ID   FETUA_MERUN             Reviewed;         348 AA.
AC   P97515;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Alpha-2-HS-glycoprotein;
DE   AltName: Full=Countertrypin;
DE   AltName: Full=Fetuin-A;
DE   Flags: Precursor;
GN   Name=AHSG; Synonyms=FETUA;
OS   Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Gerbillinae; Meriones.
OX   NCBI_TaxID=10047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-38.
RC   TISSUE=Liver;
RX   PubMed=9133634; DOI=10.1093/oxfordjournals.jbchem.a021630;
RA   Goto K., Yoshida K., Suzuki Y., Yamamoto K., Sinohara H.;
RT   "Molecular cloning and sequencing of cDNA encoding plasma countertrypin, a
RT   member of mammalian fetuin family, from the Mongolian gerbil, Meriones
RT   unguiculatus.";
RL   J. Biochem. 121:619-625(1997).
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; D88777; BAA13702.1; -; mRNA.
DR   PIR; JC5431; JC5431.
DR   AlphaFoldDB; P97515; -.
DR   SMR; P97515; -.
DR   MEROPS; I25.020; -.
DR   PRIDE; P97515; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
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   Repeat; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:9133634"
FT   CHAIN           19..348
FT                   /note="Alpha-2-HS-glycoprotein"
FT                   /id="PRO_0000008890"
FT   DOMAIN          19..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   MOD_RES         134
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         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24090"
FT   MOD_RES         311
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02765"
FT   MOD_RES         314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02765"
FT   MOD_RES         316
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..339
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   348 AA;  37375 MW;  62717A0F0DB2C6B1 CRC64;
     MKTLVLLLCF TLLWGCQSAP QGTGLGFREV ACDDPEVEQV ALTAVDYLNQ HLLQGFKHIL
     NQIDKVKVWS RRPFGEVYEL ELDTLETTCH ALDPTPLANC SVRQLAQHAV EGDCDFHILK
     QDGQFSVMHT KCHSNPDSAE DVRKVCPHCA LLTPFNSSNV VYAVNAALGA FNEKNNKTYF
     KLVELARAQT VPFPPSTHVE FVIAATDCAA PKVADPAKCN LLAEKQYSFC KASLFQNLGG
     EEVTVTCTAF PTQANGVTPA SPAPAVEKGI PVALPDAPPA SLVVGPMVVP AEHLPHKTHH
     DLRHAFSPVA SVESASGEAF QSPTQAGNAG AAGPAVPLCP GRVRHFKI