LIMC1_HUMAN
ID LIMC1_HUMAN Reviewed; 1083 AA.
AC Q9UPQ0; A8MXC3; E9PHM7; Q503B5; Q5CZB1; Q5CZB6; Q5H9S8; Q68E07; Q6PJ44;
AC Q7Z3G5; Q8N3S9; Q8N6M2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=LIM and calponin homology domains-containing protein 1 {ECO:0000305};
GN Name=LIMCH1 {ECO:0000312|HGNC:HGNC:29191};
GN Synonyms=KIAA1102 {ECO:0000312|EMBL:BAA83054.2};
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-759.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5; 6; 9 AND 10),
RP AND VARIANT THR-759.
RC TISSUE=Endometrial adenocarcinoma, Fetal kidney, Retina, Salivary gland,
RC and Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 8), AND VARIANT
RP THR-759.
RC TISSUE=Brain, Muscle, and Ovary;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-201 AND SER-718, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-718, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; THR-215; SER-217;
RP SER-231; SER-233; SER-377; SER-471; SER-516; THR-529; SER-718; SER-875 AND
RP SER-973, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-233; SER-377;
RP SER-516; SER-523; THR-537; SER-601; SER-718; THR-724; SER-875 AND SER-973,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-215; SER-217 AND SER-718, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-192; SER-201;
RP SER-204; SER-207; THR-215; SER-217; SER-231; SER-233; SER-297; SER-303;
RP SER-377; THR-402; SER-471; SER-518; SER-523; SER-670; SER-681; SER-718;
RP SER-875; SER-966 AND SER-973, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP FUNCTION, INTERACTION WITH MYH9, SUBCELLULAR LOCATION, AND REGION.
RX PubMed=28228547; DOI=10.1091/mbc.e15-04-0218;
RA Lin Y.H., Zhen Y.Y., Chien K.Y., Lee I.C., Lin W.C., Chen M.Y., Pai L.M.;
RT "LIMCH1 regulates nonmuscle myosin-II activity and suppresses cell
RT migration.";
RL Mol. Biol. Cell 28:1054-1065(2017).
CC -!- FUNCTION: Actin stress fibers-associated protein that activates non-
CC muscle myosin IIa. Activates the non-muscle myosin IIa complex by
CC promoting the phosphorylation of its regulatory subunit MRLC/MYL9.
CC Through the activation of non-muscle myosin IIa, positively regulates
CC actin stress fibers assembly and stabilizes focal adhesions. It
CC therefore negatively regulates cell spreading and cell migration.
CC {ECO:0000269|PubMed:28228547}.
CC -!- SUBUNIT: Interacts with MYH9; independently of the integration of MYH9
CC into the myosin complex. {ECO:0000269|PubMed:28228547}.
CC -!- INTERACTION:
CC Q9UPQ0-1; Q6UXM1-1: LRIG3; NbExp=3; IntAct=EBI-25412679, EBI-25412632;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:28228547}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1;
CC IsoId=Q9UPQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPQ0-2; Sequence=VSP_026550;
CC Name=3;
CC IsoId=Q9UPQ0-3; Sequence=VSP_026541, VSP_026546, VSP_026549;
CC Name=4;
CC IsoId=Q9UPQ0-4; Sequence=VSP_026547, VSP_026548, VSP_026549,
CC VSP_026550;
CC Name=5;
CC IsoId=Q9UPQ0-5; Sequence=VSP_026541, VSP_026547, VSP_026548,
CC VSP_026549, VSP_026550;
CC Name=6;
CC IsoId=Q9UPQ0-6; Sequence=VSP_026542, VSP_026543, VSP_026549,
CC VSP_026550;
CC Name=7;
CC IsoId=Q9UPQ0-7; Sequence=VSP_026541, VSP_026544, VSP_026545;
CC Name=8;
CC IsoId=Q9UPQ0-8; Sequence=VSP_026541, VSP_026549, VSP_026550;
CC Name=9;
CC IsoId=Q9UPQ0-9; Sequence=VSP_026542, VSP_026543, VSP_026547,
CC VSP_026549, VSP_026550;
CC Name=10;
CC IsoId=Q9UPQ0-10; Sequence=VSP_026549, VSP_026550;
CC -!- SIMILARITY: Belongs to the LIMCH1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83054.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB029025; BAA83054.2; ALT_INIT; mRNA.
DR EMBL; AL831962; CAD38604.1; -; mRNA.
DR EMBL; BX537916; CAD97899.1; -; mRNA.
DR EMBL; CR749205; CAH18063.1; -; mRNA.
