LMOD1_RAT
ID LMOD1_RAT Reviewed; 595 AA.
AC A0A0G2K0D3;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Leiomodin-1;
DE AltName: Full=Smooth muscle leiomodin {ECO:0000303|PubMed:11350761};
DE Short=SM-Lmod {ECO:0000303|PubMed:11350761};
GN Name=Lmod1 {ECO:0000312|RGD:1307236};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10520227; DOI=10.1076/ceyr.19.4.313.5304;
RA Conley C.A., Fowler V.M.;
RT "Localization of the human 64kD autoantigen D1 to myofibrils in a subset of
RT extraocular muscle fibers.";
RL Curr. Eye Res. 19:313-322(1999).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11350761; DOI=10.1152/ajpcell.2001.280.6.c1645;
RA Conley C.A.;
RT "Leiomodin and tropomodulin in smooth muscle.";
RL Am. J. Physiol. 280:C1645-C1656(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-85; SER-135 AND
RP SER-550, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Required for proper contractility of visceral smooth muscle
CC cells (By similarity). Mediates nucleation of actin filaments (By
CC similarity). {ECO:0000250|UniProtKB:P29536}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000269|PubMed:10520227, ECO:0000269|PubMed:11350761}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:10520227,
CC ECO:0000269|PubMed:11350761}. Note=Colocalizes with actin filaments in
CC sarcomeres. {ECO:0000269|PubMed:10520227, ECO:0000269|PubMed:11350761}.
CC -!- TISSUE SPECIFICITY: Detected in smooth muscle, in stomach and uterus,
CC blood vessel wall, and in slow fibers in extraocular muscle, urinary
CC bladder and sternothyroid muscle (at protein level).
CC {ECO:0000269|PubMed:10520227, ECO:0000269|PubMed:11350761}.
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DR EMBL; AC096239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008767784.1; XM_008769562.2.
DR AlphaFoldDB; A0A0G2K0D3; -.
DR SMR; A0A0G2K0D3; -.
DR IntAct; A0A0G2K0D3; 4.
DR STRING; 10116.ENSRNOP00000009623; -.
DR iPTMnet; A0A0G2K0D3; -.
DR PaxDb; A0A0G2K0D3; -.
DR GeneID; 304816; -.
DR CTD; 25802; -.
DR RGD; 1307236; Lmod1.
DR VEuPathDB; HostDB:ENSRNOG00000051548; -.
DR eggNOG; KOG3735; Eukaryota.
DR OMA; ELKMDMM; -.
DR OrthoDB; 1025132at2759; -.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR PRO; PR:A0A0G2K0D3; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000051548; Expressed in esophagus and 18 other tissues.
DR GO; GO:0005884; C:actin filament; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030016; C:myofibril; ISO:RGD.
DR GO; GO:0030017; C:sarcomere; IDA:UniProtKB.
DR GO; GO:0005865; C:striated muscle thin filament; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005523; F:tropomyosin binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0045010; P:actin nucleation; ISS:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
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:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR030136; LMOD1.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR004934; TMOD.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR10901; PTHR10901; 1.
DR PANTHER; PTHR10901:SF5; PTHR10901:SF5; 1.
DR Pfam; PF03250; Tropomodulin; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00246; WH2; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..595
FT /note="Leiomodin-1"
FT /id="PRO_0000437122"
FT REPEAT 165..180
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 181..196
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 197..212
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 213..227
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 228..243
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 244..257
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 258..273
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 274..288
FT /note="8"
FT /evidence="ECO:0000305"
FT DOMAIN 569..588
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..288
FT /note="8 X approximate tandem repeats"
FT /evidence="ECO:0000305"
FT REGION 467..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..522
FT /note="5 X 4 AA approximate tandem repeats"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..515
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 595 AA; 66216 MW; AB3C2E75351BCBB8 CRC64;
MSKVAKYRRQ VSEDPDIDSL LSTLSPEEME ELEKELDVVD PDGSIPVGLR QRNQTDKQPS
GSFNREAMLN FCEKESKKII QREMSVDESK QVGRKTDAKN GEDKGSNASR KALGPRQDSD
VGKEPKKGVL KKSFSRDREE ADSRGSEKPK EEKVIRGIDK GRVRAAVDRK EAGKDGREER
AAATTKKEEE KTGSVRNAGL SRDKDKKREE VKEPSKKEEV KLTAENRSTV GRQEDGKQKE
SREDRDKKPE VKGIGCGSRD SRKEDEKVKK EETQPDKGVR EEGKTREKQP PSGPSKPSDG
QARAEEEAAP SIFDEPLEKV KNNDPEMTEV NVNNSDCITN EILVRFTEAL EFNTVVKVFA
LANTRADDHV AFAIAIMLKA NKTITSLNLD SNHITGKGIL AIFRALLQNN TLTELRFHNQ
RHICGGKTEM EIAKLLKENT TLLKLGYHFE LAGPRMTVTN LLSRNMDKQR QKRLQEQKQA
QEASGEKKDR LEVPKVGALP KGSPKPSPQP SPKSAPKNSP KKAGVPAAPP PPPPPLAPPL
IMENLKNSLS PATQRKMGDK VLPAQEKNSR DQLLAAIRSS NLKQLKKVEV PKLLQ
