FETA_HORSE
ID FETA_HORSE Reviewed; 609 AA.
AC P49066;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Alpha-fetoprotein;
DE AltName: Full=Alpha-1-fetoprotein;
DE AltName: Full=Alpha-fetoglobulin;
DE Flags: Precursor;
GN Name=AFP;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Conceptus membrane;
RA McDowell K.J., Adams M.H., Baker C.B.;
RT "Molecular cloning and sequencing of equine AFP: synthesis of AFP by
RT conceptus membranes and presence in fetal fluids.";
RL Submitted (JUN-1995) 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.
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; U28947; AAA69559.1; -; mRNA.
DR RefSeq; NP_001075421.1; NM_001081952.1.
DR AlphaFoldDB; P49066; -.
DR SMR; P49066; -.
DR STRING; 9796.ENSECAP00000020985; -.
DR PaxDb; P49066; -.
DR Ensembl; ENSECAT00000025232; ENSECAP00000020985; ENSECAG00000023229.
DR GeneID; 100034185; -.
DR KEGG; ecb:100034185; -.
DR CTD; 174; -.
DR VGNC; VGNC:51133; AFP.
DR GeneTree; ENSGT00390000000113; -.
DR HOGENOM; CLU_030161_1_0_1; -.
DR InParanoid; P49066; -.
DR OrthoDB; 906547at2759; -.
DR Proteomes; UP000002281; Chromosome 3.
DR Bgee; ENSECAG00000023229; Expressed in synovial membrane of synovial joint and 3 other tissues.
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..609
FT /note="Alpha-fetoprotein"
FT /id="PRO_0000001096"
FT DOMAIN 19..210
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 211..402
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 403..601
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 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
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..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 384..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 416..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 461..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 485..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 500..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 538..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 582..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
SQ SEQUENCE 609 AA; 68350 MW; 8ED7FD63069CC7A2 CRC64;
MKWVVSILLI FLLNSTESRT MHSNAYGIAS ALDSFQCSPE MNLVDLATIF FAQFVQEATY
KEVSKMVKDV LTVTEKSTGS EQPTGCSENR LSAFLEEICH EEEIPEKYGL SGCCSQNEEE
RHNCLLARKK DSPASIPPFQ VPEPVTSCKA YEENREMFLN RYLYEIARRH PFLYSSTALY
LASHYDKIIS ACCKSENAVE CFQSKAATIT KELRETSLLN QHVCAVIRNF GPRTLQAITV
TTLSQRYSKA NFTEIQKLVL DVAHAHEECC RGNVEECVQD GEKLISYVCS QEDILSSSIV
ECCKLPTVEL AQCIIHAEND DKPEGLSPNL NRLLGERDFN QFSSKEKDLF MARFTYEYSR
RHTKLAVPVI LRVAKGYQEF LEKCSQSENP LECQDKGEEE LQKYIQEGQA LAKRSCGLFQ
KLGDYYLQNA FLVAYTKKAP QLTPPELIAL TRKMATAAAT CCQLSEDKQL ACGEQVAGLI
IGQLCIRHEE SPINPGVGQC CTSSYANRRP CFSSLVVDET YVPPPFSDDK FIFHKDLCQA
QGVALQTMKQ QFLINLVKQK PQITEEQLEA VIADFSGLLE KCCQGQGQEV CFSEEGPQLI
SKTRAALGV
