ID LMOD1_HUMAN Reviewed; 600 AA. AC P29536; B1APV6; C4AMB1; Q68EN2; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 08-MAR-2011, sequence version 3. DT 12-AUG-2020, entry version 164. DE RecName: Full=Leiomodin-1; DE AltName: Full=64 kDa autoantigen 1D; DE AltName: Full=64 kDa autoantigen 1D3; DE AltName: Full=64 kDa autoantigen D1 {ECO:0000303|PubMed:2026759}; DE AltName: Full=Leiomodin, muscle form; DE AltName: Full=Smooth muscle leiomodin; DE Short=SM-Lmod; DE AltName: Full=Thyroid-associated ophthalmopathy autoantigen; GN Name=LMOD1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY. RC TISSUE=Thyroid; RX PubMed=2026759; DOI=10.1210/jcem-72-6-1375; RA Dong Q., Ludgate M., Vassart G.; RT "Cloning and sequencing of a novel 64-kDa autoantigen recognized by RT patients with autoimmune thyroid disease."; RL J. Clin. Endocrinol. Metab. 72:1375-1381(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=PNS; 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 [4] RP TISSUE SPECIFICITY. RX PubMed=11318603; DOI=10.1006/geno.2000.6501; RA Conley C.A., Fritz-Six K.L., Almenar-Queralt A., Fowler V.M.; RT "Leiomodins: larger members of the tropomodulin (Tmod) gene family."; RL Genomics 73:127-139(2001). RN [5] RP TISSUE SPECIFICITY. RX PubMed=27144530; DOI=10.1371/journal.pone.0153780; RA Sahoo S., Meijles D.N., Al Ghouleh I., Tandon M., Cifuentes-Pagano E., RA Sembrat J., Rojas M., Goncharova E., Pagano P.J.; RT "MEF2C-MYOCD and leiomodin1 suppression by miRNA-214 promotes smooth muscle RT cell phenotype switching in pulmonary arterial hypertension."; RL PLoS ONE 11:E0153780-E0153780(2016). RN [6] {ECO:0000244|PDB:4Z79, ECO:0000244|PDB:4Z8G, ECO:0000244|PDB:4Z94} RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 299-486, FUNCTION, ACTIN-BINDING, RP AND SUBCELLULAR LOCATION. RX PubMed=26370058; DOI=10.1038/ncomms9314; RA Boczkowska M., Rebowski G., Kremneva E., Lappalainen P., Dominguez R.; RT "How Leiomodin and Tropomodulin use a common fold for different actin RT assembly functions."; RL Nat. Commun. 6:8314-8314(2015). CC -!- FUNCTION: Mediates nucleation of actin filaments. CC {ECO:0000269|PubMed:26370058}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere CC {ECO:0000269|PubMed:26370058}. Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:A0A0G2K0D3}. Note=Colocalizes with actin CC filaments in sarcomeres. {ECO:0000250|UniProtKB:A0A0G2K0D3}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P29536-1; Sequence=Displayed; CC Name=2; CC IsoId=P29536-2; Sequence=VSP_035745; CC -!- TISSUE SPECIFICITY: Detected in lung vascular smooth muscle (at protein CC level) (PubMed:27144530). Detected in thyroid and extraocular smooth CC muscle, but not skeletal muscle (PubMed:2026759). Detected in heart, CC aorta, skeletal muscle, colon, urinary bladder, uterus, stomach, and CC small intestine (PubMed:11318603). {ECO:0000269|PubMed:2026759, CC ECO:0000269|PubMed:27144530}. CC -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X54162; CAA38101.1; -; mRNA. DR EMBL; AC099676; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL513217; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC080187; AAH80187.1; -; mRNA. DR CCDS; CCDS53457.1; -. [P29536-1] DR PIR; S18732; S18732. DR RefSeq; NP_036266.2; NM_012134.2. [P29536-1] DR PDB; 4Z79; X-ray; 1.54 A; A=299-486. DR PDB; 4Z8G; X-ray; 2.10 A; A=364-486. DR PDB; 4Z94; X-ray; 2.40 A; G=364-486. DR PDBsum; 4Z79; -. DR PDBsum; 4Z8G; -. DR PDBsum; 4Z94; -. DR SMR; P29536; -. DR BioGRID; 117334; 1. DR IntAct; P29536; 3. DR MINT; P29536; -. DR STRING; 9606.ENSP00000356257; -. DR iPTMnet; P29536; -. DR MetOSite; P29536; -. DR PhosphoSitePlus; P29536; -. DR BioMuta; LMOD1; -. DR DMDM; 325511399; -. DR jPOST; P29536; -. DR MassIVE; P29536; -. DR MaxQB; P29536; -. DR PaxDb; P29536; -. DR PeptideAtlas; P29536; -. DR PRIDE; P29536; -. DR ProteomicsDB; 54584; -. [P29536-1] DR ProteomicsDB; 54585; -. [P29536-2] DR Antibodypedia; 34518; 154 antibodies. DR Ensembl; ENST00000367288; ENSP00000356257; ENSG00000163431. [P29536-1] DR GeneID; 25802; -. DR KEGG; hsa:25802; -. DR UCSC; uc057oju.1; human. [P29536-1] DR CTD; 