DR EMBL; CR933645; CAI45946.1; -; mRNA.
DR EMBL; CR936601; CAI56749.1; -; mRNA.
DR EMBL; CR936610; CAI56754.1; -; mRNA.
DR EMBL; CR936664; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC095043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023546; AAH23546.1; -; mRNA.
DR EMBL; BC029735; AAH29735.1; -; mRNA.
DR EMBL; BC095394; AAH95394.1; -; mRNA.
DR CCDS; CCDS33977.1; -. [Q9UPQ0-1]
DR CCDS; CCDS47047.1; -. [Q9UPQ0-6]
DR CCDS; CCDS54763.1; -. [Q9UPQ0-2]
DR CCDS; CCDS54764.1; -. [Q9UPQ0-10]
DR CCDS; CCDS54765.1; -. [Q9UPQ0-9]
DR CCDS; CCDS75119.1; -. [Q9UPQ0-4]
DR CCDS; CCDS75121.1; -. [Q9UPQ0-5]
DR CCDS; CCDS82919.1; -. [Q9UPQ0-3]
DR CCDS; CCDS87222.1; -. [Q9UPQ0-8]
DR RefSeq; NP_001106188.1; NM_001112717.3. [Q9UPQ0-2]
DR RefSeq; NP_001106189.1; NM_001112718.3. [Q9UPQ0-10]
DR RefSeq; NP_001106190.1; NM_001112719.3. [Q9UPQ0-6]
DR RefSeq; NP_001106191.1; NM_001112720.3. [Q9UPQ0-9]
DR RefSeq; NP_001276051.1; NM_001289122.2. [Q9UPQ0-4]
DR RefSeq; NP_001276053.1; NM_001289124.1. [Q9UPQ0-5]
DR RefSeq; NP_001317601.1; NM_001330672.1.
DR RefSeq; NP_001317603.1; NM_001330674.1.
DR RefSeq; NP_001317713.1; NM_001330784.1.
DR RefSeq; NP_001317715.1; NM_001330786.1. [Q9UPQ0-8]
DR RefSeq; NP_055803.2; NM_014988.4. [Q9UPQ0-1]
DR AlphaFoldDB; Q9UPQ0; -.
DR SMR; Q9UPQ0; -.
DR BioGRID; 116645; 121.
DR IntAct; Q9UPQ0; 35.
DR MINT; Q9UPQ0; -.
DR STRING; 9606.ENSP00000316891; -.
DR GlyGen; Q9UPQ0; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; Q9UPQ0; -.
DR PhosphoSitePlus; Q9UPQ0; -.
DR BioMuta; LIMCH1; -.
DR DMDM; 296439483; -.
DR EPD; Q9UPQ0; -.
DR jPOST; Q9UPQ0; -.
DR MassIVE; Q9UPQ0; -.
DR MaxQB; Q9UPQ0; -.
DR PaxDb; Q9UPQ0; -.
DR PeptideAtlas; Q9UPQ0; -.
DR PRIDE; Q9UPQ0; -.
DR ProteomicsDB; 20568; -.
DR ProteomicsDB; 85402; -. [Q9UPQ0-1]
DR ProteomicsDB; 85403; -. [Q9UPQ0-2]
DR ProteomicsDB; 85404; -. [Q9UPQ0-3]
DR ProteomicsDB; 85405; -. [Q9UPQ0-4]
DR ProteomicsDB; 85406; -. [Q9UPQ0-5]
DR ProteomicsDB; 85407; -. [Q9UPQ0-6]
DR ProteomicsDB; 85408; -. [Q9UPQ0-7]
DR ProteomicsDB; 85409; -. [Q9UPQ0-8]
DR ProteomicsDB; 85410; -. [Q9UPQ0-9]
DR Antibodypedia; 1336; 72 antibodies from 17 providers.
DR DNASU; 22998; -.
DR Ensembl; ENST00000313860.11; ENSP00000316891.7; ENSG00000064042.18. [Q9UPQ0-1]
DR Ensembl; ENST00000381753.8; ENSP00000371172.4; ENSG00000064042.18. [Q9UPQ0-9]
DR Ensembl; ENST00000396595.7; ENSP00000379840.3; ENSG00000064042.18. [Q9UPQ0-6]
DR Ensembl; ENST00000508501.5; ENSP00000424825.1; ENSG00000064042.18. [Q9UPQ0-10]
DR Ensembl; ENST00000511496.5; ENSP00000421242.1; ENSG00000064042.18. [Q9UPQ0-8]
DR Ensembl; ENST00000512820.5; ENSP00000424437.1; ENSG00000064042.18. [Q9UPQ0-4]
DR Ensembl; ENST00000512946.5; ENSP00000424645.1; ENSG00000064042.18. [Q9UPQ0-2]
DR Ensembl; ENST00000513024.5; ENSP00000425222.1; ENSG00000064042.18. [Q9UPQ0-5]
DR GeneID; 22998; -.
