FETA_RAT
ID FETA_RAT Reviewed; 611 AA.
AC P02773; Q63032; Q63205;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Alpha-fetoprotein;
DE AltName: Full=Alpha-1-fetoprotein;
DE AltName: Full=Alpha-fetoglobulin;
DE Flags: Precursor;
GN Name=Afp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=1376990; DOI=10.1016/0006-291x(92)91674-f;
RA Watanabe T., Jimenez-Molina J.L., Chou J.Y.;
RT "Characterization of a rat variant alpha-fetoprotein.";
RL Biochem. Biophys. Res. Commun. 185:648-656(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-106 (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
RX PubMed=2582363; DOI=10.1093/nar/13.7.2387;
RA Turcotte B., Guertin M., Chevrette M., Belanger L.;
RT "Rat alpha 1-fetoprotein messenger RNA: 5'-end sequence and glucocorticoid-
RT suppressed liver transcription in an improved nuclear run-off assay.";
RL Nucleic Acids Res. 13:2387-2398(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 91-611 (ISOFORM 1).
RX PubMed=6167988; DOI=10.1073/pnas.78.6.3521;
RA Jagodzinski L.L., Sargent T.D., Yang M., Glackin C., Bonner J.;
RT "Sequence homology between RNAs encoding rat alpha-fetoprotein and rat
RT serum albumin.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:3521-3525(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-51 (ISOFORM 1).
RX PubMed=1722723; DOI=10.3109/10425179009041345;
RA Buzard G.S., Locker J.;
RT "The transcription control region of the rat alpha-fetoprotein gene. DNA
RT sequence and homology studies.";
RL DNA Seq. 1:33-48(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34 (ISOFORM 1).
RX PubMed=2434929; DOI=10.1093/nar/15.3.1338;
RA Chevrette M., Guertin M., Turcotte B., Belanger L.;
RT "The rat alpha 1-fetoprotein gene: characterization of the 5'-flanking
RT region and tandem organization with the albumin gene.";
RL Nucleic Acids Res. 15:1338-1338(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13 (ISOFORM 1).
RX PubMed=2442163; DOI=10.1016/s0021-9258(18)45231-3;
RA Nahon J.-L., Danan J.L., Poiret M., Tratner I., Jose-Estanyol M.,
RA Sala-Trepat J.M.;
RT "The rat alpha-fetoprotein and albumin genes. Transcriptional control and
RT comparison of the sequence organization and promoter region.";
RL J. Biol. Chem. 262:12479-12487(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 476-611.
RX PubMed=6157690; DOI=10.1016/s0021-9258(19)70511-0;
RA Innis M.A., Miller D.L.;
RT "Alpha-fetoprotein gene expression. Partial DNA sequence and COOH-terminal
RT homology to albumin.";
RL J. Biol. Chem. 255:8994-8996(1980).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 556-611.
RX PubMed=6157681; DOI=10.1016/s0021-9258(19)70603-6;
RA Liao W.S.L., Hamilton R.W., Taylor J.M.;
RT "Amino acid sequence homology between rat alpha-fetoprotein and albumin at
RT the COOH-terminal regions.";
RL J. Biol. Chem. 255:8046-8049(1980).
CC -!- FUNCTION: Binds estrogens, fatty acids and metals.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P02773-1; Sequence=Displayed;
CC Name=2; Synonyms=ARFP9;
CC IsoId=P02773-2; Sequence=VSP_011552;
CC -!- TISSUE SPECIFICITY: Plasma. {ECO:0000269|PubMed:1376990}.
CC -!- PTM: Sulfated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40695.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X02361; CAA26214.1; -; mRNA.
DR EMBL; V01254; CAA24567.1; -; mRNA.
DR EMBL; X05093; CAA28744.1; -; Genomic_DNA.
DR EMBL; J02816; AAA40695.1; ALT_INIT; Genomic_DNA.
