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 02-OCT-2024, entry version 195. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NUCLEOTIDE SEQUENCE [MRNA] OF RP 157-496. RX PubMed=2246248; DOI=10.1016/s0021-9258(17)45417-2; 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 cartilage RT 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., 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., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., 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., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., 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 collagen. CC -!- SUBUNIT: Homotrimer. Interacts with COMP. CC {ECO:0000269|PubMed:15075323}. CC -!- INTERACTION: CC P21941; P02459: COL2A1; Xeno; NbExp=3; IntAct=EBI-20828128, EBI-5281315; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; P21941; -. DR SMR; P21941; -. DR BioGRID; 110316; 14. DR ComplexPortal; CPX-4423; Matrilin-1 complex. DR ComplexPortal; CPX-4503; Matrilin-1 - Matrilin-3 complex. DR IntAct; P21941; 7. DR STRING; 9606.ENSP00000362870; -. DR GlyCosmos; P21941; 1 site, No reported glycans. DR GlyGen; P21941; 1 site. DR iPTMnet; P21941; -. DR PhosphoSitePlus; P21941; -. DR BioMuta; MATN1; -. DR DMDM; 115556; -. DR MassIVE; P21941; -. DR PaxDb; 9606-ENSP00000362870; -. DR PeptideAtlas; P21941; -. DR ProteomicsDB; 53943; -. DR Antibodypedia; 31055; 241 antibodies from 31 providers. DR DNASU; 4146; -. DR Ensembl; ENST00000373765.5; ENSP00000362870.4; ENSG00000162510.6. DR GeneID; 4146; -. DR KEGG; hsa:4146; -. DR MANE-Select; ENST00000373765.5; ENSP00000362870.4; NM_002379.3; NP_002370.1. DR UCSC; uc001brz.4; human. DR AGR; HGNC:6907; -. DR CTD; 4146; -. DR DisGeNET; 4146; -. DR GeneCards; MATN1; -. DR HGNC; HGNC:6907; MATN1. DR HPA; ENSG00000162510; Tissue enriched (retina). DR MIM; 115437; gene. DR neXtProt; NX_P21941; -. DR OpenTargets; ENSG00000162510; -. DR PharmGKB; PA30650; -. DR VEuPathDB; HostDB:ENSG00000162510; -. DR eggNOG; KOG1217; Eukaryota. DR GeneTree; ENSGT00940000159638; -. DR HOGENOM; CLU_008905_7_0_1; -. DR InParanoid; P21941; -. DR OMA; ICIEEDP; -. DR OrthoDB; 1453590at2759; -. DR PhylomeDB; P21941; -. DR TreeFam; TF330078; -. DR PathwayCommons; P21941; -. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR SignaLink; P21941; -. DR BioGRID-ORCS; 4146; 13 hits in 1142 CRISPR screens. DR GeneWiki; MATN1; -. DR GenomeRNAi; 4146; -. DR Pharos; P21941; Tbio. DR PRO; PR:P21941; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P21941; protein. DR Bgee; ENSG00000162510; Expressed in cartilage tissue and 122 other cell types or tissues. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central. DR GO; GO:0031012; C:extracellular matrix; TAS:ProtInc. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0120216; C:matrilin complex; ISO:ComplexPortal. 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; NAS:ComplexPortal. DR GO; GO:0003429; P:growth plate cartilage chondrocyte morphogenesis; IEA:Ensembl. DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc. DR GO; GO:0030500; P:regulation of bone mineralization; IEA:Ensembl. DR CDD; cd01475; vWA_Matrilin; 2. DR Gene3D; 1.20.5.30; -; 1. DR Gene3D; 2.10.25.10; Laminin; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 2. DR InterPro; IPR050525; ECM_Assembly_Org. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. 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; CARTILAGE MATRIX PROTEIN; 1. DR PANTHER; PTHR24020; COLLAGEN ALPHA; 1. DR Pfam; PF14670; FXa_inhibition; 1. DR Pfam; PF10393; Matrilin_ccoil; 1. DR Pfam; PF00092; VWA; 2. DR PRINTS; PR00453; VWFADOMAIN. DR SMART; SM00181; EGF; 1. DR SMART; SM00179; EGF_CA; 1. DR SMART; SM01279; Matrilin_ccoil; 1. DR SMART; SM00327; VWA; 2. DR SUPFAM; SSF58002; Chicken cartilage matrix protein; 1. DR SUPFAM; SSF53300; vWA-like; 2. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50234; VWFA; 2. PE 1: Evidence at protein level; KW Coiled coil; Disulfide bond; EGF-like domain; Extracellular matrix; KW Glycoprotein; Proteomics identification; Reference proteome; Repeat; KW Secreted; Signal. FT SIGNAL 1..22 FT CHAIN 23..496 FT /note="Cartilage matrix protein" FT /id="PRO_0000007495" FT DOMAIN 23..222 FT /note="VWFA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 223..263 FT /note="EGF-like" FT DOMAIN 264..453 FT /note="VWFA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT COILED 467..495 FT /evidence="ECO:0000255" FT CARBOHYD 76 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 35..221 FT /evidence="ECO:0000255" FT DISULFID 227..238 FT /evidence="ECO:0000250" FT DISULFID 234..247 FT /evidence="ECO:0000250" FT DISULFID 249..262 FT /evidence="ECO:0000250" FT DISULFID 265..452 FT /evidence="ECO:0000255" FT CONFLICT 291 FT /note="F -> L (in Ref. 1; AAA63904)" FT /evidence="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 //