LMOD1_MOUSE
ID LMOD1_MOUSE Reviewed; 595 AA.
AC Q8BVA4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Leiomodin-1;
GN Name=Lmod1;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=22157009; DOI=10.1074/jbc.m111.302224;
RA Nanda V., Miano J.M.;
RT "Leiomodin 1, a new serum response factor-dependent target gene expressed
RT preferentially in differentiated smooth muscle cells.";
RL J. Biol. Chem. 287:2459-2467(2012).
RN [3]
RP FUNCTION.
RX PubMed=28292896; DOI=10.1073/pnas.1620507114;
RA Halim D., Wilson M.P., Oliver D., Brosens E., Verheij J.B., Han Y.,
RA Nanda V., Lyu Q., Doukas M., Stoop H., Brouwer R.W., van Ijcken W.F.,
RA Slivano O.J., Burns A.J., Christie C.K., de Mesy Bentley K.L., Brooks A.S.,
RA Tibboel D., Xu S., Jin Z.G., Djuwantono T., Yan W., Alves M.M.,
RA Hofstra R.M., Miano J.M.;
RT "Loss of LMOD1 impairs smooth muscle cytocontractility and causes
RT megacystis microcolon intestinal hypoperistalsis syndrome in humans and
RT mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E2739-E2747(2017).
CC -!- FUNCTION: Required for proper contractility of visceral smooth muscle
CC cells (PubMed:28292896). Mediates nucleation of actin filaments (By
CC similarity). {ECO:0000250|UniProtKB:P29536,
CC ECO:0000269|PubMed:28292896}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000250|UniProtKB:A0A0G2K0D3}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:A0A0G2K0D3}. Note=Colocalizes with actin
CC filaments in sarcomeres. {ECO:0000250|UniProtKB:A0A0G2K0D3}.
CC -!- TISSUE SPECIFICITY: Detected in aorta, urinary bladder and uterus (at
CC protein level). Detected in smooth muscle cells. Detected in aorta,
CC bladder, colon, intestine, stomach and uterus.
CC {ECO:0000269|PubMed:22157009}.
CC -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR EMBL; AK079173; BAC37567.1; -; mRNA.
DR CCDS; CCDS35718.1; -.
DR RefSeq; NP_444336.2; NM_053106.2.
DR AlphaFoldDB; Q8BVA4; -.
DR SMR; Q8BVA4; -.
DR STRING; 10090.ENSMUSP00000061597; -.
DR iPTMnet; Q8BVA4; -.
DR PhosphoSitePlus; Q8BVA4; -.
DR jPOST; Q8BVA4; -.
DR MaxQB; Q8BVA4; -.
DR PaxDb; Q8BVA4; -.
DR PRIDE; Q8BVA4; -.
DR ProteomicsDB; 286223; -.
DR DNASU; 93689; -.
DR GeneID; 93689; -.
DR KEGG; mmu:93689; -.
DR CTD; 25802; -.
DR MGI; MGI:2135671; Lmod1.
DR eggNOG; KOG3735; Eukaryota.
DR InParanoid; Q8BVA4; -.
DR OrthoDB; 1025132at2759; -.
DR PhylomeDB; Q8BVA4; -.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR BioGRID-ORCS; 93689; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Lmod1; mouse.
DR PRO; PR:Q8BVA4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BVA4; protein.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030016; C:myofibril; ISS:UniProtKB.
DR GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR GO; GO:0005865; C:striated muscle thin filament; IBA:GO_Central.
DR GO; GO:0003779; F:actin 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: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 Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..595
FT /note="Leiomodin-1"
FT /id="PRO_0000354070"
FT REPEAT 165..179
FT /note="1"
FT REPEAT 180..195
FT /note="2"
FT REPEAT 196..211
FT /note="3"
FT REPEAT 212..226
FT /note="4"
FT REPEAT 227..240
FT /note="5"
FT REPEAT 242..255
FT /note="6"
FT REPEAT 256..271
FT /note="7"
FT REPEAT 272..288
FT /note="8"
FT DOMAIN 569..588
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..288
FT /note="8 X approximate tandem repeats"
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 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 81..286
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 505..540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K0D3"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K0D3"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K0D3"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K0D3"
SQ SEQUENCE 595 AA; 66310 MW; 5E4BD8E084A13FF6 CRC64;
MSKVAKYRRQ VSEDPDIDSL LSTLSPEEME ELEKELDVVD PDGSIPVGLR QRNQTDKQPS
GSFNREAMLN FCEKESKKLI QREMSVDESK QVGRKTDAKN GEEKDSDASR KAPGPRQDSD
LGKEPKKGVL KKSFSRDREE ADGRGGEKPK EEKVIRGIDK GRVRAAVDRK ESGKDGREER
AAAARKEEEK TGSVKNAGLS RDKDKKKEEV KEPSKKEEVK LTAESRNTVG RREDGRLKES
SKENKKPEDE GIGSGGRDWR KEDEKVKKEE NQPDKEVREE SKTKAPEKQA PSCPNKPSDG
QARAEEEAAP SIFDEPLEKV KNNDPEMTEV NVNNSDCITN EILVRFTEAL EFNTVVKVFA
LANTRADDHV AFAIAIMLKA NKTITSLNLD SNHITGKGIL AIFRALLQNN TLTELRFHNQ
RHICGVKTEM EIAKLLKENT TLLKLGYHFE LAGPRMTVTN LLSRNMDKQR QKRLQEQKQA
QEASGEKKDR LEVPKVGALA KGSPKPSPQP SPKPAPKNSP KKAGVPAAPP PPPPPLAPPL
IMENLKNSLS PATQRKMGDK VLPAQEKNSR DQLLAAIRSS NLKQLKKVEV PKLLQ