DR KEGG; hsa:22998; -.
DR UCSC; uc003gvu.6; human. [Q9UPQ0-1]
DR CTD; 22998; -.
DR DisGeNET; 22998; -.
DR GeneCards; LIMCH1; -.
DR HGNC; HGNC:29191; LIMCH1.
DR HPA; ENSG00000064042; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 617750; gene.
DR neXtProt; NX_Q9UPQ0; -.
DR OpenTargets; ENSG00000064042; -.
DR PharmGKB; PA162393957; -.
DR VEuPathDB; HostDB:ENSG00000064042; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00950000183159; -.
DR InParanoid; Q9UPQ0; -.
DR OrthoDB; 298177at2759; -.
DR PhylomeDB; Q9UPQ0; -.
DR TreeFam; TF332155; -.
DR PathwayCommons; Q9UPQ0; -.
DR SignaLink; Q9UPQ0; -.
DR BioGRID-ORCS; 22998; 10 hits in 1064 CRISPR screens.
DR ChiTaRS; LIMCH1; human.
DR GeneWiki; LIMCH1; -.
DR GenomeRNAi; 22998; -.
DR Pharos; Q9UPQ0; Tbio.
DR PRO; PR:Q9UPQ0; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UPQ0; protein.
DR Bgee; ENSG00000064042; Expressed in lower lobe of lung and 203 other tissues.
DR ExpressionAtlas; Q9UPQ0; baseline and differential.
DR Genevisible; Q9UPQ0; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032034; F:myosin II head/neck binding; IDA:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR GO; GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; IMP:CACAO.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IMP:UniProtKB.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001997; Calponin/LIMCH1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR031865; DUF4757.
DR InterPro; IPR029980; LIMCH1.
DR InterPro; IPR003096; SM22_calponin.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR15551:SF3; PTHR15551:SF3; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF15949; DUF4757; 1.
DR Pfam; PF00412; LIM; 1.
DR PRINTS; PR00889; CALPONIN.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; LIM domain;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..1083
FT /note="LIM and calponin homology domains-containing protein
FT 1"
FT /id="PRO_0000293619"
FT DOMAIN 21..125
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1011..1077
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 185..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..639
FT /note="Mediates interaction with MYH9"
FT /evidence="ECO:0000269|PubMed:28228547"
FT REGION 615..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 354..439
FT /evidence="ECO:0000255"
FT COILED 782..823
FT /evidence="ECO:0000255"
FT COMPBIAS 185..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH68"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH68"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 313
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH68"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 402
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 472
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH68"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 724
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH68"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH68"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 900
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UH68"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 3, isoform 5, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_026541"
FT VAR_SEQ 1..154
FT /note="Missing (in isoform 6 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_026542"
FT VAR_SEQ 155..161
FT /note="GLLAQMR -> MDSERQV (in isoform 6 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_026543"
FT VAR_SEQ 288..297
FT /note="KAEREEYRKS -> NADTMRRSVR (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026544"
FT VAR_SEQ 298..1083
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026545"
FT VAR_SEQ 311
