MATN2_MOUSE
ID MATN2_MOUSE Reviewed; 956 AA.
AC O08746; E9QPK9; Q8R542;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Matrilin-2;
DE Flags: Precursor;
GN Name=Matn2;
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] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Limb;
RX PubMed=9083061; DOI=10.1074/jbc.272.14.9268;
RA Deak F., Piecha D., Bachrati C., Paulsson M., Kiss I.;
RT "Primary structure and expression of matrilin-2, the closest relative of
RT cartilage matrix protein within the von Willebrand factor type A-like
RT module superfamily.";
RL J. Biol. Chem. 272:9268-9274(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=129/Sv;
RX PubMed=11852232; DOI=10.1016/s0945-053x(01)00194-9;
RA Mates L., Korpos E., Deak F., Liu Z., Beier D.R., Aszodi A., Kiss I.;
RT "Comparative analysis of the mouse and human genes (Matn2 and MATN2) for
RT matrilin-2, a filament-forming protein widely distributed in extracellular
RT matrices.";
RL Matrix Biol. 21:163-174(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Involved in matrix assembly. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O08746-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O08746-2; Sequence=VSP_041771;
CC -!- TISSUE SPECIFICITY: Detected in a variety of organs, including
CC calvaria, uterus, heart and brain, as well as fibroblast and osteoblast
CC cell lines.
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DR EMBL; U69262; AAC53163.1; -; mRNA.
DR EMBL; AF358844; AAM11539.1; -; Genomic_DNA.
DR EMBL; AF358831; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AF358832; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AF358833; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AF358834; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AF358835; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AF358836; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AF358837; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AF358838; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AF358839; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AF358840; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AF358841; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AF358842; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AF358843; AAM11539.1; JOINED; Genomic_DNA.
DR EMBL; AC126028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37056.1; -. [O08746-2]
DR CCDS; CCDS88747.1; -. [O08746-1]
DR RefSeq; XP_006520086.1; XM_006520023.2.
DR AlphaFoldDB; O08746; -.
DR SMR; O08746; -.
DR BioGRID; 201321; 7.
DR ComplexPortal; CPX-4467; Matrilin-2 complex.
DR IntAct; O08746; 2.
DR STRING; 10090.ENSMUSP00000128202; -.
DR GlyGen; O08746; 2 sites.
DR iPTMnet; O08746; -.
DR PhosphoSitePlus; O08746; -.
DR MaxQB; O08746; -.
DR PaxDb; O08746; -.
DR PeptideAtlas; O08746; -.
DR PRIDE; O08746; -.
DR ProteomicsDB; 287316; -. [O08746-1]
DR ProteomicsDB; 287317; -. [O08746-2]
DR Antibodypedia; 26033; 186 antibodies from 33 providers.
DR Ensembl; ENSMUST00000022947; ENSMUSP00000022947; ENSMUSG00000022324. [O08746-2]
DR Ensembl; ENSMUST00000227759; ENSMUSP00000154040; ENSMUSG00000022324. [O08746-1]
DR UCSC; uc007vln.1; mouse. [O08746-1]
DR UCSC; uc007vlo.1; mouse. [O08746-2]
DR MGI; MGI:109613; Matn2.
DR VEuPathDB; HostDB:ENSMUSG00000022324; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000158008; -.
DR HOGENOM; CLU_008905_0_0_1; -.
DR InParanoid; O08746; -.
DR OMA; CATEDHA; -.
DR OrthoDB; 1174178at2759; -.
DR BioGRID-ORCS; 17181; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Matn2; mouse.
DR PRO; PR:O08746; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O08746; protein.
DR Bgee; ENSMUSG00000022324; Expressed in external carotid artery and 252 other tissues.
DR ExpressionAtlas; O08746; baseline and differential.
DR Genevisible; O08746; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:ComplexPortal.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0120216; C:matrilin complex; IPI:ComplexPortal.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; IGI:MGI.
DR GO; GO:0031104; P:dendrite regeneration; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IC:ComplexPortal.
DR GO; GO:0008347; P:glial cell migration; IDA:MGI.
DR GO; GO:0001764; P:neuron migration; IDA:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR GO; GO:0048678; P:response to axon injury; IMP:MGI.
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; IPR030747; Matrilin-2.
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:SF35; PTHR24020:SF35; 4.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF10393; Matrilin_ccoil; 1.
DR Pfam; PF00092; VWA; 2.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 10.
DR SMART; SM01279; Matrilin_ccoil; 1.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF53300; SSF53300; 2.
DR SUPFAM; SSF57184; SSF57184; 3.
DR SUPFAM; SSF58002; SSF58002; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 7.
DR PROSITE; PS01186; EGF_2; 9.
