FETA_CHICK
ID FETA_CHICK Reviewed; 615 AA.
AC P84407;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Alpha-fetoprotein;
DE AltName: Full=Alpha-1-fetoprotein;
DE AltName: Full=Alpha-fetoglobulin;
DE Flags: Precursor;
GN Name=AFP;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP PROTEIN SEQUENCE OF 355-365, AND IDENTIFICATION.
RC TISSUE=Embryo;
RX PubMed=15912509; DOI=10.1002/pmic.200401207;
RA Mangum J.E., Farlie P.G., Hubbard M.J.;
RT "Proteomic profiling of facial development in chick embryos.";
RL Proteomics 5:2542-2550(2005).
CC -!- FUNCTION: Binds copper, nickel, and fatty acids as well as, and
CC bilirubin less well than, serum albumin.
CC {ECO:0000250|UniProtKB:P02771}.
CC -!- SUBUNIT: Dimeric and trimeric forms have been found in addition to the
CC monomeric form. {ECO:0000250|UniProtKB:P02771}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P02771}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; AADN02009177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P84407; -.
DR SMR; P84407; -.
DR STRING; 9031.ENSGALP00000019033; -.
DR VEuPathDB; HostDB:geneid_422652; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR InParanoid; P84407; -.
DR OrthoDB; 906547at2759; -.
DR PhylomeDB; P84407; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00015; ALBUMIN; 1.
DR InterPro; IPR000264; ALB/AFP/VDB.
DR InterPro; IPR020858; Serum_albumin-like.
DR InterPro; IPR021177; Serum_albumin/AFP/Afamin.
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; PS51438; ALBUMIN_2; 3.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Metal-binding; Nickel; Reference proteome; Repeat; Secreted; Signal;
KW Sulfation.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..615
FT /note="Alpha-fetoprotein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000001101"
FT DOMAIN 27..218
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 223..415
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 416..609
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT MOTIF 14..16
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 283..285
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..121
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 120..131
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 155..200
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 199..213
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 236..282
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 281..289
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 301..315
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 314..325
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 396..405
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 428..458
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 457..468
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 485..501
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 500..511
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 538..593
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 592..601
FT /evidence="ECO:0000250|UniProtKB:P02771,
FT ECO:0000255|PROSITE-ProRule:PRU00769"
SQ SEQUENCE 615 AA; 70680 MW; E1ED1813D9537ED4 CRC64;
MAVLPLSGAI RLSRGDLVIE TQTQDPWAKK LITQGTDKAC ADLDVQQIQA LKMKCAMIMF
AQYVQGNTFG QVVKMAEAVT DLAKKCTEVD RDNPNCRKPL DWIFLNTICQ EDNLPRFTDC
CAKKDPERND CFLSLKNSSR GFISPFERPN AEAACKNYSE HRHSLPGYFI YEVSRRHPFL
YAPTILSVAI HYDEMMKDCC RSAEDSTHNL EECFRRQAPK VVKPIREDGL RQEHTCGILK
KFGERTIKAL KLVQISQRFP KADFFTVTKL VSDIANMHKD CCRGDMLECM RDREEILHYV
CTNQDVISSK IKKCCEKPLL QRSECIVNAE NDDKPANLSP QVREFIEDKG ICERFAQEKD
THLARFLYEY SRRHPEFSAQ MLLRIGKGYE DLLDECCKTG SPDNCCSRGE EELKKHIYET
ESVMKTSCDI YKEKGDYYFQ NEYIKFTKQM TTIGSKCCQL SQDKLLPCAE ENVSLLVDLV
LGEICRRHLT NPINPAVCHC CSSSYALRRP CMGKLEIDEN YVPLSLTPDL FTFHEDLCTT
EEEKLQHRKQ EFGIPLLLSY PMLINLIKYK PQITQEQLTS ITVAFTAMRE QCCKEENREA
CFAKEVLVTL SPICS
