FETUA_SHEEP
ID FETUA_SHEEP Reviewed; 364 AA.
AC P29701;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Alpha-2-HS-glycoprotein;
DE AltName: Full=Fetuin-A;
DE Flags: Precursor;
GN Name=AHSG; Synonyms=FETUA;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 16-23.
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 -!- 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; X16578; CAA34597.1; -; mRNA.
DR PIR; S22394; S22394.
DR RefSeq; NP_001009802.1; NM_001009802.1.
DR AlphaFoldDB; P29701; -.
DR SMR; P29701; -.
DR STRING; 9940.ENSOARP00000022056; -.
DR MEROPS; I25.020; -.
DR MEROPS; I25.021; -.
DR PRIDE; P29701; -.
DR GeneID; 443392; -.
DR KEGG; oas:443392; -.
DR CTD; 197; -.
DR eggNOG; ENOG502RYRI; Eukaryota.
DR OrthoDB; 913381at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
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: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 /note="Or 17"
FT /evidence="ECO:0000269|PubMed:1372866"
FT CHAIN 16..364
FT /note="Alpha-2-HS-glycoprotein"
FT /id="PRO_0000008898"
FT DOMAIN 27..133
FT /note="Cystatin fetuin-A-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DOMAIN 144..256
FT /note="Cystatin fetuin-A-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
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 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24090"
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 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 CARBOHYD 301
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P12763"
FT CARBOHYD 339
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P12763"
FT DISULFID 32..355
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..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT VARIANT 16..17
FT /note="Missing (in 60 to 70% of the chains)"
SQ SEQUENCE 364 AA; 38680 MW; 5046E569789AA7DB CRC64;
MKSFLLLFCL AQLCSCRSIP LDPIAGYKEP ACDDPDTEQA ALAAVDYINK HLPRGYKHTL
NQIDSVKVWP RRPTGEVYDI EIDTLETTCH VLDPTPLVNC SVRQQTEHAV EGDCDIHVLK
QDGQFSVLFT KCDSSPDSAE DVRKLCPDCP LLAPLNNSQV VHAAEVALAT FNAQNNGSYF
QLVEISRAQF VPLPGSVSVE FAVAATDCIA KEVVDPTKCN LLAEKQYGFC KGSVIQKALG
GEDVTVTCTL FQTQPVIPQP QPEGAEAGAP SAVPDAAVPD AAVPAPSAAG LPVGSVVAGP
SVVAVPLPLH RAHYDLRHTF SGVASVESAS GEAFHVGKTP IVGQPSVPGG PVHLCPGRIR
YFKI
