MATN1_MOUSE
ID MATN1_MOUSE Reviewed; 500 AA.
AC P51942; Q80VN5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cartilage matrix protein;
DE AltName: Full=Matrilin-1;
DE Flags: Precursor;
GN Name=Matn1; Synonyms=Cmp, Crtm;
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 [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Cartilage;
RX PubMed=8665920; DOI=10.1111/j.1432-1033.1996.00970.x;
RA Aszodi A., Hauser N., Studer D., Paulsson M., Hiripi L., Bosze Z.;
RT "Cloning, sequencing and expression analysis of mouse cartilage matrix
RT protein cDNA.";
RL Eur. J. Biochem. 236:970-977(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Aszodi A., Beier D.R., Hiripi L., Bosze Z., Faessler R.;
RT "Sequence, structure and chromosomal localization of Crtm gene encoding
RT mouse cartilage matrix protein.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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).
CC -!- FUNCTION: Cartilage matrix protein is a major component of the
CC extracellular matrix of non-articular cartilage. It binds to collagen.
CC -!- SUBUNIT: Homotrimer. Interacts with COMP (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
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DR EMBL; U35035; AAB06521.1; -; mRNA.
DR EMBL; Y13902; CAC79633.1; -; Genomic_DNA.
DR EMBL; AL669980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU210856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047140; AAH47140.1; -; mRNA.
DR CCDS; CCDS18713.1; -.
DR PIR; S66522; S66522.
DR RefSeq; NP_034899.2; NM_010769.2.
DR AlphaFoldDB; P51942; -.
DR SMR; P51942; -.
DR BioGRID; 201320; 1.
DR ComplexPortal; CPX-4463; Matrilin-1 complex.
DR ComplexPortal; CPX-4504; Matrilin-1 - Matrilin-3 complex.
DR IntAct; P51942; 1.
DR MINT; P51942; -.
DR STRING; 10090.ENSMUSP00000099636; -.
DR GlyGen; P51942; 2 sites.
DR PhosphoSitePlus; P51942; -.
DR MaxQB; P51942; -.
DR PaxDb; P51942; -.
DR PRIDE; P51942; -.
DR ProteomicsDB; 287315; -.
DR Antibodypedia; 31055; 224 antibodies from 31 providers.
DR DNASU; 17180; -.
DR Ensembl; ENSMUST00000102576; ENSMUSP00000099636; ENSMUSG00000040533.
DR GeneID; 17180; -.
DR KEGG; mmu:17180; -.
DR UCSC; uc008uzx.2; mouse.
DR CTD; 4146; -.
DR MGI; MGI:106591; Matn1.
DR VEuPathDB; HostDB:ENSMUSG00000040533; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000159638; -.
DR HOGENOM; CLU_008905_7_0_1; -.
DR InParanoid; P51942; -.
DR OMA; PLGRFNN; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; P51942; -.
DR TreeFam; TF330078; -.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR BioGRID-ORCS; 17180; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Matn1; mouse.
DR PRO; PR:P51942; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P51942; protein.
DR Bgee; ENSMUSG00000040533; Expressed in humerus cartilage element and 84 other tissues.
DR Genevisible; P51942; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IC:ComplexPortal.
DR GO; GO:0003429; P:growth plate cartilage chondrocyte morphogenesis; IMP:MGI.
DR GO; GO:0030500; P:regulation of bone mineralization; IMP:MGI.
DR Gene3D; 1.20.5.30; -; 1.
DR Gene3D; 3.40.50.410; -; 2.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR030751; Matrilin-1.
DR InterPro; IPR036337; Matrilin_cc_sf.
DR InterPro; IPR019466; Matrilin_coiled-coil_trimer.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR24020:SF16; PTHR24020:SF16; 1.
DR Pfam; PF10393; Matrilin_ccoil; 1.
DR Pfam; PF00092; VWA; 2.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM01279; Matrilin_ccoil; 1.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF53300; SSF53300; 2.
DR SUPFAM; SSF58002; SSF58002; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50234; VWFA; 2.
PE 2: Evidence at transcript level;
KW Coiled coil; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..500
FT /note="Cartilage matrix protein"
FT /id="PRO_0000007496"
FT DOMAIN 30..226
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 227..267
FT /note="EGF-like"
FT DOMAIN 268..457
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT COILED 471..499
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..225
FT /evidence="ECO:0000255"
FT DISULFID 231..242
FT /evidence="ECO:0000250"
FT DISULFID 238..251
FT /evidence="ECO:0000250"
FT DISULFID 253..266
FT /evidence="ECO:0000250"
FT DISULFID 269..456
FT /evidence="ECO:0000255"
FT CONFLICT 9
FT /note="F -> S (in Ref. 1; AAB06521)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="V -> L (in Ref. 1; AAB06521)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="T -> S (in Ref. 1; AAB06521)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="A -> R (in Ref. 1; AAB06521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 54421 MW; DD034F293479A882 CRC64;
MKVTSGPAFA LCSLLLLLLL LLQVPDSLSL VPQPRGHLCR TRPTDLVFVV DSSRSVRPVE
FEKVKVFLSQ VIESLDVGPN ATRVGLVNYA STVKPEFPLR AHGSKASLLQ AVRRIQPLST
GTMTGLALQF AITKALSDAE GGRARSPDIS KVVIVVTDGR PQDSVRDVSE RARASGIELF
AIGVGRVDKA TLRQIASEPQ DEHVDYVESY NVIEKLAKKF QEAFCVVSDL CATGDHDCEQ
LCVSSPGSYT CACHEGFTLN SDGKTCNVCR GGGSGSATDL VFLIDGSKSV RPENFELVKK
FINQIVDTLD VSDRLAQVGL VQYSSSIRQE FPLGRFHTKK DIKAAVRNMS YMEKGTMTGA
ALKYLIDNSF TVSSGARPGA QKVGIVFTDG RSQDYINDAA RKAKDLGFKM FAVGVGNAVE
EELREIASEP VADHYFYTAD FKTINQIGKK LQKQICVEED PCACESILKF EAKVEGLLQA
LTRKLEAVSG RLAVLENRII
