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P02771

- FETA_HUMAN

UniProt

P02771 - FETA_HUMAN

Protein

Alpha-fetoprotein

Gene

AFP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi22 – 221Copper or nickel1 Publication

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. ovulation from ovarian follicle Source: Ensembl
    2. progesterone metabolic process Source: Ensembl
    3. SMAD protein signal transduction Source: Ensembl
    4. transport Source: InterPro

    Keywords - Ligandi

    Copper, Metal-binding, Nickel

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-fetoprotein
    Alternative name(s):
    Alpha-1-fetoprotein
    Alpha-fetoglobulin
    Gene namesi
    Name:AFP
    Synonyms:HPAFP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:317. AFP.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular space Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    MIMi104150. gene+phenotype.
    Orphaneti168612. Congenital deficiency in alpha-fetoprotein.
    168615. Hereditary persistence of alpha-fetoprotein.
    PharmGKBiPA24614.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 609591Alpha-fetoproteinPRO_0000001097Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi99 ↔ 114
    Disulfide bondi113 ↔ 124
    Disulfide bondi148 ↔ 193
    Disulfide bondi192 ↔ 201
    Disulfide bondi224 ↔ 270
    Glycosylationi251 – 2511N-linked (GlcNAc...)CAR_000070
    Disulfide bondi269 ↔ 277
    Disulfide bondi289 ↔ 303
    Disulfide bondi302 ↔ 313
    Disulfide bondi384 ↔ 393
    Disulfide bondi416 ↔ 462
    Disulfide bondi461 ↔ 472
    Disulfide bondi485 ↔ 501
    Disulfide bondi500 ↔ 511
    Disulfide bondi538 ↔ 583
    Disulfide bondi582 ↔ 591

    Post-translational modificationi

    Independent studies suggest heterogeneity of the N-terminal sequence of the mature protein and of the cleavage site of the signal sequence.
    Sulfated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Sulfation

    Proteomic databases

    MaxQBiP02771.
    PaxDbiP02771.
    PeptideAtlasiP02771.
    PRIDEiP02771.

    PTM databases

    PhosphoSiteiP02771.
    UniCarbKBiP02771.

    Expressioni

    Tissue specificityi

    Plasma. Synthesized by the fetal liver and yolk sac.

    Developmental stagei

    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.

    Gene expression databases

    ArrayExpressiP02771.
    BgeeiP02771.
    CleanExiHS_AFP.
    GenevestigatoriP02771.

    Organism-specific databases

    HPAiCAB024283.
    CAB025339.
    HPA010607.
    HPA023600.

    Interactioni

    Subunit structurei

    Dimeric and trimeric forms have been found in addition to the monomeric form.

    Protein-protein interaction databases

    BioGridi106682. 11 interactions.
    IntActiP02771. 9 interactions.
    MINTiMINT-1401527.
    STRINGi9606.ENSP00000226359.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MRKX-ray1.40P137-145[»]
    ProteinModelPortaliP02771.
    SMRiP02771. Positions 39-608.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 210192Albumin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini211 – 402192Albumin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini403 – 601199Albumin 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ALB/AFP/VDB family.PROSITE-ProRule annotation
    Contains 3 albumin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG45992.
    HOGENOMiHOG000293137.
    HOVERGENiHBG004207.
    InParanoidiP02771.
    KOiK16144.
    OrthoDBiEOG7S4X5C.
    PhylomeDBiP02771.
    TreeFamiTF335561.

