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 18-JUN-2025, entry version 198. DE RecName: Full=Matrilin-1 {ECO:0000312|HGNC:HGNC:6907}; DE AltName: Full=Cartilage matrix protein {ECO:0000303|PubMed:2246248}; DE Flags: Precursor; GN Name=MATN1 {ECO:0000312|HGNC:HGNC:6907}; GN Synonyms=CMP {ECO:0000303|PubMed:2246248}, CRTM GN {ECO:0000250|UniProtKB:P51942}; 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). RN [5] RP INTERACTION WITH TYPE 2 AND TYPE 6 COLLAGENS, GLYCOSYLATION AT ASN-76 AND RP ASN-344, AND MUTAGENESIS OF ASN-76 AND ASN-344. RX PubMed=20729554; DOI=10.1074/jbc.m110.154443; RA Fresquet M., Jowitt T.A., Stephen L.A., Yloestalo J., Briggs M.D.; RT "Structural and functional investigations of Matrilin-1 A-domains reveal RT insights into their role in cartilage ECM assembly."; RL J. Biol. Chem. 285:34048-34061(2010). CC -!- FUNCTION: A major component of the extracellular matrix of non- CC articular cartilage (By similarity). Binds to type 2 collagens and CC forms long concatenated protein networks as part of the extracellular CC matrix (By similarity). Required for the network-like organization and CC bundling of collagen fibrils surrounding chondrocytes in the zones of CC maturation and hypertrophy (By similarity). Required for CC mechanotransduction and adaption to mechanical loading in cartilage CC chondrocytes, resulting in an increase in expression of the CC extracellular matrix components ACAN and COL2A1 (By similarity). Acts CC as a moderator of angiogenesis in response to injury (By similarity). CC {ECO:0000250|UniProtKB:P05099, ECO:0000250|UniProtKB:P51942}. CC -!- SUBUNIT: Homotrimer (By similarity). Part of a complex composed of CC MATN1 (via VWFA1 domain), type 2 collagens and type 6 collagens CC (PubMed:20729554). Forms a complex (via covalent bonds) with ACAN; the CC interaction increases in abundance with increasing age of the organism CC via an increase in occupancy of MATN1 binding sites (By similarity). CC Interacts with COMP (PubMed:15075323). {ECO:0000250|UniProtKB:E1BMV3, CC ECO:0000250|UniProtKB:P05099, ECO:0000269|PubMed:15075323, CC ECO:0000269|PubMed:20729554}. CC -!- INTERACTION: CC P21941; P02459: COL2A1; Xeno; NbExp=3; IntAct=EBI-20828128, EBI-5281315; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000250|UniProtKB:P05099}. CC -!- PTM: N-glycosylated; reduces binding affinity for type 2 collagens. CC {ECO:0000269|PubMed:20729554}. 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 FunCoup; P21941; 95. 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; 219 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; FPLRAHS; -. DR OrthoDB; 6022609at2759; -. DR PAN-GO; P21941; 1 GO annotation based on evolutionary models. 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 FunFam; 1.20.5.30:FF:000003; cartilage matrix protein-like; 1. DR FunFam; 2.10.25.10:FF:000600; cartilage matrix protein-like; 1. DR FunFam; 3.40.50.410:FF:000004; collagen alpha-6(VI) chain; 1. DR FunFam; 3.40.50.410:FF:000018; Matrilin 1; 1. 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="Matrilin-1" 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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" 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:0000269|PubMed:20729554" FT CARBOHYD 344 FT /note="N-linked (GalNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20729554" FT DISULFID 227..238 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 234..247 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 249..262 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT MUTAGEN 76 FT /note="N->A: Abolishes N-glycosylation; no effect on FT protein secretion and increases interaction with type 2 FT collagens." FT /evidence="ECO:0000269|PubMed:20729554" FT MUTAGEN 344 FT /note="N->A: Abolishes N-glycosylation; no effect on FT protein secretion and increases interaction with type 2 FT collagens." FT /evidence="ECO:0000269|PubMed:20729554" 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 //