FETA_CANLF
ID FETA_CANLF Reviewed; 609 AA.
AC Q8MJU5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Alpha-fetoprotein;
DE AltName: Full=Alpha-1-fetoprotein;
DE AltName: Full=Alpha-fetoglobulin;
DE Flags: Precursor;
GN Name=AFP;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Furuichi M., Neo S., Hisasue M., Tsuchiya R., Watanabe M., Hashizaki K.,
RA Hisamatsu S., Yamada T.;
RT "Canine alpha-fetoprotein cDNA.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds copper, nickel, and fatty acids as well as, and
CC bilirubin less well than, serum albumin. {ECO:0000250}.
CC -!- SUBUNIT: Dimeric and trimeric forms have been found in addition to the
CC monomeric form. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00769}.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: Sulfated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB089789; BAC07513.1; -; mRNA.
DR RefSeq; NP_001003027.1; NM_001003027.1.
DR AlphaFoldDB; Q8MJU5; -.
DR SMR; Q8MJU5; -.
DR STRING; 9615.ENSCAFP00000066373; -.
DR PaxDb; Q8MJU5; -.
DR PRIDE; Q8MJU5; -.
DR GeneID; 403551; -.
DR KEGG; cfa:403551; -.
DR CTD; 174; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR InParanoid; Q8MJU5; -.
DR OrthoDB; 906547at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_0000247327"
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 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02771"
FT MOD_RES 344
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; 68783 MW; BE4B8250C5AF2AF0 CRC64;
MKWVVSFFSI FLLNFSESRT MHRNAYGIAS ILDSSQCSAE MNLVDLATIF FAQFVQEATY
KEVSKMVKDI LTVIEKSTGS EQPGGCLENQ LPAFLEEICH EKEISEKYGL ADCCSQREEE
RHNCFLAHKK AAPPSIPPFQ VAEPVTSCKA YEENRDMFMN RYIYEIARRH PFLYAPTILS
LAAHYGKIIP LCCKAENAVE CFQTKTSLIT KELRESSLLN QHICAVMRNF GPRTFRAITV
TKLSQKFSKA NFTEIQKLVL DVAHIHEECC RGNVLECLQD GEKIMSYICS QQDILSSKIA
DCCKLPILEL GQCIIHAEND GKPEGLSPNL NRFLEERDFN QFSSREKDLF MARFTYEYSR
RHTKLAVPVV LRVAKGYQEL LEKCSQSENP LECQDKGEEE LEKYIQESQA LAKRSCGLFQ
KLGEYYLQNA FLVAYTKKAP QLTPPELMAF TRKMATAAAT CCQLSEDRQL ACGEGAADLI
IGQLCIRHEE TPINPGVGQC CSSSYANRRP CFSSLVVDET YIPSPFSADK FIFHKDLCQA
QGVALQTMKQ QFLINLVKQK PQITEEQLEA VIADFSGLLE KCCQGQEQEA CFEEEGPKLI
SKTRAALGV
