MATN4_HUMAN
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 03-AUG-2022, entry version 196.
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};
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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 AlphaFoldDB; O95460; -.
DR SMR; O95460; -.
DR BioGRID; 114313; 36.
DR ComplexPortal; CPX-4641; Matrilin-4 complex.
DR IntAct; O95460; 16.
DR GlyConnect; 1493; 6 N-Linked glycans (1 site).
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 PRIDE; O95460; -.
DR ProteomicsDB; 50892; -. [O95460-1]
DR ProteomicsDB; 50893; -. [O95460-2]
DR ProteomicsDB; 50894; -. [O95460-3]
DR ProteomicsDB; 50895; -. [O95460-4]
DR Antibodypedia; 27542; 128 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 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; HQCVSAL; -.
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 1068 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 69 other tissues.
DR ExpressionAtlas; O95460; baseline and differential.
DR Genevisible; O95460; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IC:ComplexPortal.
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; IPR000742; EGF-like_dom.
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; PTHR24020:SF14; PTHR24020:SF14; 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; Disulfide bond; EGF-like domain;
KW Glycoprotein; Reference proteome; Repeat; 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