DR PROSITE; PS50234; VWFA; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Disulfide bond; EGF-like domain;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..956
FT /note="Matrilin-2"
FT /id="PRO_0000007656"
FT DOMAIN 57..232
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 238..278
FT /note="EGF-like 1"
FT DOMAIN 279..319
FT /note="EGF-like 2"
FT DOMAIN 320..360
FT /note="EGF-like 3"
FT DOMAIN 361..401
FT /note="EGF-like 4"
FT DOMAIN 402..442
FT /note="EGF-like 5"
FT DOMAIN 443..483
FT /note="EGF-like 6"
FT DOMAIN 484..524
FT /note="EGF-like 7"
FT DOMAIN 525..565
FT /note="EGF-like 8"
FT DOMAIN 566..606
FT /note="EGF-like 9"
FT DOMAIN 607..647
FT /note="EGF-like 10"
FT DOMAIN 655..830
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT COILED 917..955
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 890
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 242..253
FT /evidence="ECO:0000250"
FT DISULFID 249..262
FT /evidence="ECO:0000250"
FT DISULFID 264..277
FT /evidence="ECO:0000250"
FT DISULFID 283..294
FT /evidence="ECO:0000250"
FT DISULFID 290..303
FT /evidence="ECO:0000250"
FT DISULFID 305..318
FT /evidence="ECO:0000250"
FT DISULFID 324..335
FT /evidence="ECO:0000250"
FT DISULFID 331..344
FT /evidence="ECO:0000250"
FT DISULFID 346..359
FT /evidence="ECO:0000250"
FT DISULFID 365..376
FT /evidence="ECO:0000250"
FT DISULFID 372..385
FT /evidence="ECO:0000250"
FT DISULFID 387..400
FT /evidence="ECO:0000250"
FT DISULFID 406..417
FT /evidence="ECO:0000250"
FT DISULFID 413..426
FT /evidence="ECO:0000250"
FT DISULFID 428..441
FT /evidence="ECO:0000250"
FT DISULFID 447..458
FT /evidence="ECO:0000250"
FT DISULFID 454..467
FT /evidence="ECO:0000250"
FT DISULFID 469..482
FT /evidence="ECO:0000250"
FT DISULFID 488..499
FT /evidence="ECO:0000250"
FT DISULFID 495..508
FT /evidence="ECO:0000250"
FT DISULFID 510..523
FT /evidence="ECO:0000250"
FT DISULFID 529..540
FT /evidence="ECO:0000250"
FT DISULFID 536..549
FT /evidence="ECO:0000250"
FT DISULFID 551..564
FT /evidence="ECO:0000250"
FT DISULFID 570..581
FT /evidence="ECO:0000250"
FT DISULFID 577..590
FT /evidence="ECO:0000250"
FT DISULFID 592..605
FT /evidence="ECO:0000250"
FT DISULFID 611..622
FT /evidence="ECO:0000250"
FT DISULFID 618..631
FT /evidence="ECO:0000250"
FT DISULFID 633..646
FT /evidence="ECO:0000250"
FT VAR_SEQ 861..879
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041771"
FT CONFLICT 321
FT /note="V -> M (in Ref. 1; AAC53163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 106748 MW; 3E4A608FF92BDE55 CRC64;
MEKMLVGCLL MLGQLFLVLP VDGRERPQAR FPSRGRHVRM YPQTALLESS CENKRADLVF
IIDSSRSVNT YDYAKVKEFI LDILQFLDIG PDVTRVGLLQ YGSTVKNEFS LKTFKRKSEV
ERAVKRMRHL STGTMTGLAI QYALNIAFSE AEGARPLREN VPRIIMIVTD GRPQDSVAEV
AAKARNTGIL IFAIGVGQVD LNTLKAIGSE PHKDHVFLVA NFSQIESLTS VFQNKLCTVH
MCSVLEHNCA HFCLNTPGSY ICKCKQGYIL STDQKTCRIQ DLCATEDHGC EQLCVNMLGS
FVCQCYSGYT LAEDGKRCTA VDYCASENHG CEHECVNAES SYLCRCHEGF ALNSDKKTCS
KIDYCASSNH GCQHECVNAQ TSALCRCLKG FMLNPDRKTC RRINYCALNK PGCEHECVNT
EEGHYCRCRQ GYNLDPNGKT CSRVDHCAQQ DHGCEQLCLN TEESFVCQCS EGFLINDDLK
TCSRADYCLL SNHGCEYSCV NTDKSFACQC PEGHVLRSDG KTCAKLDSCA LGDHGCEHSC
VSSEDSFVCQ CFEGYILRDD GKTCRRKDVC QDVNHGCEHL CVNSGESYVC KCLEGFRLAE
DGKRCRRKNV CKSTQHGCEH MCVNNGNSYL CRCSEGFVLA EDGKHCKRCT EGPIDLVFVI
DGSKSLGEEN FETVKHFVTG IIDSLAVSPK AARVGLLQYS TQVRTEFTLR GFSSAKEMKK
AVTHMKYMGK GSMTGLALKH MFERSFTQVE GARPPSTQVP RVAIVFTDGR AQDDVSEWAS
KAKANGITMY AVGVGKAIEE ELQEIASEPI DKHLFYAEDF STMGEISEKL KEGICEALED
SGGRQDSAAW DLPQQAHQPT EPEPVTIKIK DLLSCSNFAV QHRFLFEEDN LSRSTQKLFH
STKSSGNPLE ESQDQCKCEN LILFQNVANE EVRKLTQRLE EMTQRMEALE NRLKYR
