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   27-MAR-2024, entry version 192.
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.
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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; 4.
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; 243 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; 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.
DR   Genevisible; P21941; HS.
PE   1: Evidence at protein level;
KW   Coiled coil; Disulfide bond; EGF-like domain; Extracellular matrix;
KW   Glycoprotein; Reference proteome; Repeat; 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
//