ID   FETUA_MOUSE             Reviewed;         345 AA.
AC   P29699; O35634;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 178.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=1373325; DOI=10.1016/0167-4781(92)90522-2;
RA   Yang F., Chen Z.-L., Bergeron J.M., Cupples R.L., Friedrichs W.E.;
RT   "Human alpha 2-HS-glycoprotein/bovine fetuin homologue in mice:
RT   identification and developmental regulation of the gene.";
RL   Biochim. Biophys. Acta 1130:149-156(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=9395485; DOI=10.1074/jbc.272.50.31496;
RA   Jahnen-Dechent W., Schinke T., Trindl A., Mueller-Esterl W., Sablitzky F.,
RA   Kaiser S., Blessing M.;
RT   "Cloning and targeted deletion of the mouse fetuin gene.";
RL   J. Biol. Chem. 272:31496-31503(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=7688730; DOI=10.1016/s0021-9258(17)46768-8;
RA   Yamamoto K., Sinohara H.;
RT   "Isolation and characterization of mouse countertrypin, a new trypsin
RT   inhibitor belonging to the mammalian fetuin family.";
RL   J. Biol. Chem. 268:17750-17753(1993).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-176.
RC   STRAIN=C57BL/6J; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-99; ASN-156 AND ASN-176.
RC   STRAIN=C57BL/6J; TISSUE=Plasma;
RX   PubMed=17330941; DOI=10.1021/pr0604559;
RA   Bernhard O.K., Kapp E.A., Simpson R.J.;
RT   "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT   tryptic glycopeptides.";
RL   J. Proteome Res. 6:987-995(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-309; SER-312 AND
RP   SER-314, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-309; SER-312 AND
RP   SER-314, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135; SER-138; SER-309;
RP   SER-312 AND SER-314, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Probably involved in differentiation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Liver is the major site of synthesis, but fetuin is
CC       also expressed in limb buds and other extrahepatic tissues during
CC       development.
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; S96534; AAB22070.1; -; mRNA.
DR   EMBL; AF007900; AAB81718.1; -; Genomic_DNA.
DR   EMBL; AJ002146; CAA05210.1; -; Genomic_DNA.
DR   EMBL; BC012678; AAH12678.1; -; mRNA.
DR   EMBL; BC019822; AAH19822.1; -; mRNA.
DR   CCDS; CCDS28071.1; -.
DR   PIR; S21094; S21094.
DR   RefSeq; NP_038493.1; NM_013465.2.
DR   AlphaFoldDB; P29699; -.
DR   SMR; P29699; -.
DR   BioGRID; 198039; 10.
DR   IntAct; P29699; 3.
DR   STRING; 10090.ENSMUSP00000023583; -.
DR   MEROPS; I25.020; -.
DR   MEROPS; I25.021; -.
DR   GlyConnect; 729; 1 N-Linked glycan (1 site).
DR   GlyCosmos; P29699; 3 sites, 2 glycans.
DR   GlyGen; P29699; 4 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P29699; -.
DR   PhosphoSitePlus; P29699; -.
DR   SwissPalm; P29699; -.
DR   REPRODUCTION-2DPAGE; IPI00128249; -.
DR   CPTAC; non-CPTAC-3578; -.
DR   jPOST; P29699; -.
DR   PaxDb; 10090-ENSMUSP00000023583; -.
DR   PeptideAtlas; P29699; -.
DR   ProteomicsDB; 271742; -.
DR   Antibodypedia; 870; 723 antibodies from 41 providers.
DR   DNASU; 11625; -.
DR   Ensembl; ENSMUST00000023583.7; ENSMUSP00000023583.6; ENSMUSG00000022868.7.
DR   GeneID; 11625; -.
DR   KEGG; mmu:11625; -.
DR   UCSC; uc007ysr.2; mouse.
DR   AGR; MGI:107189; -.
DR   CTD; 197; -.
DR   MGI; MGI:107189; Ahsg.
DR   VEuPathDB; HostDB:ENSMUSG00000022868; -.
DR   eggNOG; ENOG502RYRI; Eukaryota.
DR   GeneTree; ENSGT00950000182930; -.
DR   HOGENOM; CLU_052519_0_0_1; -.
DR   InParanoid; P29699; -.
DR   OMA; KVWPRQP; -.
DR   OrthoDB; 5312104at2759; -.
DR   PhylomeDB; P29699; -.
DR   TreeFam; TF333729; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR   BioGRID-ORCS; 11625; 1 hit in 80 CRISPR screens.
DR   ChiTaRS; Ahsg; mouse.
DR   PRO; PR:P29699; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P29699; Protein.
DR   Bgee; ENSMUSG00000022868; Expressed in left lobe of liver and 69 other cell types or tissues.
DR   ExpressionAtlas; P29699; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
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:0030294; F:receptor signaling protein tyrosine kinase inhibitor activity; ISO:MGI.
DR   GO; GO:0006953; P:acute-phase response; ISS:UniProtKB.
DR   GO; GO:0008584; P:male gonad development; ISO:MGI.
DR   GO; GO:0030502; P:negative regulation of bone mineralization; IDA:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR   GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR   GO; GO:0001503; P:ossification; IDA:MGI.
DR   GO; GO:0045780; P:positive regulation of bone resorption; ISO:MGI.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR   CDD; cd00042; CY; 2.
DR   Gene3D; 3.10.450.10; -; 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   PANTHER; PTHR13814:SF6; ALPHA-2-HS-GLYCOPROTEIN; 1.
DR   PANTHER; PTHR13814; FETUIN; 1.
DR   Pfam; PF00031; Cystatin; 1.
DR   SMART; SM00043; CY; 2.
DR   SUPFAM; SSF54403; Cystatin/monellin; 2.
DR   PROSITE; PS51529; CYSTATIN_FETUIN_A; 2.
DR   PROSITE; PS01254; FETUIN_1; 1.
DR   PROSITE; PS01255; FETUIN_2; 1.
DR   Genevisible; P29699; MM.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Phosphoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..345
FT                   /note="Alpha-2-HS-glycoprotein"
FT                   /id="PRO_0000008891"
FT   DOMAIN          19..133
FT                   /note="Cystatin fetuin-A-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DOMAIN          144..250
FT                   /note="Cystatin fetuin-A-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   REGION          312..334
FT                   /note="Disordered"
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:0007744|PubMed:21183079"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT   MOD_RES         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24090"
FT   MOD_RES         309
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT   MOD_RES         312
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT   MOD_RES         314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17330941"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17330941"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16944957,
FT                   ECO:0000269|PubMed:17330941"
FT   DISULFID        32..336
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"
FT   CONFLICT        71
FT                   /note="R -> RQ (in Ref. 2; CAA05210)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   345 AA;  37326 MW;  4B7B9C9B1410658E CRC64;
     MKSLVLLLCF AQLWGCQSAP QGTGLGFREL ACDDPEAEQV ALLAVDYLNN HLLQGFKQVL
     NQIDKVKVWS RRPFGVVYEM EVDTLETTCH ALDPTPLANC SVRQLTEHAV EGDCDFHILK
     QDGQFRVMHT QCHSTPDSAE DVRKLCPRCP LLTPFNDTNV VHTVNTALAA FNTQNNGTYF
     KLVEISRAQN VPLPVSTLVE FVIAATDCTA KEVTDPAKCN LLAEKQHGFC KANLMHNLGG
     EEVSVACKLF QTQPQPANAN AVGPVPTANA ALPADPPASV VVGPVVVPRG LSDHRTYHDL
     RHAFSPVASV ESASGETLHS PKVGQPGAAG PVSPMCPGRI RHFKI
//