MYOM3_MOUSE
ID MYOM3_MOUSE Reviewed; 1439 AA.
AC A2ABU4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Myomesin-3;
DE AltName: Full=Myomesin family member 3;
GN Name=Myom3;
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 [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).
RN [2]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18177667; DOI=10.1016/j.jmb.2007.11.048;
RA Schoenauer R., Lange S., Hirschy A., Ehler E., Perriard J.C., Agarkova I.;
RT "Myomesin 3, a novel structural component of the M-band in striated
RT muscle.";
RL J. Mol. Biol. 376:338-351(2008).
CC -!- FUNCTION: May link the intermediate filament cytoskeleton to the M-disk
CC of the myofibrils in striated muscle. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18177667}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:18177667}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in slow muscle, extraocular muscle
CC and embryonic/neonatal skeletal muscle (at protein level). Expression
CC in skeletal muscle is fiber type specific, with the highest levels in
CC type IIA fibers (intermediate speed) and lower levels in type I fibers.
CC {ECO:0000269|PubMed:18177667}.
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DR EMBL; AL662911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38921.1; -.
DR RefSeq; NP_001078978.1; NM_001085509.2.
DR AlphaFoldDB; A2ABU4; -.
DR SMR; A2ABU4; -.
DR BioGRID; 232446; 3.
DR STRING; 10090.ENSMUSP00000101480; -.
DR iPTMnet; A2ABU4; -.
DR PhosphoSitePlus; A2ABU4; -.
DR MaxQB; A2ABU4; -.
DR PaxDb; A2ABU4; -.
DR PeptideAtlas; A2ABU4; -.
DR PRIDE; A2ABU4; -.
DR ProteomicsDB; 287594; -.
DR Antibodypedia; 30256; 67 antibodies from 20 providers.
DR Ensembl; ENSMUST00000105854; ENSMUSP00000101480; ENSMUSG00000037139.
DR GeneID; 242702; -.
DR KEGG; mmu:242702; -.
DR UCSC; uc008vgy.2; mouse.
DR CTD; 127294; -.
DR MGI; MGI:2685280; Myom3.
DR VEuPathDB; HostDB:ENSMUSG00000037139; -.
DR eggNOG; ENOG502RDUJ; Eukaryota.
DR GeneTree; ENSGT00940000158669; -.
DR HOGENOM; CLU_004753_1_0_1; -.
DR InParanoid; A2ABU4; -.
DR OMA; YYVERCD; -.
DR OrthoDB; 57219at2759; -.
DR PhylomeDB; A2ABU4; -.
DR TreeFam; TF331825; -.
DR BioGRID-ORCS; 242702; 3 hits in 74 CRISPR screens.
DR PRO; PR:A2ABU4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2ABU4; protein.
DR Bgee; ENSMUSG00000037139; Expressed in extra-ocular muscle and 90 other tissues.
DR Genevisible; A2ABU4; MM.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 12.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 3.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Immunoglobulin domain; Reference proteome; Repeat.
FT CHAIN 1..1439
FT /note="Myomesin-3"
FT /id="PRO_0000315395"
FT DOMAIN 154..246
FT /note="Ig-like C2-type 1"
FT DOMAIN 269..362
FT /note="Ig-like C2-type 2"
FT DOMAIN 376..471
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 504..599
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 605..698
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 704..799
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 806..901
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1122..1207
FT /note="Ig-like C2-type 3"
FT DOMAIN 1336..1425
FT /note="Ig-like C2-type 4"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..149
FT /evidence="ECO:0000255"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1439 AA; 161778 MW; EBAAC8EE292CF110 CRC64;
MTLPHSPGSA GEPQASQTVQ VHRLEHRQEE EQKEERQHSL QMGSSVQRRT YRSSEEEQQF
SSEDYALAAA LALTASSELS WEAKLRRQTT TVELEERGQR RVGFGNDLER MELAFLRTQR
LLRQRRDWKA LRQRTEEKVR EAKELIELCS GRGPWFWIPL RSHAVWEHTT VLLTCTVQGS
PPFQVTWYKN DIRIDPRLFP AGKYRITNNY GLLTLEIMRC TVEDSATYTV LVKNAYGQAS
SFAKVLIRNY LGKDAGFDSE IFKRSMFGPS AEFTSVLKPI FAQEKEPFSL TCLFSDDVLE
AEQRIQWYRD GRLLRSSTRR QILYADRQAS VKVSCAYKED EGFYTIRVSS PFGPQEQSAY
VFIRDAAAEK PGAPGSPLNV RCLNVHRDCL TLTWVPPSDT RGSTITGYSI EMCQGDSEEW
MPCLKAPGGT CRCPIQGLVE GQSYQFRVRA ISKAGTSLPS KASEAVVTGD YDAVHKSTEI
PYDLGSKITI SKNDFEDAVT IPSAPTNVHA SEIREAYAVL SWEEPRPRGR APLTYTLEKS
VIGSGTWEAI STETPIKSPR FALLDLEKGK SYVFRVRALN QYGMSDPSEP SEPVALKGKP
ATLPPPAQVQ AFRNTQTSVS LAWEPVDGGS ELLGYYIYSR EAGASEWQTV NNKPIQDTKF
TVPGLRTGKE YDFCIRSVSE AGVGESSAAT QPVRVKQALA TPSAPYDFAL LNCGKNEMVI
GWKPPKRRGG GKILGYFMDQ HDSVESDWHP VNRQPIPSRV CKVTNLHEGH FYEFRARAVN
WAGIGELSAP SSLFECKEWT MPEPGPPYDV RVSEVQATSV MLQWEPPLYI GAGPVTGYHV
SFQEKGSEEW KPVTPDATSD THLRVSDLQP GKQYMFRVQA MNSAGLGQPS VPTDPVLLED
KPDAQEIEVG VDDEGQIYLA FEAPEAPDFP EFQWSKDYQG PPDPQRVEVE DEISKSKVIL
KEPDLQDLGI YSVVVPDADE DTSASHTLTE EELNKLKKLS HEIRNPVIKL ISGWNVEILE
QGEVRLWLEV EKLSPAAELH LIFNEKEIFS SPNRKINFDR EKGLVEVIIQ QLSEDDKGSY
TAQLQDGKAK NQITLALVDD EFDKLLRKAD AKRRDWKRKQ GPYFQEPLTW KVTDDCQVLL
SCKVTNTKKE SRFQWFFQKK EAPHGQYNPP TGDGSLSIEG FSKENQGVYR AVVSDERGED
DTVLDLTGEA LDAVLTELGR IGALSATPLK IQGTEEGIRL FSKVKYYNVD YMKTAWFHKD
KRLESGDRVR AGTTLDEIWL HILDPKDSDK GKYTLEITAG KEVRQLSADL SGQAFDDALA
EHQRLKALAV IEKNRAKVVR GLPDVATIME DKTLCLTCVI SGDPSPEISW LKNDQPISFF
DRYHMEVKGT EVTVTIDKVT SEDSGRYGIF VKNKYGSETG QVTISVFKHG EEPKELKKK
