MATN3_MOUSE
ID MATN3_MOUSE Reviewed; 481 AA.
AC O35701; Q543Q2; Q9JHM0;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Matrilin-3;
DE Flags: Precursor;
GN Name=Matn3;
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].
RC STRAIN=C57BL/6 X CBA;
RX PubMed=9287130; DOI=10.1016/s0014-5793(97)00895-8;
RA Wagener R., Kobbe B., Paulsson M.;
RT "Primary structure of matrilin-3, a new member of a family of extracellular
RT matrix proteins related to cartilage matrix protein (matrilin-1) and von
RT Willebrand factor.";
RL FEBS Lett. 413:129-134(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=10656920; DOI=10.1007/s003350010018;
RA Wagener R., Kobbe B., Aszodi A., Liu Z., Beier D.R., Paulsson M.;
RT "Structure and mapping of the mouse matrilin-3 gene (Matn3), a member of a
RT gene family containing a U12-type AT-AC intron.";
RL Mamm. Genome 11:85-90(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PROTEIN SEQUENCE OF N-TERMINUS, CHARACTERIZATION, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10660556; DOI=10.1074/jbc.275.6.3999;
RA Klatt A.R., Nitsche D.P., Kobbe B., Morgelin M., Paulsson M., Wagener R.;
RT "Molecular structure and tissue distribution of matrilin-3, a filament-
RT forming extracellular matrix protein expressed during skeletal
RT development.";
RL J. Biol. Chem. 275:3999-4006(2000).
RN [5]
RP IDENTIFICATION IN COMPLEX WITH CRELD2; MANF AND PDIA4, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF CYS-72; VAL-189 AND CYS-258.
RX PubMed=23956175; DOI=10.1093/hmg/ddt383;
RA Hartley C.L., Edwards S., Mullan L., Bell P.A., Fresquet M.,
RA Boot-Handford R.P., Briggs M.D.;
RT "Armet/Manf and Creld2 are components of a specialized ER stress response
RT provoked by inappropriate formation of disulphide bonds: implications for
RT genetic skeletal diseases.";
RL Hum. Mol. Genet. 22:5262-5275(2013).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-193, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Major component of the extracellular matrix of cartilage and
CC may play a role in the formation of extracellular filamentous networks.
CC {ECO:0000269|PubMed:10660556}.
CC -!- SUBUNIT: Can form homooligomers (monomers, dimers, trimers and
CC tetramers) and heterooligomers with matrilin-1. Interacts with COMP (By
CC similarity). Component of a complex containing at least CRELD2, MANF,
CC MATN3 and PDIA4 (PubMed:23956175). {ECO:0000250,
CC ECO:0000269|PubMed:23956175}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10660556,
CC ECO:0000269|PubMed:23956175}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in growing skeletal tissue such
CC as epiphyseal growth plate or in bone undergoing growth and remodeling.
CC In the bone, actively synthesized in osteoblasts and osteocytes.
CC Expressed in cartilage of sternum, femur, vertebrae, trachea, articular
CC and epiphyseal cartilage, cartilage of developing bones and bones.
CC -!- DEVELOPMENTAL STAGE: The earliest expression could be detected in a
CC 12.5 dpc embryo in the cartilage anlage of the developing bones. At
CC 14.5 dpc the primordial skeleton shows a strong expression. At birth
CC present in the developing occipital bones, bones of the nasal cavity,
CC manubrium and corpus of sternum as well as in the cartilage plates of
CC trachea. At no stage of development detected in extraskeletal tissues.
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DR EMBL; Y10521; CAA71532.1; -; mRNA.
DR EMBL; AJ242929; CAB72265.1; -; Genomic_DNA.
DR EMBL; AJ242930; CAB72265.1; JOINED; Genomic_DNA.
DR EMBL; AJ242931; CAB72265.1; JOINED; Genomic_DNA.
DR EMBL; AJ242932; CAB72265.1; JOINED; Genomic_DNA.
DR EMBL; AJ242933; CAB72265.1; JOINED; Genomic_DNA.
DR EMBL; AJ242934; CAB72265.1; JOINED; Genomic_DNA.
DR EMBL; AJ242935; CAB72265.1; JOINED; Genomic_DNA.
DR EMBL; AJ242936; CAB72265.1; JOINED; Genomic_DNA.
DR EMBL; AK048456; BAC33343.1; -; mRNA.
DR CCDS; CCDS25806.1; -.
