LIMS2_HUMAN
ID LIMS2_HUMAN Reviewed; 341 AA.
AC Q7Z4I7; A6NLH0; B4DMV1; F5H6E6; Q7Z4I2; Q7Z4I6; Q7Z4I8; Q8NFE7; Q9HA13;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=LIM and senescent cell antigen-like-containing domain protein 2;
DE AltName: Full=LIM-like protein 2;
DE AltName: Full=Particularly interesting new Cys-His protein 2;
DE Short=PINCH-2;
GN Name=LIMS2; Synonyms=PINCH2;
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 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH ILK.
RX PubMed=12167643; DOI=10.1074/jbc.m205576200;
RA Zhang Y., Chen K., Guo L., Wu C.;
RT "Characterization of PINCH-2, a new focal adhesion protein that regulates
RT the PINCH-1-ILK interaction, cell spreading, and migration.";
RL J. Biol. Chem. 277:38328-38338(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Zeng W., Zhu Y., Jiao W., Yuan W., Wu X.;
RT "Cloning and characterization a novel human gene LIMS2.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Brain, and Lung;
RA Ding P., Han W., Cheng Y., Qiu X., Song Q., Zhang Y., Ma D.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Brain, and Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327 AND SER-328, AND
RP 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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 (ISOFORM 2), AND
RP IDENTIFICATION BY 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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-73 IN COMPLEX WITH ILK, AND
RP SUBUNIT.
RX PubMed=19963065; DOI=10.1016/j.jsb.2009.12.002;
RA Chiswell B.P., Stiegler A.L., Razinia Z., Nalibotski E., Boggon T.J.,
RA Calderwood D.A.;
RT "Structural basis of competition between PINCH1 and PINCH2 for binding to
RT the ankyrin repeat domain of integrin-linked kinase.";
RL J. Struct. Biol. 170:157-163(2010).
RN [12]
RP VARIANTS MDRCMTT LYS-92; LEU-97 AND PRO-323.
RX PubMed=25589244; DOI=10.1111/cge.12561;
RG FORGE Canada Consortium;
RA Chardon J.W., Smith A.C., Woulfe J., Pena E., Rakhra K., Dennie C.,
RA Beaulieu C., Huang L., Schwartzentruber J., Hawkins C., Harms M.B.,
RA Dojeiji S., Zhang M., Majewski J., Bulman D.E., Boycott K.M., Dyment D.A.;
RT "LIMS2 mutations are associated with a novel muscular dystrophy, severe
RT cardiomyopathy and triangular tongues.";
RL Clin. Genet. 88:558-564(2015).
CC -!- FUNCTION: Adapter protein in a cytoplasmic complex linking beta-
CC integrins to the actin cytoskeleton, bridges the complex to cell
CC surface receptor tyrosine kinases and growth factor receptors. Plays a
CC role in modulating cell spreading and migration.
CC {ECO:0000269|PubMed:12167643}.
CC -!- SUBUNIT: Interacts with TGFB1I1 (By similarity). Interacts with
CC integrin-linked protein kinase 1 (ILK) via the first LIM domain, and in
CC competition with LIMS1. Part of the heterotrimeric IPP complex composed
CC of integrin-linked kinase (ILK), LIMS1 or LIMS2, and PARVA.
CC {ECO:0000250, ECO:0000269|PubMed:12167643,
CC ECO:0000269|PubMed:19963065}.
