FETUA_PANTR
ID FETUA_PANTR Reviewed; 367 AA.
AC Q9N2D0;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Alpha-2-HS-glycoprotein;
DE AltName: Full=Fetuin-A;
DE Contains:
DE RecName: Full=Alpha-2-HS-glycoprotein chain A;
DE Contains:
DE RecName: Full=Alpha-2-HS-glycoprotein chain B;
DE Flags: Precursor;
GN Name=AHSG; Synonyms=FETUA;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11415520; DOI=10.1046/j.1469-1809.2001.6510027.x;
RA Osawa M., Yuasa I., Kitano T., Henke J., Kaneko M., Udono T., Saitou N.,
RA Umetsu K.;
RT "Haplotype analysis of the human alpha2-HS glycoprotein (fetuin) gene.";
RL Ann. Hum. Genet. 65:27-34(2001).
CC -!- FUNCTION: Promotes endocytosis, possesses opsonic properties and
CC influences the mineral phase of bone. Shows affinity for calcium and
CC barium ions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Alpha-2-HS glycoprotein derives from this precursor, when the
CC connecting peptide is cleaved off. The two chains A and B are held
CC together by a single disulfide bond (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P02765}.
CC -!- SIMILARITY: Belongs to the fetuin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00861}.
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DR EMBL; AB038690; BAA92190.1; -; Genomic_DNA.
DR RefSeq; NP_001009098.1; NM_001009098.1.
DR AlphaFoldDB; Q9N2D0; -.
DR SMR; Q9N2D0; -.
DR STRING; 9598.ENSPTRP00000027036; -.
DR MEROPS; I25.020; -.
DR MEROPS; I25.021; -.
DR PaxDb; Q9N2D0; -.
DR PRIDE; Q9N2D0; -.
DR GeneID; 460912; -.
DR KEGG; ptr:460912; -.
DR CTD; 197; -.
DR eggNOG; ENOG502RYRI; Eukaryota.
DR HOGENOM; CLU_052519_0_0_1; -.
DR InParanoid; Q9N2D0; -.
DR OrthoDB; 913381at2759; -.
DR TreeFam; TF333729; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0006953; P:acute-phase response; ISS:UniProtKB.
DR GO; GO:0030502; P:negative regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR CDD; cd00042; CY; 2.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR025760; Cystatin_Fetuin_A.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR001363; Prot_inh_fetuin_CS.
DR Pfam; PF00031; Cystatin; 1.
DR SMART; SM00043; CY; 2.
DR SUPFAM; SSF54403; SSF54403; 2.
DR PROSITE; PS51529; CYSTATIN_FETUIN_A; 2.
DR PROSITE; PS01254; FETUIN_1; 1.
DR PROSITE; PS01255; FETUIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Mineral balance; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..300
FT /note="Alpha-2-HS-glycoprotein chain A"
FT /id="PRO_0000008892"
FT PROPEP 301..340
FT /note="Connecting peptide"
FT /id="PRO_0000008893"
FT CHAIN 341..367
FT /note="Alpha-2-HS-glycoprotein chain B"
FT /id="PRO_0000008894"
FT DOMAIN 27..133
FT /note="Cystatin fetuin-A-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DOMAIN 144..255
FT /note="Cystatin fetuin-A-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT REGION 254..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..293
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P12763"
FT DISULFID 32..358
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 89..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 114..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 146..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 208..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 230..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
SQ SEQUENCE 367 AA; 39444 MW; 2FCB2FC5BDE5FE4E CRC64;
MKSLVLLLCL AQLWGCHSAP RGLGLIYRQP NCDDPETEEA ALVAIDYINQ NHPWGYKHTL
NQIDEVKVWP RQPSGELFEI EIDTLETTCH VLDPTPVARC SVRQLKEHAV EGDCDFQLLK
LDGKFSVVYA KCDSSPDSAE DVRKVCQDCP LLAPLNDTRV VHAAKAALAA FNAQNNGSNF
QLEEISRAQL VPLPPSTYVE FTVSGTDCVA KEATEAAKCN LLAEKQYGFC KATLSEKLGG
AEVAVTCTVF QTQPVTSQPQ PEGANETVPT PVVDPDAPPS PPLGAPGLPP AGSPPDSHVL
LAAPPGHQLH WAHYDLRHTF MGVVSLGSPS GEASHPRKTR TVVQPSVGAA AGPVVPPCPG
RIRHFKV
