FETA_PIG
ID FETA_PIG Reviewed; 610 AA.
AC Q8MJ76;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, 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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12464028; DOI=10.1046/j.1365-2052.2002.00938_4.x;
RA Kim J.G., Nonneman D., Vallet J.L., Christenson R.K.;
RT "Mapping of the porcine alpha-fetoprotein (AFP) gene to swine chromosome
RT 8.";
RL Anim. Genet. 33:471-472(2002).
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. Synthesized by the fetal liver and yolk
CC sac.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF517770; AAM66710.1; -; mRNA.
DR RefSeq; NP_999482.1; NM_214317.1.
DR AlphaFoldDB; Q8MJ76; -.
DR SMR; Q8MJ76; -.
DR STRING; 9823.ENSSSCP00000009550; -.
DR PaxDb; Q8MJ76; -.
DR PeptideAtlas; Q8MJ76; -.
DR PRIDE; Q8MJ76; -.
DR Ensembl; ENSSSCT00000009803; ENSSSCP00000009550; ENSSSCG00000008949.
DR Ensembl; ENSSSCT00005066987; ENSSSCP00005041583; ENSSSCG00005041620.
DR Ensembl; ENSSSCT00015102417; ENSSSCP00015042518; ENSSSCG00015075988.
DR Ensembl; ENSSSCT00025024215; ENSSSCP00025010246; ENSSSCG00025017831.
DR Ensembl; ENSSSCT00030050198; ENSSSCP00030022827; ENSSSCG00030036109.
DR Ensembl; ENSSSCT00035066218; ENSSSCP00035026852; ENSSSCG00035049651.
DR Ensembl; ENSSSCT00040104307; ENSSSCP00040047489; ENSSSCG00040075243.
DR Ensembl; ENSSSCT00050108209; ENSSSCP00050047948; ENSSSCG00050078532.
DR Ensembl; ENSSSCT00055060893; ENSSSCP00055048813; ENSSSCG00055030552.
DR Ensembl; ENSSSCT00060051862; ENSSSCP00060022071; ENSSSCG00060038356.
DR Ensembl; ENSSSCT00065043611; ENSSSCP00065018546; ENSSSCG00065032162.
DR Ensembl; ENSSSCT00070012410; ENSSSCP00070010206; ENSSSCG00070006487.
DR GeneID; 397586; -.
DR KEGG; ssc:397586; -.
DR CTD; 174; -.
DR VGNC; VGNC:85172; AFP.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR GeneTree; ENSGT00390000000113; -.
DR HOGENOM; CLU_030161_1_0_1; -.
DR InParanoid; Q8MJ76; -.
DR OMA; HEECCRG; -.
DR OrthoDB; 906547at2759; -.
DR TreeFam; TF335561; -.
DR Reactome; R-SSC-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-SSC-8957275; Post-translational protein phosphorylation.
DR Proteomes; UP000008227; Chromosome 8.
DR Proteomes; UP000314985; Chromosome 8.
DR Bgee; ENSSSCG00000008949; Expressed in forelimb bud and 6 other tissues.
DR Genevisible; Q8MJ76; SS.
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 /id="PRO_0000321958"
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 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
FT MOD_RES 345
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..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; 68625 MW; C985BEAD44963D5E CRC64;
MKWVVSIFLI VLLNFTESRT MHENAYGIAS ILDSSQCSAE MNLVDLATIF FAQFVQEATY
KEVNQMVKDV LTVIEKSTGS EQPAGCLENQ VSVFLEEICH EEEIPEKYGL SHCCSQSGEE
RHNCFLARKK AAPASIPPFQ VPEPVTSCKA YEENRELFMT RYIYEIARRH PFLYAPTILS
LAAQYDKIIP PCCKAENAVE CFQTKAASIT KELRESSLLN QHMCTVMRQF GARTFRAITV
TKLSQKFPKA NFTEIQKLVL DVAHIHEECC RGNVLECLQD AERVVSYVCS QQDTLSSKIA
ECCKLPTTLE LGQCIIHAEN DDKPEGLSPN LNRFLGERDF NQLSSREKDL SMARFTYEYS
RRHPKLAVPV ILRVAKGYQE LLEKCSQSEN PLECQDKGEE ELEKYIQESQ ALAKRSCGLF
QKLGEYYLQN AFLVAYTKKA PQLTPPELMA LTRKMATTGA ACCHLSEDRQ LACGEGAADL
IIGQLCIRHE EMPINPGVGQ CCTSSYANRR PCFSSLVLDE TYVPPPFSDD KFIFHKDLCQ
AQGVALQTMK QQFLINLVKQ KPQITEEQLE AVIADFSGLL EKCCQGQEQE VCFAEEGPAL
ISKTRASLGV
