MYOM1_MOUSE
ID MYOM1_MOUSE Reviewed; 1667 AA.
AC Q62234; Q546T8; Q6PAC0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Myomesin-1;
DE AltName: Full=Myomesin family member 1;
DE AltName: Full=Skelemin;
GN Name=Myom1;
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=C57BL/10J; TISSUE=Muscle;
RX PubMed=8408035; DOI=10.1016/s0021-9258(20)80613-9;
RA Price M.G., Gomer R.H.;
RT "Skelemin, a cytoskeletal M-disc periphery protein, contains motifs of
RT adhesion/recognition and intermediate filament proteins.";
RL J. Biol. Chem. 268:21800-21810(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10036188; DOI=10.1006/geno.1998.5682;
RA Steiner F., Weber K., Furst D.O.;
RT "M band proteins myomesin and skelemin are encoded by the same gene:
RT analysis of its organization and expression.";
RL Genomics 56:78-89(1999).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 [5]
RP INTERACTION WITH BETA-INTEGRIN.
RX PubMed=9857037; DOI=10.1074/jbc.273.52.35039;
RA Reddy K.B., Gascard P., Price M.G., Negrescu E.V., Fox J.E.B.;
RT "Identification of an interaction between the M-band protein skelemin and
RT beta-integrin subunits. Colocalization of a skelemin-like protein with
RT beta1- and beta3-integrins in non-muscle cells.";
RL J. Biol. Chem. 273:35039-35047(1998).
RN [6]
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-142; SER-863;
RP SER-867 AND SER-1036, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Lung;
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).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=22562206; DOI=10.1387/ijdb.113327lp;
RA du Puy L., Beqqali A., van Tol H.T., Monshouwer-Kloots J., Passier R.,
RA Haagsman H.P., Roelen B.A.;
RT "Sarcosin (Krp1) in skeletal muscle differentiation: gene expression
RT profiling and knockdown experiments.";
RL Int. J. Dev. Biol. 56:301-309(2012).
CC -!- FUNCTION: May link the intermediate filament cytoskeleton to the M-disk
CC of the myofibrils in striated muscle. May also contact myosin
CC filaments. Also binds beta-integrins.
CC -!- SUBUNIT: Homodimer. Interacts with TTN/titin and PNKD (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:18177667, ECO:0000269|PubMed:22562206}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62234-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62234-2; Sequence=VSP_035664;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all striated muscles.
CC Expressed in all fiber types. {ECO:0000269|PubMed:18177667}.
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DR EMBL; Z22866; CAA80488.1; -; mRNA.
DR EMBL; AJ012072; CAB46494.1; -; mRNA.
DR EMBL; AC154187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060378; AAH60378.1; -; mRNA.
DR CCDS; CCDS37685.1; -. [Q62234-1]
DR CCDS; CCDS50176.1; -. [Q62234-2]
DR PIR; A48594; A48594.
DR RefSeq; NP_001077403.1; NM_001083934.1. [Q62234-2]
DR RefSeq; NP_034997.2; NM_010867.2. [Q62234-1]
DR PDB; 2JTD; NMR; -; A=1208-1329.
DR PDB; 4V10; NMR; -; A=1208-1434.
DR PDBsum; 2JTD; -.
DR PDBsum; 4V10; -.
DR AlphaFoldDB; Q62234; -.
DR SMR; Q62234; -.
DR BioGRID; 201675; 9.
DR IntAct; Q62234; 4.
DR MINT; Q62234; -.
DR STRING; 10090.ENSMUSP00000072945; -.
DR iPTMnet; Q62234; -.
DR PhosphoSitePlus; Q62234; -.
DR SWISS-2DPAGE; Q62234; -.
DR MaxQB; Q62234; -.
DR PaxDb; Q62234; -.
DR PeptideAtlas; Q62234; -.
DR PRIDE; Q62234; -.
DR ProteomicsDB; 286114; -. [Q62234-1]
DR ProteomicsDB; 286115; -. [Q62234-2]
DR Antibodypedia; 2827; 171 antibodies from 28 providers.
DR DNASU; 17929; -.
DR Ensembl; ENSMUST00000073211; ENSMUSP00000072945; ENSMUSG00000024049. [Q62234-1]
DR Ensembl; ENSMUST00000179759; ENSMUSP00000136266; ENSMUSG00000024049. [Q62234-2]
DR GeneID; 17929; -.
DR KEGG; mmu:17929; -.
