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Database: UniProt
Entry: P51942
LinkDB: P51942
Original site: P51942 
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   13-FEB-2019, entry version 144.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   encoding 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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
CC       collagen.
CC   -!- SUBUNIT: Homotrimer. Interacts with COMP (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
DR   EMBL; U35035; AAB06521.1; -; mRNA.
DR   EMBL; Y13902; CAC79633.1; -; Genomic_DNA.
DR   EMBL; AL669980; CAM17812.1; -; Genomic_DNA.
DR   EMBL; CU210856; CAQ51562.1; -; 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   UniGene; Mm.271796; -.
DR   ProteinModelPortal; P51942; -.
DR   SMR; P51942; -.
DR   BioGrid; 201320; 1.
DR   IntAct; P51942; 1.
DR   MINT; P51942; -.
DR   STRING; 10090.ENSMUSP00000099636; -.
DR   PhosphoSitePlus; P51942; -.
DR   MaxQB; P51942; -.
DR   PaxDb; P51942; -.
DR   PRIDE; P51942; -.
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   eggNOG; ENOG410KD9M; Eukaryota.
DR   eggNOG; ENOG410XSCQ; LUCA.
DR   GeneTree; ENSGT00940000159638; -.
DR   HOGENOM; HOG000263415; -.
DR   HOVERGEN; HBG056906; -.
DR   InParanoid; P51942; -.
DR   OMA; NTWVFAA; -.
DR   OrthoDB; 1174178at2759; -.
DR   TreeFam; TF330078; -.
DR   Reactome; R-MMU-3000178; ECM proteoglycans.
DR   PRO; PR:P51942; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000040533; Expressed in 82 organ(s), highest expression level in humerus cartilage element.
DR   Genevisible; P51942; MM.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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: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; IPR013032; EGF-like_CS.
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; PTHR44857; PTHR44857; 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; Complete proteome; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     29       {ECO:0000255}.
FT   CHAIN        30    500       Cartilage matrix protein.
FT                                /FTId=PRO_0000007496.
FT   DOMAIN       30    226       VWFA 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN      227    267       EGF-like.
FT   DOMAIN      268    457       VWFA 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   COILED      471    499       {ECO:0000255}.
FT   CARBOHYD     80     80       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    348    348       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     39    225       {ECO:0000255}.
FT   DISULFID    231    242       {ECO:0000250}.
FT   DISULFID    238    251       {ECO:0000250}.
FT   DISULFID    253    266       {ECO:0000250}.
FT   DISULFID    269    456       {ECO:0000255}.
FT   CONFLICT      9      9       F -> S (in Ref. 1; AAB06521).
FT                                {ECO:0000305}.
FT   CONFLICT    184    184       V -> L (in Ref. 1; AAB06521).
FT                                {ECO:0000305}.
FT   CONFLICT    338    338       T -> S (in Ref. 1; AAB06521).
FT                                {ECO:0000305}.
FT   CONFLICT    345    345       A -> R (in Ref. 1; AAB06521).
FT                                {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
//
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