DR RefSeq; NP_034900.4; NM_010770.4.
DR AlphaFoldDB; O35701; -.
DR SMR; O35701; -.
DR ComplexPortal; CPX-4501; Matrilin-3 complex.
DR ComplexPortal; CPX-4504; Matrilin-1 - Matrilin-3 complex.
DR STRING; 10090.ENSMUSP00000020899; -.
DR GlyGen; O35701; 1 site.
DR iPTMnet; O35701; -.
DR PhosphoSitePlus; O35701; -.
DR MaxQB; O35701; -.
DR PaxDb; O35701; -.
DR PRIDE; O35701; -.
DR ProteomicsDB; 295699; -.
DR Antibodypedia; 27187; 220 antibodies from 27 providers.
DR DNASU; 17182; -.
DR Ensembl; ENSMUST00000020899; ENSMUSP00000020899; ENSMUSG00000020583.
DR GeneID; 17182; -.
DR KEGG; mmu:17182; -.
DR UCSC; uc007nag.2; mouse.
DR CTD; 4148; -.
DR MGI; MGI:1328350; Matn3.
DR VEuPathDB; HostDB:ENSMUSG00000020583; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000157581; -.
DR HOGENOM; CLU_008905_6_1_1; -.
DR InParanoid; O35701; -.
DR OMA; PCMLGTH; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; O35701; -.
DR TreeFam; TF330078; -.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 17182; 2 hits in 74 CRISPR screens.
DR PRO; PR:O35701; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O35701; protein.
DR Bgee; ENSMUSG00000020583; Expressed in intervertebral disk and 82 other tissues.
DR Genevisible; O35701; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:ComplexPortal.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
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:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:ComplexPortal.
DR Gene3D; 1.20.5.30; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
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; IPR030765; Matrilin_3.
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; PTHR24034:SF105; PTHR24034:SF105; 2.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF10393; Matrilin_ccoil; 1.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM01279; Matrilin_ccoil; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF58002; SSF58002; 1.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Glycoprotein; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:10660556"
FT CHAIN 28..481
FT /note="Matrilin-3"
FT /id="PRO_0000007658"
FT DOMAIN 78..253
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 259..300
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 301..342
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 343..384
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 385..426
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT COILED 451..475
FT /evidence="ECO:0000255"
FT MOD_RES 193
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 436
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000250|UniProtKB:O15232"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 263..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 270..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 286..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 305..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 312..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 328..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 347..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 354..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 370..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 389..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 396..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 412..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 72
FT /note="C->A: Prevents Matn3 protein aggregation; in
FT association with D-189 and A-258."
FT /evidence="ECO:0000269|PubMed:23956175"
FT MUTAGEN 189
FT /note="V->D: Increased protein levels of Creld2 and Manf in
FT chondrocytes. Prevents Matn3 protein aggregation; in
FT association with A-72 and A-258."
FT /evidence="ECO:0000269|PubMed:23956175"
FT MUTAGEN 258
FT /note="C->A: Prevents Matn3 protein aggregation; in
FT association with A-72 and D-189."
FT /evidence="ECO:0000269|PubMed:23956175"
FT CONFLICT 317
FT /note="V -> I (in Ref. 1; CAA71532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 51845 MW; BC82B8A140344CBD CRC64;
MLLSAPLRHL PGLLLLLWPL LLLPSLAAPG RLARASVRRL GTRVPGGSPG HLSALATSTR
APYSGGRGAG VCKSRPLDLV FIIDSSRSVR PLEFTKVKTF VSRIIDTLDI GATDTRVAVV
NYASTVKIEF QLNTYSDKQA LKQAVARITP LSTGTMSGLA IQTAMEEAFT VEAGARGPMS
NIPKVAIIVT DGRPQDQVNE VAARARASGI ELYAVGVDRA DMESLKMMAS KPLEEHVFYV
ETYGVIEKLS ARFQETFCAL DQCMLGTHQC QHVCVSDGDG KHHCECSQGY TLNADGKTCS
AIDKCALSTH GCEQICVNDR NGSYHCECYG GYALNADRRT CAALDKCASG THGCQHICVN
DGAGSHHCEC FEGYTLNADK KTCSVRNKCA LGTHGCQHIC VSDGAVAYHC DCFPGYTLND
DKKTCSDIEE ARSLISIEDA CGCGATLAFQ EKVSSHLQKL NTKLDNILKK LKVTEYGQVH
R