DR UCSC; uc008dlx.1; mouse. [Q62234-1]
DR UCSC; uc008dly.1; mouse. [Q62234-2]
DR CTD; 8736; -.
DR MGI; MGI:1341430; Myom1.
DR VEuPathDB; HostDB:ENSMUSG00000024049; -.
DR eggNOG; ENOG502QTR4; Eukaryota.
DR GeneTree; ENSGT00940000154982; -.
DR HOGENOM; CLU_004753_1_0_1; -.
DR InParanoid; Q62234; -.
DR OMA; GYPECVL; -.
DR OrthoDB; 57219at2759; -.
DR PhylomeDB; Q62234; -.
DR TreeFam; TF331825; -.
DR BioGRID-ORCS; 17929; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Myom1; mouse.
DR EvolutionaryTrace; Q62234; -.
DR PRO; PR:Q62234; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q62234; protein.
DR Bgee; ENSMUSG00000024049; Expressed in triceps brachii and 171 other tissues.
DR ExpressionAtlas; Q62234; baseline and differential.
DR Genevisible; Q62234; MM.
DR GO; GO:0005856; C:cytoskeleton; TAS:MGI.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0030017; C:sarcomere; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:MGI.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0010737; P:protein kinase A signaling; ISO:MGI.
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; 5.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 7.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Immunoglobulin domain;
KW Muscle protein; Phosphoprotein; Reference proteome; Repeat; Thick filament.
FT CHAIN 1..1667
FT /note="Myomesin-1"
FT /id="PRO_0000072685"
FT DOMAIN 258..349
FT /note="Ig-like C2-type 1"
FT DOMAIN 376..478
FT /note="Ig-like C2-type 2"
FT DOMAIN 492..587
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 620..714
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 721..814
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 918..1016
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1023..1122
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1114..1212
FT /note="Ig-like C2-type 3"
FT DOMAIN 1340..1426
FT /note="Ig-like C2-type 4"
FT DOMAIN 1555..1644
FT /note="Ig-like C2-type 5"
FT REGION 192..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 816..913
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035664"
FT CONFLICT 133..134
FT /note="SL -> V (in Ref. 1; CAA80488 and 2; CAB46494)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="F -> V (in Ref. 1; CAA80488 and 2; CAB46494)"
FT /evidence="ECO:0000305"
FT CONFLICT 1092
FT /note="S -> C (in Ref. 1; CAA80488 and 2; CAB46494)"
FT /evidence="ECO:0000305"
FT HELIX 1212..1216
FT /evidence="ECO:0007829|PDB:2JTD"
FT STRAND 1227..1229
FT /evidence="ECO:0007829|PDB:2JTD"
FT STRAND 1231..1237
FT /evidence="ECO:0007829|PDB:2JTD"
FT TURN 1238..1240
FT /evidence="ECO:0007829|PDB:2JTD"
FT STRAND 1241..1247
FT /evidence="ECO:0007829|PDB:2JTD"
FT STRAND 1252..1254
FT /evidence="ECO:0007829|PDB:4V10"
FT STRAND 1256..1261
FT /evidence="ECO:0007829|PDB:2JTD"
FT STRAND 1268..1271
FT /evidence="ECO:0007829|PDB:2JTD"
