FETUA_PIG
ID FETUA_PIG Reviewed; 362 AA.
AC P29700;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Alpha-2-HS-glycoprotein;
DE AltName: Full=Fetuin-A;
DE Flags: Precursor; Fragment;
GN Name=AHSG; Synonyms=FETUA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=1372866; DOI=10.1111/j.1432-1033.1992.tb16783.x;
RA Brown W.M., Christie D.L., Saunders N.R., Nawratil P., Dziegielewska K.D.,
RA Mueller-Esterl W.;
RT "The nucleotide and deduced amino acid structures of sheep and pig fetuin.
RT Common structural features of the mammalian fetuin family.";
RL Eur. J. Biochem. 205:321-331(1992).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
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; X56021; CAA39498.1; -; mRNA.
DR PIR; S22395; S22395.
DR AlphaFoldDB; P29700; -.
DR SMR; P29700; -.
DR STRING; 9823.ENSSSCP00000012570; -.
DR MEROPS; I25.020; -.
DR MEROPS; I25.021; -.
DR PaxDb; P29700; -.
DR PeptideAtlas; P29700; -.
DR PRIDE; P29700; -.
DR eggNOG; ENOG502RYRI; Eukaryota.
DR InParanoid; P29700; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL <1..15
FT CHAIN 16..362
FT /note="Alpha-2-HS-glycoprotein"
FT /id="PRO_0000008895"
FT DOMAIN 24..130
FT /note="Cystatin fetuin-A-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DOMAIN 141..252
FT /note="Cystatin fetuin-A-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 132
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 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24090"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P12763"
FT DISULFID 29..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 86..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 111..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 143..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 205..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 227..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT NON_TER 1
SQ SEQUENCE 362 AA; 38425 MW; 532648EE434B5686 CRC64;
LILFFCLAQL WGCRAVPHGP ILGYREPACD DVETEQAALA AVDYINKHLP RGYKHTLNQV
DSVKVWPRRP AGEVFDIEID TLETTCHVLD PTPLANCSVR QLTEHAVEGD CDFHVLKQDG
QFSVLFAKCD SSPDSAEDVH KVCPNCPLLA PLNDSRVVHA AESALAAFNA QSNGSYLQLV
EISRAQLVPL SASVSVEFAV AVTDCVAKEA YSPTKCNLLV EKQYGFCKGT VTAKVNEEDV
AVTCTVFQTQ PVVLQPQPAG ADAGATPVVD AAATASPLAD VPAASLVVGP MVVAVPPGIP
PVHRSHYDLR HSFSGVASVE SASGEAFHVG KTPKGAQPSI PAADGSVPVV RPCPGRIRHF
KI
