MYOTI_MOUSE
ID MYOTI_MOUSE Reviewed; 496 AA.
AC Q9JIF9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Myotilin;
DE AltName: Full=Myofibrillar titin-like Ig domains protein;
DE AltName: Full=Titin immunoglobulin domain protein;
GN Name=Myot; Synonyms=Myo, Ttid;
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 TISSUE=Muscle;
RX PubMed=11335118; DOI=10.1016/s0925-4773(01)00325-2;
RA Mologni L., Salmikangas P., Fougerousse F., Beckmann J.S., Carpen O.;
RT "Developmental expression of myotilin, a gene mutated in limb-girdle
RT muscular dystrophy type 1A.";
RL Mech. Dev. 103:121-125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17074808; DOI=10.1128/mcb.00561-06;
RA Moza M., Mologni L., Trokovic R., Faulkner G., Partanen J., Carpen O.;
RT "Targeted deletion of the muscular dystrophy gene myotilin does not perturb
RT muscle structure or function in mice.";
RL Mol. Cell. Biol. 27:244-252(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-20, 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: Component of a complex of multiple actin cross-linking
CC proteins. Involved in the control of myofibril assembly and stability
CC at the Z lines in muscle cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with ACTA1, ACTN1, FLNA, FLNB, FLNC, and
CC MYOZ2. Interacts with the C-terminal region of MYOZ1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q9UBF9}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9UBF9}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:Q9UBF9}. Note=Sarcomeric, also localized to the
CC sarcolemma. Colocalizes with MYOZ1 at the Z-lines in skeletal muscle.
CC {ECO:0000250|UniProtKB:Q9UBF9}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:17074808}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mutant mice develop
CC normally, have a normal life span, and their muscle capacity does not
CC significantly differ from wild-type animals, even after prolonged
CC physical stress. {ECO:0000269|PubMed:17074808}.
CC -!- SIMILARITY: Belongs to the myotilin/palladin family. {ECO:0000305}.
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DR EMBL; AF230979; AAF76465.1; -; mRNA.
DR EMBL; BC016214; AAH16214.1; -; mRNA.
DR CCDS; CCDS29228.1; -.
DR RefSeq; NP_001028793.1; NM_001033621.3.
DR RefSeq; XP_006526196.1; XM_006526133.3.
DR AlphaFoldDB; Q9JIF9; -.
DR SMR; Q9JIF9; -.
DR IntAct; Q9JIF9; 1.
DR MINT; Q9JIF9; -.
DR STRING; 10090.ENSMUSP00000025349; -.
DR iPTMnet; Q9JIF9; -.
DR PhosphoSitePlus; Q9JIF9; -.
DR MaxQB; Q9JIF9; -.
DR PaxDb; Q9JIF9; -.
DR PRIDE; Q9JIF9; -.
DR ProteomicsDB; 287338; -.
DR Antibodypedia; 26530; 270 antibodies from 31 providers.
DR DNASU; 58916; -.
DR Ensembl; ENSMUST00000025349; ENSMUSP00000025349; ENSMUSG00000024471.
DR Ensembl; ENSMUST00000115498; ENSMUSP00000111160; ENSMUSG00000024471.
DR GeneID; 58916; -.
DR KEGG; mmu:58916; -.
DR UCSC; uc008euw.1; mouse.
DR CTD; 9499; -.
DR MGI; MGI:1889800; Myot.
DR VEuPathDB; HostDB:ENSMUSG00000024471; -.
DR eggNOG; ENOG502QTWI; Eukaryota.
DR GeneTree; ENSGT00940000159795; -.
DR HOGENOM; CLU_006487_0_1_1; -.
DR InParanoid; Q9JIF9; -.
DR OMA; IQSQNTC; -.
DR OrthoDB; 496055at2759; -.
DR PhylomeDB; Q9JIF9; -.
DR BioGRID-ORCS; 58916; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Synpo2; mouse.
DR PRO; PR:Q9JIF9; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9JIF9; protein.
DR Bgee; ENSMUSG00000024471; Expressed in digastric muscle group and 116 other tissues.
DR ExpressionAtlas; Q9JIF9; baseline and differential.
DR Genevisible; Q9JIF9; MM.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
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; PF07679; I-set; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Cell membrane; Cytoplasm; Cytoskeleton;
KW Immunoglobulin domain; Membrane; Methylation; Muscle protein;
KW Reference proteome; Repeat.
FT CHAIN 1..496
FT /note="Myotilin"
FT /id="PRO_0000072688"
FT DOMAIN 248..333
FT /note="Ig-like C2-type 1"
FT DOMAIN 347..439
FT /note="Ig-like C2-type 2"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..149
FT /note="Necessary for interaction with ACTN1"
FT /evidence="ECO:0000250"
FT REGION 202..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..496
FT /note="Necessary for interaction with ACTA1"
FT /evidence="ECO:0000250"
FT REGION 213..491
FT /note="Necessary for interaction with FLNC"
FT /evidence="ECO:0000250"
FT COMPBIAS 202..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 496 AA; 55316 MW; BC4E2C0537F091D3 CRC64;
MFNYERPKHF IQPQNPCGSR LQPPGPEVSG FPSQTKQSSI VIQPRQCTEQ RFSASSTVSS
HITVSSSAYP APQQLAGPNP GQKVTATYNQ SPASFLSSIL PSQPDYCNSK IPSTVDSNYQ
QSSVNQPVNA MSSQAANARP TPKTPDHEIQ GSKEALIQDL ERKLKCKDTL LHNGNQRLTY
EEKMARRLLG PQNAAAVFQA QNSDVQDSPQ HNPEQARLHV PTSQVRSRSS SRAEANDQDA
IQEKFYPPRF IQVPENMSIE EGRFCRMDFK VSGLPAPDVS WYLNGRPVQS DELHKMIVSE
KGFHSLIFEV VRASDAGPYA CVARNRAGEA TFTVQLDVLA KEHKRAPMFI FKPQSKKVFE
GETVKLECQI SAIPPPKLFW KRNNEMVQFN TDRISLYHDN AGRVTLLIKD VNKKDAGWYT
VSAVNEAGVT TCNTRLDVTA RPIQTLPAPK QLRVRPTFSK YLALNGRGLD VKQAFNPEGE
FQRLAAQSGL YESEEL