    Family and domain databases

    InterProiIPR000264. ALB/AFP/VDB.
    IPR001703. Alpha-fetoprotein.
    IPR020858. Serum_albumin-like.
    IPR021177. Serum_albumin/AFP.
    IPR020857. Serum_albumin_CS.
    IPR014760. Serum_albumin_N.
    [Graphical view]
    PfamiPF00273. Serum_albumin. 3 hits.
    [Graphical view]
    PIRSFiPIRSF002520. Serum_albumin_subgroup. 1 hit.
    PRINTSiPR00803. AFETOPROTEIN.
    PR00802. SERUMALBUMIN.
    SMARTiSM00103. ALBUMIN. 3 hits.
    [Graphical view]
    SUPFAMiSSF48552. SSF48552. 3 hits.
    PROSITEiPS00212. ALBUMIN_1. 2 hits.
    PS51438. ALBUMIN_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P02771-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKWVESIFLI FLLNFTESRT LHRNEYGIAS ILDSYQCTAE ISLADLATIF    50
    FAQFVQEATY KEVSKMVKDA LTAIEKPTGD EQSSGCLENQ LPAFLEELCH 100
    EKEILEKYGH SDCCSQSEEG RHNCFLAHKK PTPASIPLFQ VPEPVTSCEA 150
    YEEDRETFMN KFIYEIARRH PFLYAPTILL WAARYDKIIP SCCKAENAVE 200
    CFQTKAATVT KELRESSLLN QHACAVMKNF GTRTFQAITV TKLSQKFTKV 250
    NFTEIQKLVL DVAHVHEHCC RGDVLDCLQD GEKIMSYICS QQDTLSNKIT 300
    ECCKLTTLER GQCIIHAEND EKPEGLSPNL NRFLGDRDFN QFSSGEKNIF 350
    LASFVHEYSR RHPQLAVSVI LRVAKGYQEL LEKCFQTENP LECQDKGEEE 400
    LQKYIQESQA LAKRSCGLFQ KLGEYYLQNA FLVAYTKKAP QLTSSELMAI 450
    TRKMAATAAT CCQLSEDKLL ACGEGAADII IGHLCIRHEM TPVNPGVGQC 500
    CTSSYANRRP CFSSLVVDET YVPPAFSDDK FIFHKDLCQA QGVALQTMKQ 550
    EFLINLVKQK PQITEEQLEA VIADFSGLLE KCCQGQEQEV CFAEEGQKLI 600
    SKTRAALGV 609
    Length:609
    Mass (Da):68,678
    Last modified:July 21, 1986 - v1
    Checksum:i4D4E45820E1C2D4F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti187 – 1871K → Q.
    Corresponds to variant rs35765619 [ dbSNP | Ensembl ].
    VAR_033928
    Natural varianti570 – 5701A → G.1 Publication
    Corresponds to variant rs7790 [ dbSNP | Ensembl ].
    VAR_012049

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS3556.1.
    PIRiA26624. FPHU.
    RefSeqiNP_001125.1. NM_001134.2.
    UniGeneiHs.518808.

    Genome annotation databases

    EnsembliENST00000395792; ENSP00000379138; ENSG00000081051.
    GeneIDi174.
    KEGGihsa:174.
    UCSCiuc003hgz.1. human.

    Polymorphism databases

    DMDMi120042.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Alpha-fetoprotein entry

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS3556.1.
    PIRi A26624. FPHU.
    RefSeqi NP_001125.1. NM_001134.2.
    UniGenei Hs.518808.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MRK X-ray 1.40 P 137-145 [» ]
    ProteinModelPortali P02771.
    SMRi P02771. Positions 39-608.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106682. 11 interactions.
    IntActi P02771. 9 interactions.
    MINTi MINT-1401527.
    STRINGi 9606.ENSP00000226359.

    PTM databases

    PhosphoSitei P02771.
    UniCarbKBi P02771.

    Polymorphism databases

    DMDMi 120042.

    Proteomic databases

    MaxQBi P02771.
    PaxDbi P02771.
    PeptideAtlasi P02771.
    PRIDEi P02771.

    Protocols and materials databases

    DNASUi 174.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000395792 ; ENSP00000379138 ; ENSG00000081051 .
    GeneIDi 174.
    KEGGi hsa:174.
    UCSCi uc003hgz.1. human.

    Organism-specific databases

    CTDi 174.
    GeneCardsi GC04P074302.
    HGNCi HGNC:317. AFP.
    HPAi CAB024283.
    CAB025339.
    HPA010607.
    HPA023600.
    MIMi 104150. gene+phenotype.
    neXtProti NX_P02771.
    Orphaneti 168612. Congenital deficiency in alpha-fetoprotein.
    168615. Hereditary persistence of alpha-fetoprotein.
    PharmGKBi PA24614.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45992.
    HOGENOMi HOG000293137.
    HOVERGENi HBG004207.
    InParanoidi P02771.
    KOi K16144.
    OrthoDBi EOG7S4X5C.
    PhylomeDBi P02771.
    TreeFami TF335561.

    Miscellaneous databases

    ChiTaRSi AFP. human.
    GeneWikii Alpha-fetoprotein.
    GenomeRNAii 174.
    NextBioi 698.
    PROi P02771.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02771.
    Bgeei P02771.
    CleanExi HS_AFP.
    Genevestigatori P02771.

    Family and domain databases

    InterProi IPR000264. ALB/AFP/VDB.
    IPR001703. Alpha-fetoprotein.
    IPR020858. Serum_albumin-like.
    IPR021177. Serum_albumin/AFP.
    IPR020857. Serum_albumin_CS.
    IPR014760. Serum_albumin_N.
    [Graphical view ]
    Pfami PF00273. Serum_albumin. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF002520. Serum_albumin_subgroup. 1 hit.
    PRINTSi PR00803. AFETOPROTEIN.
    PR00802. SERUMALBUMIN.
    SMARTi SM00103. ALBUMIN. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48552. SSF48552. 3 hits.
    PROSITEi PS00212. ALBUMIN_1. 2 hits.
    PS51438. ALBUMIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiFETA_HUMAN
    AccessioniPrimary (citable) accession number: P02771
    Secondary accession number(s): B2RBU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 153 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3