MATN1_HUMAN
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 03-AUG-2022, entry version 183.
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 GlyGen; P21941; 1 site.
DR iPTMnet; P21941; -.
DR PhosphoSitePlus; P21941; -.
DR BioMuta; MATN1; -.
DR DMDM; 115556; -.
DR MassIVE; P21941; -.
DR PaxDb; P21941; -.
DR PeptideAtlas; P21941; -.
DR PRIDE; P21941; -.
DR ProteomicsDB; 53943; -.
DR Antibodypedia; 31055; 224 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 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; NTWVFAA; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; P21941; -.
DR TreeFam; TF330078; -.
DR PathwayCommons; P21941; -.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR SignaLink; P21941; -.
DR BioGRID-ORCS; 4146; 12 hits in 1064 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 121 other tissues.
DR Genevisible; P21941; HS.
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: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; IC: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 Gene3D; 1.20.5.30; -; 1.
DR Gene3D; 3.40.50.410; -; 2.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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; PTHR24020:SF16; PTHR24020:SF16; 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; 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
