ID MATN4_HUMAN Reviewed; 622 AA. AC O95460; A6NH94; A6NKN5; Q5QPU2; Q5QPU3; Q5QPU4; Q8N2M5; Q8N2M7; Q9H1F8; AC Q9H1F9; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 3. DT 02-OCT-2024, entry version 207. DE RecName: Full=Matrilin-4; DE Flags: Precursor; GN Name=MATN4; 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 [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING. RC TISSUE=Embryonic kidney; RX PubMed=9827539; DOI=10.1016/s0014-5793(98)01293-9; RA Wagener R., Kobbe B., Paulsson M.; RT "Genomic organisation, alternative splicing and primary structure of human RT matrilin-4."; RL FEBS Lett. 438:165-170(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT SER-164. RC TISSUE=Embryo; 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=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). 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: Major component of the extracellular matrix of cartilage. CC -!- SUBUNIT: Interacts with COMP. {ECO:0000269|PubMed:15075323}. CC -!- INTERACTION: CC O95460-2; Q4G176: ACSF3; NbExp=3; IntAct=EBI-12072296, EBI-10714818; CC O95460-2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-12072296, EBI-744099; CC O95460-2; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-12072296, EBI-739467; CC O95460-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12072296, EBI-741158; CC O95460-2; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-12072296, EBI-1105153; CC O95460-2; O00560: SDCBP; NbExp=3; IntAct=EBI-12072296, EBI-727004; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=O95460-1; Sequence=Displayed; CC Name=2; CC IsoId=O95460-2; Sequence=VSP_001400; CC Name=3; CC IsoId=O95460-3; Sequence=VSP_015255; CC Name=4; CC IsoId=O95460-4; Sequence=VSP_001400, VSP_015256; CC -!- TISSUE SPECIFICITY: Embryonic kidney, lung and placenta. CC -!- SEQUENCE CAUTION: CC Sequence=BAC11081.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AJ007581; CAA07569.1; -; mRNA. DR EMBL; AK074595; BAC11081.1; ALT_INIT; mRNA. DR EMBL; AK074597; BAC11083.1; -; mRNA. DR EMBL; AL021578; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS13348.1; -. [O95460-2] DR CCDS; CCDS46607.1; -. [O95460-4] DR RefSeq; NP_085080.1; NM_030590.3. [O95460-4] DR RefSeq; NP_085095.1; NM_030592.3. DR RefSeq; XP_005260654.1; XM_005260597.1. DR AlphaFoldDB; O95460; -. DR SMR; O95460; -. DR BioGRID; 114313; 36. DR ComplexPortal; CPX-4641; Matrilin-4 complex. DR IntAct; O95460; 19. DR STRING; 9606.ENSP00000361842; -. DR GlyConnect; 1493; 6 N-Linked glycans (1 site). DR GlyCosmos; O95460; 3 sites, 6 glycans. DR GlyGen; O95460; 3 sites, 6 N-linked glycans (1 site). DR iPTMnet; O95460; -. DR PhosphoSitePlus; O95460; -. DR BioMuta; MATN4; -. DR jPOST; O95460; -. DR MassIVE; O95460; -. DR PeptideAtlas; O95460; -. DR ProteomicsDB; 50892; -. [O95460-1] DR ProteomicsDB; 50893; -. [O95460-2] DR ProteomicsDB; 50894; -. [O95460-3] DR ProteomicsDB; 50895; -. [O95460-4] DR Antibodypedia; 27542; 142 antibodies from 28 providers. DR DNASU; 8785; -. DR Ensembl; ENST00000360607.10; ENSP00000353819.5; ENSG00000124159.17. [O95460-4] DR Ensembl; ENST00000372754.5; ENSP00000361840.1; ENSG00000124159.17. [O95460-1] DR Ensembl; ENST00000372756.6; ENSP00000361842.1; ENSG00000124159.17. [O95460-2] DR Ensembl; ENST00000537548.3; ENSP00000440328.1; ENSG00000124159.17. [O95460-2] DR GeneID; 8785; -. DR KEGG; hsa:8785; -. DR MANE-Select; ENST00000372756.6; ENSP00000361842.1; NM_001393530.1; NP_001380459.1. [O95460-2] DR UCSC; uc002xno.4; human. [O95460-1] DR AGR; HGNC:6910; -. DR CTD; 8785; -. DR DisGeNET; 8785; -. DR GeneCards; MATN4; -. DR HGNC; HGNC:6910; MATN4. DR HPA; ENSG00000124159; Tissue enriched (pancreas). DR MIM; 603897; gene. DR neXtProt; NX_O95460; -. DR OpenTargets; ENSG00000124159; -. DR PharmGKB; PA30653; -. DR VEuPathDB; HostDB:ENSG00000124159; -. DR eggNOG; KOG1217; Eukaryota. DR GeneTree; ENSGT00940000157086; -. DR InParanoid; O95460; -. DR OMA; DKRSCSM; -. DR OrthoDB; 1453590at2759; -. DR PhylomeDB; O95460; -. DR TreeFam; TF330078; -. DR PathwayCommons; O95460; -. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR SignaLink; O95460; -. DR BioGRID-ORCS; 8785; 12 hits in 1144 CRISPR screens. DR GenomeRNAi; 8785; -. DR Pharos; O95460; Tdark. DR PRO; PR:O95460; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; O95460; protein. DR Bgee; ENSG00000124159; Expressed in cartilage tissue and 70 other cell types or tissues. DR ExpressionAtlas; O95460; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:ComplexPortal. 