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00022443; -.
PIR A26624; FPHU.
RefSeq NP_001125.1; -.
UniGene Hs.518808
3D structure databases
HSSP P02768; 1E7B. [HSSP ENTRY / PDB]
ModBase P02771.
Protein-protein interaction databases
IntAct P02771; 2.
PTM databases
GlycoSuiteDB P02771; -.
PhosphoSite P02771; -.
Enzyme and pathway databases
Pathway_Interaction_DB hnf3bpathway; FOXA2 and FOXA3 transcription factor networks.
2D gel databases
Siena-2DPAGE P02771; -.
Organism-specific databases
GeneCards GC04P074541; -.
H-InvDB HIX0004279; -.
HGNC HGNC:317; AFP.
GenAtlas AFP.
HPA HPA010607; -.
MIM 104150; gene+phenotype. [NCBI / EBI]
Orphanet 168612; Congenital deficiency in alpha-fetoprotein.
168615; Hereditary persistence of alpha-fetoprotein.
PharmGKB PA24614; -.
Gene expression databases
ArrayExpress P02771; -.
Bgee P02771; -.
CleanEx HS_AFP; -.
GermOnline ENSG00000081051; Homo sapiens.
Ontologies
GO
GO:0005507; Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016151; Molecular function: nickel ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006810; Biological process: transport (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001703; Alpha-fetoprotein.
IPR000264; Serum_albumin.
IPR014760; Serum_albumin_N.
Graphical view of domain structure.
Pfam PF00273; Serum_albumin; 3.
Pfam graphical view of domain structure.
PRINTS PR00803; AFETOPROTEIN.
PR00802; SERUMALBUMIN.
ProDom PD002486; Serum_albumin; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00103; ALBUMIN; 3.
SMART graphical view of domain structure.
PROSITE PS00212; ALBUMIN_1; 2.
PS51438; ALBUMIN_2; 3.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P02771; -.
PRIDE P02771; -.
Genome annotation databases
Ensembl ENSG00000081051; Homo sapiens. [Contig view]
GeneID 174; -.
KEGG hsa:174; -.
Phylogenomic databases
HOGENOM P02771; -.
HOVERGEN P02771; -.
OMA P02771; FHKDLCQ.
Other
NextBio 698; -.
SOURCE AFP; Homo sapiens.
ProtoNet P02771.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Copper; Direct protein sequencing; Disulfide bond; Glycoprotein; Metal-binding; Nickel; Polymorphism; Repeat; Secreted; Signal; Sulfation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
CHAIN   19   609  591     Alpha-fetoprotein. PRO_0000001097
DOMAIN   19   210  192     Albumin 1. 
DOMAIN   211   402  192     Albumin 2. 
DOMAIN   403   601  199     Albumin 3. 
METAL   22    22        Copper or nickel. 
CARBOHYD   251   251        N-linked (GlcNAc...) [GlycoSuiteDB]. CAR_000070
DISULFID   99   114         
DISULFID   113   124         
DISULFID   148   193         
DISULFID   192   201         
DISULFID   224   270         
DISULFID   269   277         
DISULFID   289   303         
DISULFID   302   313         
DISULFID   384   393         
DISULFID   416   462         
DISULFID   461   472         
DISULFID   485   501         
DISULFID   500   511         
DISULFID   538   583         
DISULFID   582   591         
VARIANT   187   187  1     K -> Q (in dbSNP:rs35765619 [NCBI]). VAR_033928 
VARIANT   570   570  1     A -> G (in dbSNP:rs7790 [NCBI]). VAR_012049 
Sequence information
Length: 609 AA [This is the length of the unprocessed precursor] Molecular weight: 68678 Da [This is the MW of the unprocessed precursor] CRC64: 4D4E45820E1C2D4F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKWVESIFLI FLLNFTESRT LHRNEYGIAS ILDSYQCTAE ISLADLATIF FAQFVQEATY 

        70         80         90        100        110        120 
KEVSKMVKDA LTAIEKPTGD EQSSGCLENQ LPAFLEELCH EKEILEKYGH SDCCSQSEEG 

       130        140        150        160        170        180 
RHNCFLAHKK PTPASIPLFQ VPEPVTSCEA YEEDRETFMN KFIYEIARRH PFLYAPTILL 

       190        200        210        220        230        240 
WAARYDKIIP SCCKAENAVE CFQTKAATVT KELRESSLLN QHACAVMKNF GTRTFQAITV 

       250        260        270        280        290        300 
TKLSQKFTKV NFTEIQKLVL DVAHVHEHCC RGDVLDCLQD GEKIMSYICS QQDTLSNKIT 

       310        320        330        340        350        360 
ECCKLTTLER GQCIIHAEND EKPEGLSPNL NRFLGDRDFN QFSSGEKNIF LASFVHEYSR 

       370        380        390        400        410        420 
RHPQLAVSVI LRVAKGYQEL LEKCFQTENP LECQDKGEEE LQKYIQESQA LAKRSCGLFQ 

       430        440        450        460        470        480 
KLGEYYLQNA FLVAYTKKAP QLTSSELMAI TRKMAATAAT CCQLSEDKLL ACGEGAADII 

       490        500        510        520        530        540 
IGHLCIRHEM TPVNPGVGQC CTSSYANRRP CFSSLVVDET YVPPAFSDDK FIFHKDLCQA 

       550        560        570        580        590        600 
QGVALQTMKQ EFLINLVKQK PQITEEQLEA VIADFSGLLE KCCQGQEQEV CFAEEGQKLI 


SKTRAALGV 

P02771 in FASTA format

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