FETA_GORGO
ID FETA_GORGO Reviewed; 609 AA.
AC P28050;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, 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 Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1706310; DOI=10.1016/0888-7543(91)90221-y;
RA Ryan S.C., Zielinski R., Dugaiczyk A.;
RT "Structure of the gorilla alpha-fetoprotein gene and the divergence of
RT primates.";
RL Genomics 9:60-72(1991).
CC -!- FUNCTION: Binds copper, nickel, and fatty acids as well as, and
CC bilirubin less well than, serum albumin.
CC -!- SUBUNIT: Dimeric and trimeric forms have been found in addition to the
CC monomeric form. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
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; M38272; AAA73520.1; -; Genomic_DNA.
DR PIR; A37970; FPGO.
DR AlphaFoldDB; P28050; -.
DR SMR; P28050; -.
DR STRING; 9593.ENSGGOP00000008435; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR InParanoid; P28050; -.
DR Proteomes; UP000001519; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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..609
FT /note="Alpha-fetoprotein"
FT /id="PRO_0000001095"
FT DOMAIN 19..210
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 211..402
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 403..601
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 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
FT MOD_RES 444
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..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 384..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 416..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 461..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 485..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 500..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 538..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 582..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
SQ SEQUENCE 609 AA; 68698 MW; E8AE548377DB60EB CRC64;
MKWVESIFLI FLLNFTESRT LHRNEYGIAS ILDSYQCTAE ISLADLATIF FAQFVQEATY
KEVSKMVKDA LTAIEKPTGD EQSAGCLENQ LPAFLEELCH EKEILEKYGL SDCCSQSEEG
RHNCFLAHKK PTPASIPLFQ VPEPVTSCEA YEEDRETFMN KFIYEIARRH PFLYAPTILL
WAARYDKIIP SCCKAENAVE CFQTKAATVT KELRESSLLN QHACAVMKNF GTRTFQAITV
TKLSQKFTKV NFTEIQKLVL DVAHVHEHCC RGDVLDCLQD GEKIMSYICS QQDTLSNKIT
ECCKLTTLER GQCIIHAEND EKPEGLSPNL NRFLGDRDFN QFSSGEKNIF LASFVHEYSR
RHPQLAVSVI LRVAKGYQEL LEKCFQTENP LECQDKGEEE LQKYIQESQA LAKRSCGLFQ
KLGEYYLQNA FLVAYTKKAP QLTSSELMAI TRKMAATAAT CCQLSEDKLL ACGEGAADII
IGHLCIRHEM TPVNPGVGQC CTSSYANRRP CFSSLVVDET YVPPAFSDDK FIFHKDLCQA
QGVALQTMKQ EFLINLVKQK PQITEEQLET VIADFSGLLE KCCQGQEQEV CFAEEGQKLI
SKTRTALGV
