MATN4_MOUSE
ID MATN4_MOUSE Reviewed; 624 AA.
AC O89029; O89030; Q9QWS3;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Matrilin-4;
DE Short=MAT-4;
DE Flags: Precursor;
GN Name=Matn4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND VARIANTS.
RC STRAIN=C57BL/6J, and CD-1; TISSUE=Fetus;
RX PubMed=9771906; DOI=10.1016/s0014-5793(98)01111-9;
RA Wagener R., Kobbe B., Paulsson M.;
RT "Matrilin-4, a new member of the matrilin family of extracellular matrix
RT proteins.";
RL FEBS Lett. 436:123-127(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 218-257.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Major component of the extracellular matrix of cartilage.
CC -!- SUBUNIT: Interacts with COMP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=O89029-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O89029-2; Sequence=VSP_001401;
CC -!- TISSUE SPECIFICITY: Lung, brain, sternum, kidney and heart.
CC -!- DEVELOPMENTAL STAGE: The short isoform was detected in 7 weeks old mice
CC but not in developing mice (19.5 dpc embryos or in 2, 8, and 21 days
CC old animals).
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; AJ006140; CAA06889.1; -; mRNA.
DR EMBL; AJ006140; CAA06890.1; -; mRNA.
DR EMBL; BC036558; AAH36558.1; -; mRNA.
DR EMBL; AJ010984; CAA09451.1; -; Genomic_DNA.
DR CCDS; CCDS17034.1; -. [O89029-1]
DR RefSeq; NP_001239492.1; NM_001252563.1.
DR AlphaFoldDB; O89029; -.
DR SMR; O89029; -.
DR BioGRID; 201323; 2.
DR ComplexPortal; CPX-4661; Matrilin-4 complex.
DR STRING; 10090.ENSMUSP00000099392; -.
DR GlyGen; O89029; 2 sites.
DR PhosphoSitePlus; O89029; -.
DR MaxQB; O89029; -.
DR PaxDb; O89029; -.
DR PRIDE; O89029; -.
DR ProteomicsDB; 295700; -. [O89029-1]
DR ProteomicsDB; 295701; -. [O89029-2]
DR DNASU; 17183; -.
DR GeneID; 17183; -.
DR KEGG; mmu:17183; -.
DR CTD; 8785; -.
DR MGI; MGI:1328314; Matn4.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; O89029; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; O89029; -.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR BioGRID-ORCS; 17183; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Matn4; mouse.
DR PRO; PR:O89029; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O89029; protein.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0120216; C:matrilin complex; IPI:ComplexPortal.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IC:ComplexPortal.
DR GO; GO:0048678; P:response to axon injury; IDA:MGI.
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; 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; 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; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..624
FT /note="Matrilin-4"
FT /id="PRO_0000007661"
FT DOMAIN 36..215
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 217..257
FT /note="EGF-like 1"
FT DOMAIN 258..298
FT /note="EGF-like 2"
FT DOMAIN 299..339
FT /note="EGF-like 3"
FT DOMAIN 340..380
FT /note="EGF-like 4"
FT DOMAIN 388..563
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT COILED 590..623
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 221..232
FT /evidence="ECO:0000250"
FT DISULFID 228..241
FT /evidence="ECO:0000250"
FT DISULFID 243..256
FT /evidence="ECO:0000250"
FT DISULFID 262..273
FT /evidence="ECO:0000250"
FT DISULFID 269..282
FT /evidence="ECO:0000250"
FT DISULFID 284..297
FT /evidence="ECO:0000250"
FT DISULFID 303..314
FT /evidence="ECO:0000250"
FT DISULFID 310..323
FT /evidence="ECO:0000250"
FT DISULFID 325..338
FT /evidence="ECO:0000250"
FT DISULFID 344..355
FT /evidence="ECO:0000250"
FT DISULFID 351..364
FT /evidence="ECO:0000250"
FT DISULFID 366..379
FT /evidence="ECO:0000250"
FT VAR_SEQ 28..217
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9771906"
FT /id="VSP_001401"
FT VARIANT 319
FT /note="A -> E (in strain: C57BL/6J)"
FT VARIANT 346
FT /note="G -> D (in strain: C57BL/6J)"
SQ SEQUENCE 624 AA; 68918 MW; DFA28D2C94B1A14F CRC64;
MRGPCCWPLS LLLLFLQSWE TQLQSAGPRC YNGPLDLVFM IDSSRSVRPF EFETMRQFLV
GLLRSLDVGL NATRVGVIQY SSQVQSVFPL GAFSRREDME RAIRAVVPLA QGTMTGLAIQ
YAMNVAFSEA EGARPSEERV PRVLVIVTDG RPQDRVAEVA AQARARGIEI YAVGVQRADV
GSLRTMASPP LDQHVFLVES FDLIQEFGLQ FQGRLCGKDL CAELVHGCQH LCVNAPGTFY
CACNSGYKLA PDNKNCLALD LCAEGTHGCE HLCVNSVDSY FCRCRAGFAL QQDQRSCRAI
DYCSFGNHSC QHECVSTLAG PQCRCREGHD LLPDGRSCRV RDFCNGVDHG CEFQCVSEGL
SFHCLCPEGR RLQADGKSCD RCREGHVDLV LLVDGSKSVR PQNFELVKRF VNQIVDFLDV
SPEGTRVGLV QFSSRVRTEF PLGRYGTAAE VKQAVLAVEY MERGTMTGLA LRHMVEHSFS
EAQGARPRDL NVPRVGLVFT DGRSQDDISV WAARAKEEGI VMYAVGVGKA VEEELREIAS
EPSELHVSYS PDFSTMTHLL ENLKGSICPE EGIGAGTELR SPCECESLVE FQGRTLGALE
SLTQNLARLT ERLEELENQL ASRK
