GenomeNet

Database: UniProt
Entry: P21941
LinkDB: P21941
Original site: P21941 
ID   MATN1_HUMAN             Reviewed;         496 AA.
AC   P21941; B2R7E3; Q5TBB9;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   13-FEB-2019, entry version 164.
DE   RecName: Full=Cartilage matrix protein;
DE   AltName: Full=Matrilin-1;
DE   Flags: Precursor;
GN   Name=MATN1; Synonyms=CMP, CRTM;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP   157-496.
RX   PubMed=2246248;
RA   Jenkins R.N., Osborne-Lawrence S.L., Sinclair A.K., Eddy R.L. Jr.,
RA   Byers M.G., Shows T.B., Duby A.D.;
RT   "Structure and chromosomal location of the human gene encoding
RT   cartilage matrix protein.";
RL   J. Biol. Chem. 265:19624-19631(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   INTERACTION WITH COMP.
RX   PubMed=15075323; DOI=10.1074/jbc.M403778200;
RA   Mann H.H., Oezbek S., Engel J., Paulsson M., Wagener R.;
RT   "Interactions between the cartilage oligomeric matrix protein and
RT   matrilins. Implications for matrix assembly and the pathogenesis of
RT   chondrodysplasias.";
RL   J. Biol. Chem. 279:25294-25298(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.
CC       {ECO:0000269|PubMed:15075323}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
DR   EMBL; M55682; AAB38702.1; -; Genomic_DNA.
DR   EMBL; M55675; AAB38702.1; JOINED; Genomic_DNA.
DR   EMBL; M55676; AAB38702.1; JOINED; Genomic_DNA.
DR   EMBL; M55677; AAB38702.1; JOINED; Genomic_DNA.
DR   EMBL; M55679; AAB38702.1; JOINED; Genomic_DNA.
DR   EMBL; M55680; AAB38702.1; JOINED; Genomic_DNA.
DR   EMBL; M55681; AAB38702.1; JOINED; Genomic_DNA.
DR   EMBL; M55683; AAA63904.1; -; mRNA.
DR   EMBL; AK312949; BAG35790.1; -; mRNA.
DR   EMBL; AL137857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS336.1; -.
DR   PIR; A37979; A37979.
DR   RefSeq; NP_002370.1; NM_002379.3.
DR   UniGene; Hs.150366; -.
DR   ProteinModelPortal; P21941; -.
DR   SMR; P21941; -.
DR   BioGrid; 110316; 4.
DR   IntAct; P21941; 1.
DR   STRING; 9606.ENSP00000362870; -.
DR   iPTMnet; P21941; -.
DR   PhosphoSitePlus; P21941; -.
DR   BioMuta; MATN1; -.
DR   DMDM; 115556; -.
DR   PaxDb; P21941; -.
DR   PeptideAtlas; P21941; -.
DR   PRIDE; P21941; -.
DR   ProteomicsDB; 53943; -.
DR   DNASU; 4146; -.
DR   Ensembl; ENST00000373765; ENSP00000362870; ENSG00000162510.
DR   GeneID; 4146; -.
DR   KEGG; hsa:4146; -.
DR   UCSC; uc001brz.4; human.
DR   CTD; 4146; -.
DR   DisGeNET; 4146; -.
DR   EuPathDB; HostDB:ENSG00000162510.5; -.
DR   GeneCards; MATN1; -.
DR   H-InvDB; HIX0000347; -.
DR   H-InvDB; HIX0028643; -.
DR   H-InvDB; HIX0029177; -.
DR   HGNC; HGNC:6907; MATN1.
DR   HPA; HPA028580; -.
DR   MIM; 115437; gene.
DR   neXtProt; NX_P21941; -.
DR   OpenTargets; ENSG00000162510; -.
DR   PharmGKB; PA30650; -.
DR   eggNOG; ENOG410IR75; Eukaryota.
DR   eggNOG; ENOG410XSCQ; LUCA.
DR   GeneTree; ENSGT00940000159638; -.
DR   HOGENOM; HOG000263415; -.
DR   HOVERGEN; HBG056906; -.
DR   InParanoid; P21941; -.
DR   OMA; NTWVFAA; -.
DR   OrthoDB; 1174178at2759; -.
DR   PhylomeDB; P21941; -.
DR   TreeFam; TF330078; -.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   GeneWiki; MATN1; -.
DR   GenomeRNAi; 4146; -.
DR   PRO; PR:P21941; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000162510; Expressed in 84 organ(s), highest expression level in tibia.
DR   Genevisible; P21941; HS.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
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; TAS:ProtInc.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0003429; P:growth plate cartilage chondrocyte morphogenesis; IBA:GO_Central.
DR   GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR   GO; GO:0030500; P:regulation of bone mineralization; IEA:Ensembl.
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   1: Evidence at protein level;
KW   Coiled coil; Complete proteome; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     22
FT   CHAIN        23    496       Cartilage matrix protein.
FT                                /FTId=PRO_0000007495.
FT   DOMAIN       23    222       VWFA 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN      223    263       EGF-like.
FT   DOMAIN      264    453       VWFA 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   COILED      467    495       {ECO:0000255}.
FT   CARBOHYD     76     76       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     35    221       {ECO:0000255}.
FT   DISULFID    227    238       {ECO:0000250}.
FT   DISULFID    234    247       {ECO:0000250}.
FT   DISULFID    249    262       {ECO:0000250}.
FT   DISULFID    265    452       {ECO:0000255}.
FT   CONFLICT    291    291       F -> L (in Ref. 1; AAA63904).
FT                                {ECO:0000305}.
SQ   SEQUENCE   496 AA;  53701 MW;  2D880A8114C7940F CRC64;
     MRVLSGTSLM LCSLLLLLQA LCSPGLAPQS RGHLCRTRPT DLVFVVDSSR SVRPVEFEKV
     KVFLSQVIES LDVGPNATRV GMVNYASTVK QEFSLRAHVS KAALLQAVRR IQPLSTGTMT
     GLAIQFAITK AFGDAEGGRS RSPDISKVVI VVTDGRPQDS VQDVSARARA SGVELFAIGV
     GSVDKATLRQ IASEPQDEHV DYVESYSVIE KLSRKFQEAF CVVSDLCATG DHDCEQVCIS
     SPGSYTCACH EGFTLNSDGK TCNVCSGGGG SSATDLVFLI DGSKSVRPEN FELVKKFISQ
     IVDTLDVSDK LAQVGLVQYS SSVRQEFPLG RFHTKKDIKA AVRNMSYMEK GTMTGAALKY
     LIDNSFTVSS GARPGAQKVG IVFTDGRSQD YINDAAKKAK DLGFKMFAVG VGNAVEDELR
     EIASEPVAEH YFYTADFKTI NQIGKKLQKK ICVEEDPCAC ESLVKFQAKV EGLLQALTRK
     LEAVSKRLAI LENTVV
//
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