LMOD3_DANRE
ID LMOD3_DANRE Reviewed; 670 AA.
AC E7F7X0;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Leiomodin-3 {ECO:0000303|PubMed:25250574};
GN Name=lmod3 {ECO:0000312|ZFIN:ZDB-GENE-090313-353};
GN Synonyms=si:dkey-90a13.7 {ECO:0000312|ZFIN:ZDB-GENE-090313-353};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25250574; DOI=10.1172/jci75199;
RA Yuen M., Sandaradura S.A., Dowling J.J., Kostyukova A.S., Moroz N.,
RA Quinlan K.G., Lehtokari V.L., Ravenscroft G., Todd E.J., Ceyhan-Birsoy O.,
RA Gokhin D.S., Maluenda J., Lek M., Nolent F., Pappas C.T., Novak S.M.,
RA D'Amico A., Malfatti E., Thomas B.P., Gabriel S.B., Gupta N., Daly M.J.,
RA Ilkovski B., Houweling P.J., Davidson A.E., Swanson L.C., Brownstein C.A.,
RA Gupta V.A., Medne L., Shannon P., Martin N., Bick D.P., Flisberg A.,
RA Holmberg E., Van den Bergh P., Lapunzina P., Waddell L.B., Sloboda D.D.,
RA Bertini E., Chitayat D., Telfer W.R., Laquerriere A., Gregorio C.C.,
RA Ottenheijm C.A., Boennemann C.G., Pelin K., Beggs A.H., Hayashi Y.K.,
RA Romero N.B., Laing N.G., Nishino I., Wallgren-Pettersson C., Melki J.,
RA Fowler V.M., MacArthur D.G., North K.N., Clarke N.F.;
RT "Leiomodin-3 dysfunction results in thin filament disorganization and
RT nemaline myopathy.";
RL J. Clin. Invest. 124:4693-4708(2014).
CC -!- FUNCTION: Essential for the organization of sarcomeric thin filaments
CC in skeletal muscle. {ECO:0000269|PubMed:25250574}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q0VAK6}.
CC Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:E9QA62}.
CC Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:Q0VAK6}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q0VAK6}.
CC -!- TISSUE SPECIFICITY: expressed in muscle (at protein level).
CC {ECO:0000269|PubMed:25250574}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes short
CC bodies, bent tails, and reduced tail birefringence, consistent with
CC abnormal skeletal muscle organization, in fish larvae, 3 days after
CC fertilization. Larvae exhibit reduced trunk size, that generate less
CC force than that of wild-type counterparts, and aberrant accumulation of
CC alpha-actinin. Mutant embryos show abnormal motor function, with
CC reduced spontaneous coiling and diminished touch-evoked escape
CC responses. {ECO:0000269|PubMed:25250574}.
CC -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR EMBL; BX897727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003201226.1; XM_003201178.4.
DR AlphaFoldDB; E7F7X0; -.
DR SMR; E7F7X0; -.
DR STRING; 7955.ENSDARP00000085297; -.
DR PaxDb; E7F7X0; -.
DR PRIDE; E7F7X0; -.
DR Ensembl; ENSDART00000090864; ENSDARP00000085297; ENSDARG00000062662.
DR Ensembl; ENSDART00000193217; ENSDARP00000151281; ENSDARG00000115769.
DR GeneID; 100149390; -.
DR KEGG; dre:100149390; -.
DR CTD; 56203; -.
DR ZFIN; ZDB-GENE-090313-353; lmod3.
DR eggNOG; KOG3735; Eukaryota.
DR GeneTree; ENSGT00940000156567; -.
DR HOGENOM; CLU_031052_4_1_1; -.
DR InParanoid; E7F7X0; -.
DR OMA; PPGMWER; -.
DR OrthoDB; 1025132at2759; -.
DR PhylomeDB; E7F7X0; -.
DR TreeFam; TF315841; -.
DR PRO; PR:E7F7X0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000062662; Expressed in muscle tissue and 12 other tissues.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR GO; GO:0005865; C:striated muscle thin filament; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; IEA:InterPro.
DR GO; GO:0005523; F:tropomyosin binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IMP:ZFIN.
DR GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
DR GO; GO:0051694; P:pointed-end actin filament capping; IEA:InterPro.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISS:UniProtKB.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:ZFIN.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR030131; LMOD3.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR004934; TMOD.
DR PANTHER; PTHR10901; PTHR10901; 2.
DR PANTHER; PTHR10901:SF3; PTHR10901:SF3; 2.
DR Pfam; PF03250; Tropomodulin; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..670
FT /note="Leiomodin-3"
FT /id="PRO_0000432424"
FT DOMAIN 637..656
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 34..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 150..183
FT /evidence="ECO:0000255"
FT COILED 464..494
FT /evidence="ECO:0000255"
FT COMPBIAS 34..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 76458 MW; E15DCAB4FBB0E37F CRC64;
MSERTEQESY TDKIDEDEIL AGLSAEELKQ LQSEMDDIAP DERVPVGLRQ KDASHEMTVR
DCTEPESEEE IDEDEILAGL SAEELKQLQS EMEEIAPDER VPVGMRQRDQ TDKPPTGSFD
HRSLVEYLYW EKESKRMLEE ERVPTTLLPS QKTNEEHEAK NEDKVEELEL VYEEIVEEVE
GGQGDAVVDE VIEEVIMEVE EEDKVCDKPV KTDLDATDPT VTSEDGLQRP SESADANVEA
KTDQSGLDTE TKVNEEKKED STEPAPSSYE NWVPEKEERV ISKLKIPKLA LGGNTFVKKT
ARPSGNETNL ESTLDKIRNN NPSVTDVNLN NIENIPKEML LDYVNSLKKN RHVKTFSIAN
TGADENVAFT LANMLKENRS ITTLNIESNF ITGKGIVAII RCLQFNETLT ELRFHNQRHM
LGHHAEMEVS RLLKANNTLL KMGYHFELPG PRMVVTNLLT RNLDRQRQQR MEEQKLQQMK
EQRKVMEMYE DSLNLPPGML EMLGGYIPLS LLQNCQNGAE DIPEDSPEPS PQPSPPHQLC
KTQHLAPQQH PPNLSTGNLF EEVQLKKTPK RRDPLLEWNQ CDERKDGRPN VHLRSVPKKR
SIAREGPVDE RANLKDMIKT LKPVPRRREP PKVDLTPRDH LLSEIRQSNV AYLKAVPLPK
ILESQETSLF