DR EMBL; V01236; CAA24546.1; -; mRNA.
DR EMBL; J00694; AAA40694.1; -; mRNA.
DR PIR; A93561; FPRT.
DR AlphaFoldDB; P02773; -.
DR SMR; P02773; -.
DR STRING; 10116.ENSRNOP00000003879; -.
DR ChEMBL; CHEMBL3141; -.
DR DrugBank; DB11221; Dioxybenzone.
DR GlyGen; P02773; 2 sites.
DR PaxDb; P02773; -.
DR PRIDE; P02773; -.
DR UCSC; RGD:2065; rat. [P02773-1]
DR RGD; 2065; Afp.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR InParanoid; P02773; -.
DR PhylomeDB; P02773; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR SABIO-RK; P02773; -.
DR PRO; PR:P02773; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
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:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0001542; P:ovulation from ovarian follicle; ISO:RGD.
DR GO; GO:0031016; P:pancreas development; IEP:RGD.
DR GO; GO:0042448; P:progesterone metabolic process; ISO:RGD.
DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0019953; P:sexual reproduction; ISO:RGD.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:RGD.
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 Alternative splicing; Copper; Cytoplasm; Disulfide bond; Glycoprotein;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal; Sulfation.
FT SIGNAL 1..24
FT /evidence="ECO:0000305"
FT CHAIN 25..611
FT /note="Alpha-fetoprotein"
FT /id="PRO_0000001100"
FT DOMAIN 25..212
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 213..404
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 405..603
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT BINDING 28
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 101..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 115..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 150..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 194..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 226..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 271..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 291..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 304..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 386..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 418..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 463..474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 487..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 502..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 540..585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 584..593
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT VAR_SEQ 1..286
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_011552"
FT CONFLICT 526
FT /note="P -> L (in Ref. 7; CAA24546)"
FT /evidence="ECO:0000305"
FT CONFLICT 530..538
FT /note="EDKFIFHKD -> ATNSSSTRN (in Ref. 7; CAA24546)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="L -> P (in Ref. 7; CAA24546)"
FT /evidence="ECO:0000305"
FT CONFLICT 556..557
FT /note="IN -> VG (in Ref. 8; AAA40694)"
FT /evidence="ECO:0000305"
FT CONFLICT 598..604
FT /note="GPKLISK -> VQVDFQ (in Ref. 7; CAA24546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 68386 MW; 7DC54624B7245C41 CRC64;
MKQPATMKWS ASISFLLLLN FAEPRVLHTN EFGIESTLDS SQCPTEKNMF NVATIVVAQF
VQDATKAEVN KMSSDALAAM KENTGDGCLE NQLSVFLDEI CHETELSNKY GFSGCCNQSG
VERHQCLLAR KKTAPDSVPP FHFPETAESC PAYEENRAMS INTFIYDVSK RNPFLYAPTI
LYLAAQYDKA VPACCKADNM EECFQTKRAS MAKELREGSM LNEHVCAVIR KFGSRNLQAV
LIIKLSQKFP KANITEIRKL ALDVAHIHEQ CCHGNAMECL QDGESVMTHM CSQQEILSSK
TAECCKLPTI ELGYCIIHAE NGDKPEGLTL NPSEFLGDRN FAQFSSEEKL LFMASFLHEY
SRNHPNLPVS VILKTAKSYQ EILEKCSQSE TPSKCQDNME EELQKHIQES QALAKQSCNL
YQKLGPYYLQ NLFLIGYTRK APQLTSAELI DLTGKMVSIA STCCQLSEEK RSACGEGLAD
IYIGHLCLRH EANPVNSGIN HCCSSSYSNR RLCITSFLRD ETYVPPPFSE DKFIFHKDLC
QAQGRALQTM KQELLINLVK QKPEMTEEQH AAVTADFSGL LEKCCKDQDQ EACFAKEGPK
LISKTREALG V