25802; -. DR DisGeNET; 25802; -. DR EuPathDB; HostDB:ENSG00000163431.12; -. DR GeneCards; LMOD1; -. DR HGNC; HGNC:6647; LMOD1. DR HPA; ENSG00000163431; Tissue enhanced (smooth muscle, urinary bladder). DR MalaCards; LMOD1; -. DR MIM; 602715; gene. DR neXtProt; NX_P29536; -. DR OpenTargets; ENSG00000163431; -. DR Orphanet; 2241; Megacystis-microcolon-intestinal hypoperistalsis syndrome. DR PharmGKB; PA30413; -. DR eggNOG; KOG3735; Eukaryota. DR GeneTree; ENSGT00940000159825; -. DR HOGENOM; CLU_031052_4_0_1; -. DR InParanoid; P29536; -. DR KO; K22030; -. DR OMA; KQSTGLY; -. DR OrthoDB; 1025132at2759; -. DR PhylomeDB; P29536; -. DR TreeFam; TF315841; -. DR PathwayCommons; P29536; -. DR Reactome; R-HSA-445355; Smooth Muscle Contraction. DR BioGRID-ORCS; 25802; 16 hits in 871 CRISPR screens. DR ChiTaRS; LMOD1; human. DR GenomeRNAi; 25802; -. DR Pharos; P29536; Tbio. DR PRO; PR:P29536; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P29536; protein. DR Bgee; ENSG00000163431; Expressed in lower esophagus and 204 other tissues. DR ExpressionAtlas; P29536; baseline and differential. DR Genevisible; P29536; HS. DR GO; GO:0005884; C:actin filament; ISS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0030016; C:myofibril; IDA: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: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; IDA: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; IDA: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 3D-structure; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton; KW Phosphoprotein; Polymorphism; Reference proteome; Repeat. FT CHAIN 1..600 FT /note="Leiomodin-1" FT /id="PRO_0000084453" FT REPEAT 165..180 FT /note="1" FT REPEAT 181..196 FT /note="2" FT REPEAT 197..212 FT /note="3" FT REPEAT 213..228 FT /note="4" FT REPEAT 229..244 FT /note="5" FT REPEAT 245..260 FT /note="6" FT REPEAT 261..276 FT /note="7" FT REPEAT 277..293 FT /note="8" FT DOMAIN 574..593 FT /note="WH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406" FT REGION 165..293 FT /note="8 X approximate tandem repeats" FT REGION 508..527 FT /note="5 X 4 AA approximate tandem repeats" 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 555 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A0A0G2K0D3" FT VAR_SEQ 1..28 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:2026759" FT /id="VSP_035745" FT VARIANT 295 FT /note="T -> M (in dbSNP:rs2820312)" FT /id="VAR_021839" FT CONFLICT 102 FT /note="E -> Q (in Ref. 1; CAA38101)" FT /evidence="ECO:0000305" FT CONFLICT 118 FT /note="D -> N (in Ref. 1; CAA38101)" FT /evidence="ECO:0000305" FT CONFLICT 194 FT /note="S -> G (in Ref. 1; CAA38101)" FT /evidence="ECO:0000305" FT CONFLICT 446 FT /note="T -> S (in Ref. 1; CAA38101)" FT /evidence="ECO:0000305" FT HELIX 319..326 FT /evidence="ECO:0000244|PDB:4Z79" FT STRAND 334..336 FT /evidence="ECO:0000244|PDB:4Z79" FT HELIX 345..355 FT /evidence="ECO:0000244|PDB:4Z79" FT STRAND 363..365 FT /evidence="ECO:0000244|PDB:4Z79" FT HELIX 373..385 FT /evidence="ECO:0000244|PDB:4Z79" FT STRAND 391..393 FT /evidence="ECO:0000244|PDB:4Z79" FT HELIX 401..410 FT /evidence="ECO:0000244|PDB:4Z79" FT HELIX 411..413 FT /evidence="ECO:0000244|PDB:4Z79" FT STRAND 419..421 FT /evidence="ECO:0000244|PDB:4Z79" FT HELIX 431..441 FT /evidence="ECO:0000244|PDB:4Z79" FT STRAND 449..451 FT /evidence="ECO:0000244|PDB:4Z79" FT HELIX 457..484 FT /evidence="ECO:0000244|PDB:4Z79" SQ SEQUENCE 600 AA; 67030 MW; 79103ED8AB8231D4 CRC64; MSRVAKYRRQ VSEDPDIDSL LETLSPEEME ELEKELDVVD PDGSVPVGLR QRNQTEKQST GVYNREAMLN FCEKETKKLM QREMSMDESK QVETKTDAKN GEERGRDASK KALGPRRDSD LGKEPKRGGL KKSFSRDRDE AGGKSGEKPK EEKIIRGIDK GRVRAAVDKK EAGKDGRGEE RAVATKKEEE KKGSDRNTGL SRDKDKKREE MKEVAKKEDD EKVKGERRNT DTRKEGEKMK RAGGNTDMKK EDEKVKRGTG NTDTKKDDEK VKKNEPLHEK EAKDDSKTKT PEKQTPSGPT KPSEGPAKVE EEAAPSIFDE PLERVKNNDP EMTEVNVNNS DCITNEILVR FTEALEFNTV VKLFALANTR ADDHVAFAIA IMLKANKTIT SLNLDSNHIT GKGILAIFRA LLQNNTLTEL RFHNQRHICG GKTEMEIAKL LKENTTLLKL GYHFELAGPR MTVTNLLSRN MDKQRQKRLQ EQRQAQEAKG EKKDLLEVPK AGAVAKGSPK PSPQPSPKPS PKNSPKKGGA PAAPPPPPPP LAPPLIMENL KNSLSPATQR KMGDKVLPAQ EKNSRDQLLA AIRSSNLKQL KKVEVPKLLQ //