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   27-MAR-2024, entry version 144.
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   GlyCosmos; P02773; 2 sites, No reported glycans.
DR   GlyGen; P02773; 2 sites.
DR   PhosphoSitePlus; P02773; -.
DR   PaxDb; 10116-ENSRNOP00000003879; -.
DR   UCSC; RGD:2065; rat. [P02773-1]
DR   AGR; RGD:2065; -.
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; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0010033; P:response to organic substance; IEP:RGD.
DR   GO; GO:0019953; P:sexual reproduction; ISO:RGD.
DR   CDD; cd00015; ALBUMIN; 3.
DR   Gene3D; 1.10.246.10; -; 6.
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:SF7; ALPHA-FETOPROTEIN; 1.
DR   PANTHER; PTHR11385; SERUM ALBUMIN-RELATED; 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; Serum albumin-like; 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
//