FETA_MOUSE
ID FETA_MOUSE Reviewed; 605 AA.
AC P02772; Q3UJD0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Alpha-fetoprotein;
DE AltName: Full=Alpha-1-fetoprotein;
DE AltName: Full=Alpha-fetoglobulin;
DE Flags: Precursor;
GN Name=Afp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6164927; DOI=10.1038/291201a0;
RA Law S.W., Dugaiczyk A.;
RT "Homology between the primary structure of alpha-fetoprotein, deduced from
RT a complete cDNA sequence, and serum albumin.";
RL Nature 291:201-205(1981).
RN [2]
RP SEQUENCE REVISION TO 598.
RX PubMed=2452956; DOI=10.1093/oxfordjournals.molbev.a040350;
RA Minghetti P.P., Law S.W., Dugaiczyk A.;
RT "The rate of molecular evolution of alpha-fetoprotein approaches that of
RT pseudogenes.";
RL Mol. Biol. Evol. 2:347-358(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6172714; DOI=10.1038/294713a0;
RA Eiferman F.A., Young P.R., Scott R.W., Tilghman S.M.;
RT "Intragenic amplification and divergence in the mouse alpha-fetoprotein
RT gene.";
RL Nature 294:713-718(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Liver, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-605.
RX PubMed=6161929; DOI=10.1016/s0021-9258(19)69900-x;
RA Gorin M.B., Cooper D.L., Eiferman F.A., van de Rijn P., Tilghman S.M.;
RT "The evolution of alpha-fetoprotein and albumin. I. A comparison of the
RT primary amino acid sequences of mammalian alpha-fetoprotein and albumin.";
RL J. Biol. Chem. 256:1954-1959(1981).
CC -!- FUNCTION: Binds estrogens, fatty acids and metals.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: Glycosylated; contains two glycans.
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; V00743; CAA24118.1; -; mRNA.
DR EMBL; M16394; AAA37189.1; -; Genomic_DNA.
DR EMBL; M16381; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; M16382; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; M16383; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; M16384; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; M16385; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; M16386; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; M16387; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; M16388; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; M16389; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; M16390; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; M16391; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; M16392; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; M16393; AAA37189.1; JOINED; Genomic_DNA.
DR EMBL; AK010934; BAB27278.1; -; mRNA.
DR EMBL; AK145975; BAE26798.1; -; mRNA.
DR EMBL; AK146513; BAE27225.1; -; mRNA.
DR EMBL; AK146524; BAE27233.1; -; mRNA.
DR EMBL; AK167549; BAE39615.1; -; mRNA.
DR EMBL; AK168574; BAE40444.1; -; mRNA.
DR EMBL; AK168576; BAE40446.1; -; mRNA.
DR EMBL; AK168751; BAE40591.1; -; mRNA.
DR EMBL; AK168883; BAE40701.1; -; mRNA.
DR EMBL; AK169046; BAE40834.1; -; mRNA.
DR EMBL; AK169054; BAE40842.1; -; mRNA.
DR EMBL; AK169147; BAE40926.1; -; mRNA.
DR EMBL; BC066206; AAH66206.1; -; mRNA.
DR CCDS; CCDS19413.1; -.
DR PIR; A93254; FPMS.
DR RefSeq; NP_031449.3; NM_007423.4.
DR AlphaFoldDB; P02772; -.
DR SMR; P02772; -.
DR STRING; 10090.ENSMUSP00000041006; -.
DR GlyGen; P02772; 2 sites.
DR iPTMnet; P02772; -.
DR PhosphoSitePlus; P02772; -.
DR REPRODUCTION-2DPAGE; IPI00113163; -.
DR MaxQB; P02772; -.
DR PaxDb; P02772; -.
DR PeptideAtlas; P02772; -.
DR PRIDE; P02772; -.
DR ProteomicsDB; 272992; -.
DR Antibodypedia; 1359; 3533 antibodies from 57 providers.
DR DNASU; 11576; -.
DR Ensembl; ENSMUST00000042755; ENSMUSP00000041006; ENSMUSG00000054932.
DR GeneID; 11576; -.
DR KEGG; mmu:11576; -.
DR UCSC; uc008yba.2; mouse.
DR CTD; 174; -.
DR MGI; MGI:87951; Afp.
DR VEuPathDB; HostDB:ENSMUSG00000054932; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR GeneTree; ENSGT00390000000113; -.
DR HOGENOM; CLU_030161_1_0_1; -.
DR InParanoid; P02772; -.
DR OMA; HEECCRG; -.
DR OrthoDB; 906547at2759; -.
DR PhylomeDB; P02772; -.
DR TreeFam; TF335561; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR SABIO-RK; P02772; -.
DR BioGRID-ORCS; 11576; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Afp; mouse.
DR PRO; PR:P02772; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P02772; protein.
DR Bgee; ENSMUSG00000054932; Expressed in late embryo and 129 other tissues.
DR ExpressionAtlas; P02772; baseline and differential.
DR Genevisible; P02772; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
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; IMP:MGI.
DR GO; GO:0042448; P:progesterone metabolic process; IMP:MGI.
DR GO; GO:0019953; P:sexual reproduction; IMP:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
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..605
FT /note="Alpha-fetoprotein"
FT /id="PRO_0000001098"
FT DOMAIN 19..207
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 208..398
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 399..597
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 109..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 144..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 188..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 220..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 265..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 285..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 298..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 380..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 412..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 457..468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 481..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 496..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 534..579
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 578..587
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT CONFLICT 533..536
FT /note="LCQA -> RAKL (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 67337 MW; CE09E9F50D74619A CRC64;
MKWITPASLI LLLHFAASKA LHENEFGIAS TLDSSQCVTE KNVLSIATIT FTQFVPEATE
EEVNKMTSDV LAAMKKNSGD GCLESQLSVF LDEICHETEL SNKYGLSGCC SQSGVERHQC
LLARKKTAPA SVPPFQFPEP AESCKAHEEN RAVFMNRFIY EVSRRNPFMY APAILSLAAQ
YDKVVLACCK ADNKEECFQT KRASIAKELR EGSMLNEHVC SVIRKFGSRN LQATTIIKLS
QKLTEANFTE IQKLALDVAH IHEECCQGNS LECLQDGEKV MTYICSQQNI LSSKIAECCK
LPMIQLGFCI IHAENGVKPE GLSLNPSQFL GDRNFAQFSS EEKIMFMASF LHEYSRTHPN
LPVSVILRIA KTYQEILEKC SQSGNLPGCQ DNLEEELQKH IEESQALSKQ SCALYQTLGD
YKLQNLFLIG YTRKAPQLTS AELIDLTGKM VSIASTCCQL SEEKWSGCGE GMADIFIGHL
CIRNEASPVN SGISHCCNSS YSNRRLCITS FLRDETYAPP PFSEDKFIFH KDLCQAQGKA
LQTMKQELLI NLVKQKPELT EEQLAAVTAD FSGLLEKCCK AQDQEVCFTE EGPKLISKTR
DALGV
