ID   FETA_BOVIN              Reviewed;         610 AA.
AC   Q3SZ57;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Alpha-fetoprotein;
DE   AltName: Full=Alpha-1-fetoprotein;
DE   AltName: Full=Alpha-fetoglobulin;
DE   Flags: Precursor;
GN   Name=AFP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds copper, nickel, and fatty acids as well as, and
CC       bilirubin less well than, serum albumin. {ECO:0000250}.
CC   -!- SUBUNIT: Dimeric and trimeric forms have been found in addition to the
CC       monomeric form. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00769}.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: Sulfated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00769}.
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DR   EMBL; BC103123; AAI03124.1; -; mRNA.
DR   RefSeq; NP_001029434.1; NM_001034262.2.
DR   AlphaFoldDB; Q3SZ57; -.
DR   SMR; Q3SZ57; -.
DR   STRING; 9913.ENSBTAP00000022772; -.
DR   PaxDb; Q3SZ57; -.
DR   PeptideAtlas; Q3SZ57; -.
DR   PRIDE; Q3SZ57; -.
DR   Ensembl; ENSBTAT00000022772; ENSBTAP00000022772; ENSBTAG00000017131.
DR   GeneID; 506011; -.
DR   KEGG; bta:506011; -.
DR   CTD; 174; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017131; -.
DR   VGNC; VGNC:25717; AFP.
DR   eggNOG; ENOG502R7EA; Eukaryota.
DR   GeneTree; ENSGT00390000000113; -.
DR   HOGENOM; CLU_030161_1_0_1; -.
DR   InParanoid; Q3SZ57; -.
DR   OMA; HEECCRG; -.
DR   OrthoDB; 906547at2759; -.
DR   TreeFam; TF335561; -.
DR   Proteomes; UP000009136; Chromosome 6.
DR   Bgee; ENSBTAG00000017131; Expressed in metanephros cortex and 10 other tissues.
DR   ExpressionAtlas; Q3SZ57; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
DR   GO; GO:0042448; P:progesterone metabolic process; IEA:Ensembl.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR   CDD; cd00015; ALBUMIN; 3.
DR   InterPro; IPR000264; ALB/AFP/VDB.
DR   InterPro; IPR020858; Serum_albumin-like.
DR   InterPro; IPR021177; Serum_albumin/AFP/Afamin.
DR   InterPro; IPR020857; Serum_albumin_CS.
DR   InterPro; IPR014760; Serum_albumin_N.
DR   PANTHER; PTHR11385; PTHR11385; 1.
DR   Pfam; PF00273; Serum_albumin; 3.
DR   PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
DR   PRINTS; PR00803; AFETOPROTEIN.
DR   PRINTS; PR00802; SERUMALBUMIN.
DR   SMART; SM00103; ALBUMIN; 3.
DR   SUPFAM; SSF48552; SSF48552; 3.
DR   PROSITE; PS00212; ALBUMIN_1; 2.
DR   PROSITE; PS51438; ALBUMIN_2; 3.
PE   2: Evidence at transcript level;
KW   Copper; Disulfide bond; Glycoprotein; Metal-binding; Nickel;
KW   Phosphoprotein; Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..610
FT                   /note="Alpha-fetoprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000246080"
FT   DOMAIN          19..210
FT                   /note="Albumin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DOMAIN          211..403
FT                   /note="Albumin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DOMAIN          404..602
FT                   /note="Albumin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   BINDING         22
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02771"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02771"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02771"
FT   MOD_RES         445
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02771"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        99..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        113..124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        148..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        192..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        224..270
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        269..277
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        289..303
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        302..314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        385..394
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        417..463
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        462..473
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        486..502
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        501..512
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        539..584
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT   DISULFID        583..592
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
SQ   SEQUENCE   610 AA;  68588 MW;  1D7BC83FE2D4B11D CRC64;
     MKWVVSFFLL FLLNFSDSRT MHKNAYGIDS ILDSSPCSSG TNLVGLATIF FAQSVQGATY
     EEVSQMVKDV LTIIEKPTGS KQPAGCLENQ VSAFLEEICR EKEIPEKYGL SDCCSRTGEE
     RHDCFLAHKK AAPASIPPFP VLEPVTSCKS YKENRELFIN RYIYEIARRH PVLYAPTILS
     VANQYNKIIP HCCKAENATE CFETKVTSIT KELRESSLLN QHICAVMGKF GPRTFRAITV
     TKVSQKFPKA NFTEIQKLVM DVAHIHEECC KGNVLECLQD GERVMSYICS QQDILSRQIA
     ECCKLPTTLE LGHCIIHAEN DDKPEGLSPN VNRFLGDRDF NQLSSRDKDL SMARFTYEYS
     RRHTKLAVPI ILRVAKGYQE LLEKCSQSEN PSECQDKGEE ELEKYIQESQ ALAKRSCGLF
     QKLGEYYLQN AFLVAYTKKA PQLTSPELMA LTRKMANAGA ICCHLSEDKQ LACGEGVADL
     IIGHLCIRHE ENPINPGVDQ CCTSSYSNRR PCFSSLVVDE TYVPPPFSDD KFIFHKDLCQ
     VQGVPLQTMK QQFLINLVKQ KPQITEEQLE TVVADFSGLL EKCCQSQEQE VCFTEEGPAL
     ISKTRAALGV