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   24-JAN-2024, entry version 204.
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.
DR   AlphaFoldDB; O95460; -.
DR   SMR; O95460; -.
DR   BioGRID; 114313; 36.
DR   ComplexPortal; CPX-4641; Matrilin-4 complex.
DR   IntAct; O95460; 16.
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; 137 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; 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.
DR   Genevisible; O95460; HS.
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
//