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   27-MAR-2024, entry version 161.
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};
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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; 9606-ENSP00000326888; -.
DR   PeptideAtlas; Q7Z4I7; -.
DR   ProteomicsDB; 27166; -.
DR   ProteomicsDB; 69191; -.
DR   ProteomicsDB; 69192; -. [Q7Z4I7-1]
DR   ProteomicsDB; 69193; -. [Q7Z4I7-2]
DR   ProteomicsDB; 69194; -. [Q7Z4I7-3]
DR   Pumba; Q7Z4I7; -.
DR   Antibodypedia; 55985; 180 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   AGR; HGNC:16084; -.
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   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; 370973at2759; -.
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; 20 hits in 1148 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 162 other cell types or tissues.
DR   ExpressionAtlas; Q7Z4I7; baseline and differential.
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   CDD; cd09331; LIM1_PINCH; 1.
DR   CDD; cd09332; LIM2_PINCH; 1.
DR   CDD; cd09333; LIM3_PINCH; 1.
DR   CDD; cd09334; LIM4_PINCH; 1.
DR   CDD; cd09335; LIM5_PINCH; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 5.
DR   InterPro; IPR047944; LIMS1/2-like_LIM1.
DR   InterPro; IPR047946; PINCH-1/2-like.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24210:SF10; LIM AND SENESCENT CELL ANTIGEN-LIKE-CONTAINING DOMAIN PROTEIN 2; 1.
DR   PANTHER; PTHR24210; LIM DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00412; LIM; 5.
DR   PIRSF; PIRSF038003; PINCH; 1.
DR   SMART; SM00132; LIM; 5.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 6.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 5.
DR   Genevisible; Q7Z4I7; HS.
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; uncertain significance;
FT                   dbSNP:rs754385302)"
FT                   /evidence="ECO:0000269|PubMed:25589244"
FT                   /id="VAR_076527"
FT   VARIANT         97
FT                   /note="P -> L (in MDRCMTT; uncertain significance;
FT                   dbSNP:rs768056213)"
FT                   /evidence="ECO:0000269|PubMed:25589244"
FT                   /id="VAR_076528"
FT   VARIANT         323
FT                   /note="L -> P (in MDRCMTT; uncertain significance;
FT                   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
//