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:0030198; P:extracellular matrix organization; NAS:ComplexPortal. DR CDD; cd00054; EGF_CA; 1. DR Gene3D; 1.20.5.30; -; 1. DR Gene3D; 2.10.25.10; Laminin; 4. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 2. DR InterPro; IPR026823; cEGF. DR InterPro; IPR050525; ECM_Assembly_Org. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. 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; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24020:SF14; MATRILIN-4; 1. DR Pfam; PF12662; cEGF; 1. DR Pfam; PF14670; FXa_inhibition; 2. DR Pfam; PF10393; Matrilin_ccoil; 1. DR Pfam; PF00092; VWA; 2. DR PRINTS; PR00453; VWFADOMAIN. DR SMART; SM00181; EGF; 4. DR SMART; SM00179; EGF_CA; 4. DR SMART; SM01279; Matrilin_ccoil; 1. DR SMART; SM00327; VWA; 2. DR SUPFAM; SSF58002; Chicken cartilage matrix protein; 1. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR SUPFAM; SSF53300; vWA-like; 2. DR PROSITE; PS00010; ASX_HYDROXYL; 2. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 3. DR PROSITE; PS50234; VWFA; 2. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Disulfide bond; EGF-like domain; KW Glycoprotein; Proteomics identification; Reference proteome; Repeat; KW Secreted; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000250" FT CHAIN 19..622 FT /note="Matrilin-4" FT /id="PRO_0000007660" FT DOMAIN 34..213 FT /note="VWFA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 215..255 FT /note="EGF-like 1; incomplete" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 256..292 FT /note="EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 297..337 FT /note="EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 342..377 FT /note="EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 386..561 FT /note="VWFA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT COILED 591..622 FT /evidence="ECO:0000255" FT CARBOHYD 69 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 251 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 305 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 219..230 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 226..239 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 241..254 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 260..271 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 267..280 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 282..295 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 301..312 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 308..321 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 323..336 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 342..353 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 349..362 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 364..377 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT VAR_SEQ 25..214 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_015255" FT VAR_SEQ 215..255 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:9827539" FT /id="VSP_001400" FT VAR_SEQ 256..296 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_015256" FT VARIANT 13 FT /note="L -> F (in dbSNP:rs2743307)" FT /id="VAR_055758" FT VARIANT 164 FT /note="R -> S (in dbSNP:rs2072788)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_055759" FT CONFLICT 173 FT /note="V -> L (in Ref. 2; BAC11083)" FT /evidence="ECO:0000305" FT CONFLICT 563 FT /note="G -> S (in Ref. 2; BAC11083)" FT /evidence="ECO:0000305" SQ SEQUENCE 622 AA; 68487 MW; 283C32AF7EA58C68 CRC64; MRGLLCWPVL LLLLQPWETQ LQLTGPRCHT GPLDLVFVID SSRSVRPFEF ETMRQFLMGL LRGLNVGPNA TRVGVIQYSS QVQSVFPLRA FSRREDMERA IRDLVPLAQG TMTGLAIQYA MNVAFSVAEG ARPPEERVPR VAVIVTDGRP QDRVAEVAAQ ARARGIEIYA VGVQRADVGS LRAMASPPLD EHVFLVESFD LIQEFGLQFQ SRLCGKDQCA EGGHGCQHQC VNAWAMFHCT CNPGYKLAAD NKSCLAIDLC AEGTHGCEHH CVNSPGSYFC HCQVGFVLQQ DQRSCRAIDY CSFGNHSCQH ECVSTPGGPR CHCREGHDLQ PDGRSCQVRD LCNGVDHGCE FQCVSEGLSY RCLCPEGRQL QADGKSCNRC REGHVDLVLL VDGSKSVRPQ NFELVKRFVN QIVDFLDVSP EGTRVGLVQF SSRVRTEFPL GRYGTAAEVK QAVLAVEYME RGTMTGLALR HMVEHSFSEA QGARPRALNV PRVGLVFTDG RSQDDISVWA ARAKEEGIVM YAVGVGKAVE AELREIASEP AELHVSYAPD FGTMTHLLEN LRGSICPEEG ISAGTELRSP CECESLVEFQ GRTLGALESL TLNLAQLTAR LEDLENQLAN QK //