FT /note="F -> FSFPETIEEEGSEVGSAGEDNPAGQMNPGWKPSDGGCELPDGSGKEH
FT PSSDGAVVAPAPKSEEKDAAEIQKRERLEQAGIKVMPAAQRFASQKQLSEEKEAIRDIV
FT LRKENSFLTHQHGNDSEAEGEVVCRLPDLEKDDFAARRARMNQTKPMVPLNQLLYGPYP
FT KKGAEKSDGSKQLSKGISKKRSLEYKRNQGHTEEVKLIVTCNMRAQESEPVEGGLRKVP
FT DLHKDDLAQQRIQGSLAPHREPPSFITLSNITEADLETWERLKVSEKARDGDVQHICAS
FT EPSPEIKAETAIRDDFANRKARASKKASSPRQKFVHFGPVTELDQQKWKRLSIGKAGPR
FT EDEEEVICHGSKIQMDSVSPVSAATSSLKGHQIFNRQNDCRTMNCGRGDYCRRASWLAP
FT VPESQEEWVCSLGECPRGTEEVTSKQLPQDGKEETESAPRDSERLSKAERSEDSSQPLV
FT CPLASECEASGTEEKLEKMTAPAWSGSGLKGQRKLDDSRKDDMMARRTGMSLRHTGSNP
FT NQFLPVPFAKQQDVEESSKGLPMKDQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_026546"
FT VAR_SEQ 313..324
FT /note="Missing (in isoform 4, isoform 5 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_026547"
FT VAR_SEQ 747
FT /note="Q -> QESPGTASVPLRVQNSWRRSQFFSQS (in isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_026548"
FT VAR_SEQ 762
FT /note="Missing (in isoform 3, isoform 4, isoform 5, isoform
FT 6, isoform 8, isoform 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_026549"
FT VAR_SEQ 980..1005
FT /note="Missing (in isoform 2, isoform 4, isoform 5, isoform
FT 6, isoform 8, isoform 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_026550"
FT VARIANT 759
FT /note="M -> T (in dbSNP:rs11734372)"
FT /evidence="ECO:0000269|PubMed:10470851,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_033105"
FT CONFLICT 17
FT /note="E -> G (in Ref. 3; CAI56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="S -> P (in Ref. 3; CR936664)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="S -> F (in Ref. 3; CAI56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="I -> T (in Ref. 3; CR936664)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="T -> I (in Ref. 3; CAH18063)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="S -> G (in Ref. 3; CAD38604)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="V -> I (in Ref. 3; CR936664)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="E -> G (in Ref. 3; CAI56754)"
FT /evidence="ECO:0000305"
FT CONFLICT 750
FT /note="S -> P (in Ref. 3; CAD38604)"
FT /evidence="ECO:0000305"
FT CONFLICT 867
FT /note="K -> N (in Ref. 3; CAH18063)"
FT /evidence="ECO:0000305"
FT CONFLICT 1053
FT /note="V -> A (in Ref. 3; CAD38604)"
FT /evidence="ECO:0000305"
FT CONFLICT 1059
FT /note="R -> G (in Ref. 3; CAI45946)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1083 AA; 121867 MW; 19C8BA192EDBDC6B CRC64;
MACPALGLEA LQPLQPEPPP EPAFSEAQKW IEQVTGRSFG DKDFRTGLEN GILLCELLNA
IKPGLVKKIN RLPTPIAGLD NIILFLRGCK ELGLKESQLF DPSDLQDTSN RVTVKSLDYS
RKLKNVLVTI YWLGKAANSC TSYSGTTLNL KEFEGLLAQM RKDTDDIESP KRSIRDSGYI
DCWDSERSDS LSPPRHGRDD SFDSLDSFGS RSRQTPSPDV VLRGSSDGRG SDSESDLPHR
KLPDVKKDDM SARRTSHGEP KSAVPFNQYL PNKSNQTAYV PAPLRKKKAE REEYRKSWST
ATSPLGGERP FRYGPRTPVS DDAESTSMFD MRCEEEAAVQ PHSRARQEQL QLINNQLREE
DDKWQDDLAR WKSRRRSVSQ DLIKKEEERK KMEKLLAGED GTSERRKSIK TYREIVQEKE
RRERELHEAY KNARSQEEAE GILQQYIERF TISEAVLERL EMPKILERSH STEPNLSSFL
NDPNPMKYLR QQSLPPPKFT ATVETTIARA SVLDTSMSAG SGSPSKTVTP KAVPMLTPKP
YSQPKNSQDV LKTFKVDGKV SVNGETVHRE EEKERECPTV APAHSLTKSQ MFEGVARVHG
SPLELKQDNG SIEINIKKPN SVPQELAATT EKTEPNSQED KNDGGKSRKG NIELASSEPQ
HFTTTVTRCS PTVAFVEFPS SPQLKNDVSE EKDQKKPENE MSGKVELVLS QKVVKPKSPE
PEATLTFPFL DKMPEANQLH LPNLNSQVDS PSSEKSPVMT PQFKFWAWDP EEERRRQEKW
QQEQERLLQE RYQKEQDKLK EEWEKAQKEV EEEERRYYEE ERKIIEDTVV PFTVSSSSAD
QLSTSSSMTE GSGTMNKIDL GNCQDEKQDR RWKKSFQGDD SDLLLKTRES DRLEEKGSLT
EGALAHSGNP VSKGVHEDHQ LDTEAGAPHC GTNPQLAQDP SQNQQTSNPT HSSEDVKPKT
LPLDKSINHQ IESPSERRKK SPREHFQAGP FSPCSPTPPG QSPNRSISGK KLCSSCGLPL
GKGAAMIIET LNLYFHIQCF RCGICKGQLG DAVSGTDVRI RNGLLNCNDC YMRSRSAGQP
TTL
