FETUA_MOUSE
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 03-AUG-2022, entry version 169.
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, Pancreas,
RC 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 GlyGen; P29699; 3 sites, 2 N-linked glycans (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; P29699; -.
DR PeptideAtlas; P29699; -.
DR PRIDE; P29699; -.
DR ProteomicsDB; 271742; -.
DR Antibodypedia; 870; 673 antibodies from 41 providers.
DR DNASU; 11625; -.
DR Ensembl; ENSMUST00000023583; ENSMUSP00000023583; ENSMUSG00000022868.
DR GeneID; 11625; -.
DR KEGG; mmu:11625; -.
DR UCSC; uc007ysr.2; mouse.
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; VRKVCPQ; -.
DR OrthoDB; 913381at2759; -.
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 75 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 67 other tissues.
DR ExpressionAtlas; P29699; baseline and differential.
DR Genevisible; P29699; MM.
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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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 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..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
