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P02771 (FETA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-fetoprotein
Alternative name(s):
Alpha-1-fetoprotein
Alpha-fetoglobulin
Gene names
Name:AFP
Synonyms:HPAFP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length609 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 structure

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.

Post-translational modification

Independent studies suggest heterogeneity of the N-terminal sequence of the mature protein and of the cleavage site of the signal sequence.

Sulfated.

Sequence similarities

Belongs to the ALB/AFP/VDB family.

Contains 3 albumin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.9 Ref.10 Ref.11 Ref.12
Chain19 – 609591Alpha-fetoprotein
PRO_0000001097

Regions

Domain19 – 210192Albumin 1
Domain211 – 402192Albumin 2
Domain403 – 601199Albumin 3

Sites

Metal binding221Copper or nickel Ref.13

Amino acid modifications

Glycosylation2511N-linked (GlcNAc...)
CAR_000070
Disulfide bond99 ↔ 114
Disulfide bond113 ↔ 124
Disulfide bond148 ↔ 193
Disulfide bond192 ↔ 201
Disulfide bond224 ↔ 270
Disulfide bond269 ↔ 277
Disulfide bond289 ↔ 303
Disulfide bond302 ↔ 313
Disulfide bond384 ↔ 393
Disulfide bond416 ↔ 462
Disulfide bond461 ↔ 472
Disulfide bond485 ↔ 501
Disulfide bond500 ↔ 511
Disulfide bond538 ↔ 583
Disulfide bond582 ↔ 591

Natural variations

Natural variant1871K → Q.
Corresponds to variant rs35765619 [ dbSNP | Ensembl ].
VAR_033928
Natural variant5701A → G. Ref.3
Corresponds to variant rs7790 [ dbSNP | Ensembl ].
VAR_012049

Sequences

Sequence LengthMass (Da)Tools
P02771 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 4D4E45820E1C2D4F

FASTA60968,678
        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 

« Hide

References

« Hide 'large scale' references
[1]"Primary structures of human alpha-fetoprotein and its mRNA."
Morinaga T., Sakai M., Wegmann T.G., Tamaoki T.
Proc. Natl. Acad. Sci. U.S.A. 80:4604-4608(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure, polymorphism, and novel repeated DNA elements revealed by a complete sequence of the human alpha-fetoprotein gene."
Gibbs P.E.M., Zielinski R., Boyd C., Dugaiczyk A.
Biochemistry 26:1332-1343(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-570.
Tissue: Heart.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[5]"The human alpha-fetoprotein gene. Sequence organization and the 5' flanking region."
Sakai M., Morinaga T., Urano Y., Watanabe K., Wegmann T.G., Tamaoki T.
J. Biol. Chem. 260:5055-5060(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 AND 596-609, GENE STRUCTURE.
[6]"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)."
McVey J.H., Michaelides K., Hansen L.P., Ferguson-Smith M., Tilghman S., Krumlauf R., Tuddenham E.G.D.
Hum. Mol. Genet. 2:379-384(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[7]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 311-332; 348-372 AND 422-437, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[8]"Structure and evolution of human alpha-fetoprotein deduced from partial sequence of cloned cDNA."
Beattie W.G., Dugaiczyk A.
Gene 20:415-422(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 429-556.
[9]"Human alpha-fetoprotein primary structure: a mass spectrometric study."
Pucci P., Siciliano R., Malorni A., Marino G., Tecce M.F., Ceccarini C., Terrana B.
Biochemistry 30:5061-5066(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-609.
[10]"Studies on human alpha-fetoprotein. Isolation and characterization of monomeric and polymeric forms and amino-terminal sequence analysis."
Yachnin S., Hsu R., Heinrikson R.L., Miller J.B.
Biochim. Biophys. Acta 493:418-428(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 19-35.
[11]"Comparative chemical structures of human alpha-fetoproteins from fetal serum and from ascites fluid of a patient with hepatoma."
Aoyagi Y., Ikenaka T., Ichida F.
Cancer Res. 37:3663-3667(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 19-38.
[12]"Alpha fetoprotein: structure and expression in man and inbred mouse strains under normal conditions and liver injury."
Ruoslahti E., Pihko H., Vaheri A., Seppala M., Virolainen M., Konttinen A.
Johns Hopkins Med. J. Suppl. 3:249-255(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 19-39.
[13]"Copper(II)-binding ability of human alpha-fetoprotein."
Aoyagi Y., Ikenaka T., Ichida F.
Cancer Res. 38:3483-3486(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: METAL-BINDING.
[14]"Alpha-fetoprotein as a carrier protein in plasma and its bilirubin-binding ability."
Aoyagi Y., Ikenaka T., Ichida F.
Cancer Res. 39:3571-3574(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: BILIRUBIN-BINDING.
[15]"Tyrosine sulfation of proteins from the human hepatoma cell line HepG2."
Liu M.C., Yu S., Sy J., Redman C.M., Lipmann F.
Proc. Natl. Acad. Sci. U.S.A. 82:7160-7164(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01514 mRNA. Translation: CAA24758.1.
M16110 Genomic DNA. Translation: AAB58754.1.
AK314817 mRNA. Translation: BAG37340.1.
BC027881 mRNA. Translation: AAH27881.1.
M10949 Genomic DNA. Translation: AAA51674.1.
M10950 Genomic DNA. Translation: AAA51675.1.
Z19532 Genomic DNA. Translation: CAA79592.1.
CCDSCCDS3556.1.
PIRFPHU. A26624.
RefSeqNP_001125.1. NM_001134.2.
UniGeneHs.518808.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MRKX-ray1.40P137-145[»]
ProteinModelPortalP02771.
SMRP02771. Positions 39-608.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106682. 11 interactions.
IntActP02771. 9 interactions.
MINTMINT-1401527.
STRING9606.ENSP00000226359.

PTM databases

PhosphoSiteP02771.
UniCarbKBP02771.

Polymorphism databases

DMDM120042.

Proteomic databases

MaxQBP02771.
PaxDbP02771.
PeptideAtlasP02771.
PRIDEP02771.

Protocols and materials databases

DNASU174.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000395792; ENSP00000379138; ENSG00000081051.
GeneID174.
KEGGhsa:174.
UCSCuc003hgz.1. human.

Organism-specific databases

CTD174.
GeneCardsGC04P074302.
HGNCHGNC:317. AFP.
HPACAB024283.
CAB025339.
HPA010607.
HPA023600.
MIM104150. gene+phenotype.
neXtProtNX_P02771.
Orphanet168612. Congenital deficiency in alpha-fetoprotein.
168615. Hereditary persistence of alpha-fetoprotein.
PharmGKBPA24614.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45992.
HOGENOMHOG000293137.
HOVERGENHBG004207.
InParanoidP02771.
KOK16144.
OrthoDBEOG7S4X5C.
PhylomeDBP02771.
TreeFamTF335561.

Gene expression databases

ArrayExpressP02771.
BgeeP02771.
CleanExHS_AFP.
GenevestigatorP02771.

Family and domain databases

InterProIPR000264. ALB/AFP/VDB.
IPR001703. Alpha-fetoprotein.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSPR00803. AFETOPROTEIN.
PR00802. SERUMALBUMIN.
SMARTSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMSSF48552. SSF48552. 3 hits.
PROSITEPS00212. ALBUMIN_1. 2 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAFP. human.
GeneWikiAlpha-fetoprotein.
GenomeRNAi174.
NextBio698.
PROP02771.
SOURCESearch...

Entry information

Entry nameFETA_HUMAN
AccessionPrimary (citable) accession number: P02771
Secondary accession number(s): B2RBU3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM