ID MATN4_HUMAN Reviewed; 622 AA. AC O95460; A6NH94; A6NKN5; Q5QPU2; Q5QPU3; Q5QPU4; Q8N2M5; Q8N2M7; AC Q9H1F8; Q9H1F9; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 3. DT 16-JAN-2019, entry version 176. DE RecName: Full=Matrilin-4; DE Flags: Precursor; GN Name=MATN4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT human matrilin-4."; RL FEBS Lett. 438:165-170(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT RP 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA 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., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA 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 CC cartilage. CC -!- SUBUNIT: Interacts with COMP. {ECO:0000269|PubMed:15075323}. 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 Note=No experimental confirmation available.; CC Name=2; CC IsoId=O95460-2; Sequence=VSP_001400; CC Name=3; CC IsoId=O95460-3; Sequence=VSP_015255; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=O95460-4; Sequence=VSP_001400, VSP_015256; CC Note=No experimental confirmation available.; 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. [O95460-2] DR UniGene; Hs.278489; -. DR ProteinModelPortal; O95460; -. DR SMR; O95460; -. DR BioGrid; 114313; 11. DR IntAct; O95460; 7. DR GlyConnect; 1493; -. DR iPTMnet; O95460; -. DR PhosphoSitePlus; O95460; -. DR BioMuta; MATN4; -. DR EPD; O95460; -. DR jPOST; O95460; -. DR PeptideAtlas; O95460; -. DR PRIDE; O95460; -. DR ProteomicsDB; 50892; -. DR ProteomicsDB; 50893; -. [O95460-2] DR ProteomicsDB; 50894; -. [O95460-3] DR ProteomicsDB; 50895; -. [O95460-4] DR Ensembl; ENST00000360607; ENSP00000353819; ENSG00000124159. [O95460-4] DR Ensembl; ENST00000372754; ENSP00000361840; ENSG00000124159. [O95460-1] DR Ensembl; ENST00000372756; ENSP00000361842; ENSG00000124159. [O95460-2] DR Ensembl; ENST00000537548; ENSP00000440328; ENSG00000124159. [O95460-2] DR GeneID; 8785; -. DR KEGG; hsa:8785; -. DR UCSC; uc002xno.4; human. [O95460-1] DR CTD; 8785; -. DR EuPathDB; HostDB:ENSG00000124159.15; -. DR GeneCards; MATN4; -. DR HGNC; HGNC:6910; MATN4. DR MIM; 603897; gene. DR neXtProt; NX_O95460; -. DR OpenTargets; ENSG00000124159; -. DR PharmGKB; PA30653; -. DR GeneTree; ENSGT00940000157086; -. DR HOVERGEN; HBG056906; -. DR InParanoid; O95460; -. DR OMA; ARDLCNG; -. DR OrthoDB; 1174178at2759; -. DR PhylomeDB; O95460; -. DR TreeFam; TF330078; -. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR GenomeRNAi; 8785; -. DR PRO; PR:O95460; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; ENSG00000124159; Expressed in 89 organ(s), highest expression level in body of pancreas. DR ExpressionAtlas; O95460; baseline and differential. DR Genevisible; O95460; HS. DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0003429; P:growth plate cartilage chondrocyte morphogenesis; IBA:GO_Central. DR Gene3D; 1.20.5.30; -; 1. DR Gene3D; 3.40.50.410; -; 2. DR InterPro; IPR026823; cEGF. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR034306; Matrilin-4. 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; PTHR45365; PTHR45365; 1. DR Pfam; PF12662; cEGF; 1. DR Pfam; PF10393; Matrilin_ccoil; 1. DR Pfam; PF00092; VWA; 2. DR SMART; SM00181; EGF; 4. DR SMART; SM00179; EGF_CA; 4. DR SMART; SM01279; Matrilin_ccoil; 1. DR SMART; SM00327; VWA; 2. DR SUPFAM; SSF53300; SSF53300; 2. DR SUPFAM; SSF57184; SSF57184; 1. DR SUPFAM; SSF58002; SSF58002; 1. 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; Complete proteome; Disulfide bond; KW EGF-like domain; Glycoprotein; Polymorphism; Reference proteome; KW Repeat; Secreted; Signal. FT SIGNAL 1 18 {ECO:0000250}. FT CHAIN 19 622 Matrilin-4. FT /FTId=PRO_0000007660. FT DOMAIN 34 213 VWFA 1. {ECO:0000255|PROSITE- FT ProRule:PRU00219}. FT DOMAIN 215 255 EGF-like 1; incomplete. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 256 292 EGF-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 297 337 EGF-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 342 377 EGF-like 4. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 386 561 VWFA 2. {ECO:0000255|PROSITE- FT ProRule:PRU00219}. FT COILED 591 622 {ECO:0000255}. FT CARBOHYD 69 69 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 251 251 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 305 305 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 219 230 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 226 239 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 241 254 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 260 271 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 267 280 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 282 295 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 301 312 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 308 321 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 323 336 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 342 353 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 349 362 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 364 377 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT VAR_SEQ 25 214 Missing (in isoform 3). {ECO:0000305}. FT /FTId=VSP_015255. FT VAR_SEQ 215 255 Missing (in isoform 2 and isoform 4). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:9827539}. FT /FTId=VSP_001400. FT VAR_SEQ 256 296 Missing (in isoform 4). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_015256. FT VARIANT 13 13 L -> F (in dbSNP:rs2743307). FT /FTId=VAR_055758. FT VARIANT 164 164 R -> S (in dbSNP:rs2072788). FT {ECO:0000269|PubMed:14702039}. FT /FTId=VAR_055759. FT CONFLICT 173 173 V -> L (in Ref. 2; BAC11083). FT {ECO:0000305}. FT CONFLICT 563 563 G -> S (in Ref. 2; BAC11083). FT {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 //