CC -!- INTERACTION:
CC Q7Z4I7-4; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-22000977, EBI-5235340;
CC Q7Z4I7-5; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-10257651, EBI-739580;
CC Q7Z4I7-5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10257651, EBI-618309;
CC Q7Z4I7-5; Q6A162: KRT40; NbExp=3; IntAct=EBI-10257651, EBI-10171697;
CC Q7Z4I7-5; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-10257651, EBI-10172150;
CC Q7Z4I7-5; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10257651, EBI-10172290;
CC Q7Z4I7-5; Q99750: MDFI; NbExp=3; IntAct=EBI-10257651, EBI-724076;
CC Q7Z4I7-5; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-10257651, EBI-742948;
CC Q7Z4I7-5; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-10257651, EBI-945833;
CC Q7Z4I7-5; Q96PM5: RCHY1; NbExp=3; IntAct=EBI-10257651, EBI-947779;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cell junction, focal
CC adhesion {ECO:0000269|PubMed:12167643}. Cell membrane
CC {ECO:0000269|PubMed:12167643}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12167643}; Cytoplasmic side
CC {ECO:0000269|PubMed:12167643}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=LIM-like protein 2B;
CC IsoId=Q7Z4I7-1; Sequence=Displayed;
CC Name=2; Synonyms=LIM-like protein 2A;
CC IsoId=Q7Z4I7-2; Sequence=VSP_021917;
CC Name=3; Synonyms=LIM-like protein 2C;
CC IsoId=Q7Z4I7-3; Sequence=VSP_021916;
CC Name=4;
CC IsoId=Q7Z4I7-4; Sequence=VSP_045539;
CC Name=5;
CC IsoId=Q7Z4I7-5; Sequence=VSP_046078;
CC -!- DISEASE: Muscular dystrophy, autosomal recessive, with cardiomyopathy
CC and triangular tongue (MDRCMTT) [MIM:616827]: An autosomal recessive
CC muscular dystrophy characterized by childhood-onset of muscle weakness
CC progressing to a severe quadriparesis. Additionally, patients have
CC biventricular cardiac dysfunction due to dilated cardiomyopathy, and
CC macroglossia with a small tip resulting in a triangular tongue.
CC {ECO:0000269|PubMed:25589244}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM77350.1; Type=Frameshift; Evidence={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; AF484961; AAM97589.1; -; mRNA.
DR EMBL; AF520987; AAM77350.1; ALT_FRAME; mRNA.
DR EMBL; AF527764; AAQ09011.1; -; mRNA.
DR EMBL; AF527765; AAQ09012.1; -; mRNA.
DR EMBL; AF527766; AAQ09013.1; -; mRNA.
DR EMBL; AF527770; AAQ09017.1; -; mRNA.
DR EMBL; AK022470; BAB14047.1; -; mRNA.
DR EMBL; AK297645; BAG60013.1; -; mRNA.
DR EMBL; BX458594; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC010976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC074114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065816; AAH65816.1; -; mRNA.
DR CCDS; CCDS2147.1; -. [Q7Z4I7-2]
DR CCDS; CCDS54394.1; -. [Q7Z4I7-3]
DR CCDS; CCDS54395.1; -. [Q7Z4I7-1]
DR CCDS; CCDS54396.1; -. [Q7Z4I7-5]
DR CCDS; CCDS58725.1; -. [Q7Z4I7-4]
DR RefSeq; NP_001129509.2; NM_001136037.2. [Q7Z4I7-5]
DR RefSeq; NP_001154875.1; NM_001161403.1. [Q7Z4I7-1]
DR RefSeq; NP_001154876.1; NM_001161404.1. [Q7Z4I7-3]
DR RefSeq; NP_001243471.1; NM_001256542.1. [Q7Z4I7-4]
DR RefSeq; NP_060450.2; NM_017980.4. [Q7Z4I7-2]
DR PDB; 3IXE; X-ray; 1.90 A; B=11-73.
DR PDBsum; 3IXE; -.
DR AlphaFoldDB; Q7Z4I7; -.
DR SMR; Q7Z4I7; -.
DR BioGRID; 120808; 22.
DR CORUM; Q7Z4I7; -.
DR IntAct; Q7Z4I7; 18.
DR MINT; Q7Z4I7; -.
DR STRING; 9606.ENSP00000326888; -.
DR GlyGen; Q7Z4I7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z4I7; -.