FT STRAND 1274..1276
FT /evidence="ECO:0007829|PDB:2JTD"
FT STRAND 1278..1280
FT /evidence="ECO:0007829|PDB:2JTD"
FT STRAND 1283..1287
FT /evidence="ECO:0007829|PDB:2JTD"
FT TURN 1292..1294
FT /evidence="ECO:0007829|PDB:2JTD"
FT STRAND 1297..1304
FT /evidence="ECO:0007829|PDB:2JTD"
FT STRAND 1307..1314
FT /evidence="ECO:0007829|PDB:2JTD"
FT HELIX 1317..1327
FT /evidence="ECO:0007829|PDB:2JTD"
FT HELIX 1333..1335
FT /evidence="ECO:0007829|PDB:4V10"
FT STRAND 1356..1359
FT /evidence="ECO:0007829|PDB:4V10"
FT STRAND 1373..1375
FT /evidence="ECO:0007829|PDB:4V10"
FT STRAND 1385..1387
FT /evidence="ECO:0007829|PDB:4V10"
FT STRAND 1394..1397
FT /evidence="ECO:0007829|PDB:4V10"
FT TURN 1402..1404
FT /evidence="ECO:0007829|PDB:4V10"
FT STRAND 1406..1411
FT /evidence="ECO:0007829|PDB:4V10"
FT STRAND 1414..1417
FT /evidence="ECO:0007829|PDB:4V10"
FT STRAND 1423..1425
FT /evidence="ECO:0007829|PDB:4V10"
FT HELIX 1428..1431
FT /evidence="ECO:0007829|PDB:4V10"
SQ SEQUENCE 1667 AA; 185464 MW; CDFDE2DE4A54DB42 CRC64;
MSLPFYQRSH QHYDLSYRNK DLRTTMSHYQ QEKKRSAVYT HGSTAYSSRS LAARRQESEA
FSQASATSYQ QQASQTYSLG ASSSSRHSQG SEVSRKTASA YDYGYSHGLT DSSLLLEDYS
SKLSPQTKRA KRSLLSGEET GSLPGNYLVP IYSGRQVHIS GIRDSEEERI KEAAAYIAQK
TLLASEEAIA ASKQSTASKQ SATSKRTTST LQREETFEKK SRNIAIREKA EELSLKKTLE
ETQTYHGKLN EDHLLHAPEF IIKPRSHTVW EKENVKLHCS VAGWPEPRLT WYKNQVPINV
HANPGKYIIE SRYGMHTLEI SKCDFEDTAQ YRASAMNVQG ELSAYASVVV KRYKGELDES
LLRGGVSMPL SFAVTPYGYA SKFEIHFDDK FDVSFGREGE TMSLGCRVVI TPEIKHFQPE
VQWYRNGAPV SPSKWVQPHW SGDRATLTFS HLNKEDEGLY TIRVRMGEYY EQYSAYVFVR
DADAEIEGAP AAPLDVVSLD ANKDYIIISW KQPAVDGGSP ILGYFIDKCE VGTDTWSQCN
DTPVKFARFP VTGLIEGRSY IFRVRAVNKT GIGLPSRVSE PVAALDPAEK ARLKSHPSAP
WTGQIIVTEE EPTEGVIPGP PTDLSVTEAT RSYVVLSWKP PGQRGHEGIM YFVEKCDVGA
ENWQRVNTEL PVKSPRFALF DLVEGKSYRF RVRCSNSAGV GEPSETTEVT VVGDKLDIPK
APGKIIPSRN TDTSVVVSWE ESRDAKELVG YYIEASVVGS GKWEPCNNNP VKGSRFTCHG
LTTAQSYIFR VRAVNAAGLS EYSQDSEAIE VKAAIGGGVS PDVWPQLSDT PGGLTDSRGG
MNGASPPTSQ KDALLGSNPN KPSPPSSPSS RGQKEVSTVS ESVQEPLSSP PQEAAPEEEQ
SQSEPPKKKK DPVAVPSAPY DITCLESFRD SMVLGWKQPD TTGGAEITGY YVNYREVVGE
VPGKWREANI KAVSDAAYKI SNLKENTLYQ FQVSAMNIAG LGAPSTVSEC FKCEEWTIAV
PGPPHSVKLS EVRKNSLVLQ WKPPVYSGRT PVTGYFVDLK EASAKDDQWR GLNEAAIVNK
YLRVQGLKEG TSYVFRVRAV NQAGVGKPSD LAGPVVAETR PGTKEVVVSV DDDGVISLNF
ECDQMTPKSE FVWSKDYVPT EDSPRLEVEN KGDKTKMTFK DLGTDDLGTY SCDVTDTDGI
ASSYLIDEEE MKRLLALSQE HKFPTVPTKS ELAVEILEKG QVRFWMQAEK LSSNAKVSYI
FNEKEIFEGP KYKMHIDRNT GIIEMFMEKL QDEDEGTYTF QIQDGKATGH STLVLIGDVY
KKLQKEAEFQ RQEWIRKQGP HFAEYLSWEV TGECNVLLKC KVANIKKETH IVWYKDEREI
SVDEKHDFKD GICTLLITEF SKKDAGFYEV ILKDDRGKDK SRLKLVDEAF QDLMTEVCKK
IALSATDLKI QSTAEGIRLY SFVCYYLDDL KVNWSHNGTG IKYTDRVKSG VTGEQIWLQI
NEPTPNDKGK YVMELFDGKT GHQKTVDLSG QAFDEAFAEF QRLKQAAIAE KNRARVLGGL
PDVVTIQEGK ALNLTCNVWG DPPPEVSWLK NEKPLTSDDH CSLKFEAGKT AFFTISGVST
ADSGKYGLVV KNKYGSETSD FTVSVFIPEE ELRKGAMEPP KGNQKSK
