FETUA_CAVPO
ID FETUA_CAVPO Reviewed; 358 AA.
AC O70159;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Alpha-2-HS-glycoprotein;
DE AltName: Full=Fetuin-A;
DE Flags: Precursor;
GN Name=AHSG; Synonyms=FETUA;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley; TISSUE=Liver;
RX PubMed=10064143; DOI=10.1515/bc.1999.013;
RA Yoshida K., Suzuki Y., Yamamoto K., Sinohara H.;
RT "cDNA sequencing of guinea pig alpha 2-HS glycoprotein, its expression in
RT various tissues and acute phase expression.";
RL Biol. Chem. 380:95-99(1999).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Bone marrow.
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; AB006443; BAA25304.1; -; mRNA.
DR RefSeq; NP_001166384.1; NM_001172913.1.
DR AlphaFoldDB; O70159; -.
DR SMR; O70159; -.
DR STRING; 10141.ENSCPOP00000000953; -.
DR MEROPS; I25.020; -.
DR MEROPS; I25.021; -.
DR Ensembl; ENSCPOT00000001067; ENSCPOP00000000953; ENSCPOG00000001057.
DR GeneID; 100135479; -.
DR KEGG; cpoc:100135479; -.
DR CTD; 197; -.
DR eggNOG; ENOG502RYRI; Eukaryota.
DR GeneTree; ENSGT00950000182930; -.
DR HOGENOM; CLU_052519_0_0_1; -.
DR InParanoid; O70159; -.
DR OMA; VRKVCPQ; -.
DR OrthoDB; 913381at2759; -.
DR TreeFam; TF333729; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000001057; Expressed in liver and 6 other tissues.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
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:0001503; P:ossification; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Phosphoprotein; Protease inhibitor;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..358
FT /note="Alpha-2-HS-glycoprotein"
FT /id="PRO_0000008886"
FT DOMAIN 27..133
FT /note="Cystatin fetuin-A-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DOMAIN 144..254
FT /note="Cystatin fetuin-A-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT REGION 257..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..281
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="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P29699"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 DISULFID 32..349
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..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 229..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
SQ SEQUENCE 358 AA; 38472 MW; ACCB5942E3032517 CRC64;
MKFFVLFLCL VQLWGCHSTP VVLGLEERNP ACDDPETEAA ALAGVDYLNQ HVRWGYKHVL
NQIDKVRVWP RRPSGEVYEL EFDTLETTCH ALDITPLANC SVRTVTQHAV EGDCDMHVLK
QDGQFSVVFA KCESTPDSRE DVRKVCPQCP LLTPVNNTKV VHAANAALAA FNAQNNGSHF
ELLEISRAQL VPLPVSTYVE FAVVATDCAA ADGTDPACSG PPKKQYGFCK ATVAEKLGGE
EVSVTCTVFP TQPVAPLPQP DAASSANPPP AADPAVSPPS SPSVPVDSVA LGPKRVLLPP
PVHREHYNLR YSFPDVDSAS GEAFGPRQKP KVTHPGVASG VGPVPPPPCP GRIRHFKI