DR PhosphoSitePlus; Q7Z4I7; -.
DR BioMuta; LIMS2; -.
DR DMDM; 74750091; -.
DR EPD; Q7Z4I7; -.
DR jPOST; Q7Z4I7; -.
DR MassIVE; Q7Z4I7; -.
DR MaxQB; Q7Z4I7; -.
DR PaxDb; Q7Z4I7; -.
DR PeptideAtlas; Q7Z4I7; -.
DR PRIDE; Q7Z4I7; -.
DR ProteomicsDB; 27166; -.
DR ProteomicsDB; 69191; -.
DR ProteomicsDB; 69192; -. [Q7Z4I7-1]
DR ProteomicsDB; 69193; -. [Q7Z4I7-2]
DR ProteomicsDB; 69194; -. [Q7Z4I7-3]
DR Antibodypedia; 55985; 157 antibodies from 22 providers.
DR DNASU; 55679; -.
DR Ensembl; ENST00000324938.9; ENSP00000326888.5; ENSG00000072163.20. [Q7Z4I7-2]
DR Ensembl; ENST00000355119.9; ENSP00000347240.4; ENSG00000072163.20. [Q7Z4I7-1]
DR Ensembl; ENST00000409254.1; ENSP00000386907.1; ENSG00000072163.20. [Q7Z4I7-4]
DR Ensembl; ENST00000409286.5; ENSP00000386252.1; ENSG00000072163.20. [Q7Z4I7-4]
DR Ensembl; ENST00000409455.5; ENSP00000386383.1; ENSG00000072163.20. [Q7Z4I7-3]
DR Ensembl; ENST00000409754.5; ENSP00000386345.1; ENSG00000072163.20. [Q7Z4I7-4]
DR Ensembl; ENST00000409808.6; ENSP00000386637.2; ENSG00000072163.20. [Q7Z4I7-3]
DR Ensembl; ENST00000410011.5; ENSP00000387002.1; ENSG00000072163.20. [Q7Z4I7-3]
DR Ensembl; ENST00000410038.5; ENSP00000386570.1; ENSG00000072163.20. [Q7Z4I7-4]
DR Ensembl; ENST00000545738.6; ENSP00000443794.2; ENSG00000072163.20. [Q7Z4I7-5]
DR GeneID; 55679; -.
DR KEGG; hsa:55679; -.
DR MANE-Select; ENST00000355119.9; ENSP00000347240.4; NM_001161403.3; NP_001154875.1.
DR UCSC; uc002tov.4; human. [Q7Z4I7-1]
DR CTD; 55679; -.
DR DisGeNET; 55679; -.
DR GeneCards; LIMS2; -.
DR HGNC; HGNC:16084; LIMS2.
DR HPA; ENSG00000072163; Tissue enhanced (intestine).
DR MalaCards; LIMS2; -.
DR MIM; 607908; gene.
DR MIM; 616827; phenotype.
DR neXtProt; NX_Q7Z4I7; -.
DR OpenTargets; ENSG00000072163; -.
DR Orphanet; 466801; LIMS2-related limb-girdle muscular dystrophy.
DR PharmGKB; PA30390; -.
DR VEuPathDB; HostDB:ENSG00000072163; -.
DR eggNOG; KOG2272; Eukaryota.
DR GeneTree; ENSGT00940000153518; -.
DR HOGENOM; CLU_001357_0_0_1; -.
DR InParanoid; Q7Z4I7; -.
DR OMA; FHEHCFV; -.
DR OrthoDB; 1593918at2759; -.
DR PhylomeDB; Q7Z4I7; -.
DR TreeFam; TF314113; -.
DR PathwayCommons; Q7Z4I7; -.
DR Reactome; R-HSA-446353; Cell-extracellular matrix interactions.
DR SignaLink; Q7Z4I7; -.
DR SIGNOR; Q7Z4I7; -.
DR BioGRID-ORCS; 55679; 18 hits in 1070 CRISPR screens.
DR ChiTaRS; LIMS2; human.
DR EvolutionaryTrace; Q7Z4I7; -.
DR GenomeRNAi; 55679; -.
DR Pharos; Q7Z4I7; Tbio.
DR PRO; PR:Q7Z4I7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q7Z4I7; protein.
DR Bgee; ENSG00000072163; Expressed in apex of heart and 160 other tissues.
DR ExpressionAtlas; Q7Z4I7; baseline and differential.
DR Genevisible; Q7Z4I7; HS.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0045216; P:cell-cell junction organization; IBA:GO_Central.
DR GO; GO:1990705; P:cholangiocyte proliferation; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:1904055; P:negative regulation of cholangiocyte proliferation; IEA:Ensembl.
DR GO; GO:2000346; P:negative regulation of hepatocyte proliferation; IEA:Ensembl.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR InterPro; IPR017351; PINCH_1-like.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24210; PTHR24210; 1.
DR Pfam; PF00412; LIM; 5.
DR PIRSF; PIRSF038003; PINCH; 1.
DR SMART; SM00132; LIM; 5.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Disease variant; LIM domain; Limb-girdle muscular dystrophy; Membrane;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..341
FT /note="LIM and senescent cell antigen-like-containing
FT domain protein 2"
FT /id="PRO_0000266011"
FT DOMAIN 13..74
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 76..133
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 138..195
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 196..255
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 256..315
FT /note="LIM zinc-binding 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..152
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_045539"
FT VAR_SEQ 1..5
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_021916"
FT VAR_SEQ 1..4
FT /note="MTGS -> MAARLGALAASGLYRRRQHRQSPPPATG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_021917"
FT VAR_SEQ 3
FT /note="G -> GRKRKWGETGTGSGAAPAAALRW (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046078"
FT VARIANT 92
FT /note="N -> K (in MDRCMTT; unknown pathological
FT significance; dbSNP:rs754385302)"
FT /evidence="ECO:0000269|PubMed:25589244"
FT /id="VAR_076527"
FT VARIANT 97
FT /note="P -> L (in MDRCMTT; unknown pathological
FT significance; dbSNP:rs768056213)"
FT /evidence="ECO:0000269|PubMed:25589244"
FT /id="VAR_076528"
FT VARIANT 323
FT /note="L -> P (in MDRCMTT; unknown pathological
FT significance; dbSNP:rs869025562)"
FT /evidence="ECO:0000269|PubMed:25589244"
FT /id="VAR_076529"
FT CONFLICT 111
FT /note="D -> G (in Ref. 5; BAG60013)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="N -> D (in Ref. 1; AAM97589 and 6; BAB14047)"
FT /evidence="ECO:0000305"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:3IXE"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3IXE"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3IXE"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:3IXE"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:3IXE"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3IXE"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3IXE"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3IXE"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:3IXE"
FT MOD_RES Q7Z4I7-2:22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 341 AA; 38916 MW; EEA8D74C309D9C8A CRC64;
MTGSNMSDAL ANAVCQRCQA RFSPAERIVN SNGELYHEHC FVCAQCFRPF PEGLFYEFEG
RKYCEHDFQM LFAPCCGSCG EFIIGRVIKA MNNNWHPGCF RCELCDVELA DLGFVKNAGR
HLCRPCHNRE KAKGLGKYIC QRCHLVIDEQ PLMFRSDAYH PDHFNCTHCG KELTAEAREL
KGELYCLPCH DKMGVPICGA CRRPIEGRVV NALGKQWHVE HFVCAKCEKP FLGHRHYEKK
GLAYCETHYN QLFGDVCYNC SHVIEGDVVS ALNKAWCVSC FSCSTCNSKL TLKNKFVEFD
MKPVCKRCYE KFPLELKKRL KKLSELTSRK AQPKATDLNS A
