ID UNC97_CAEEL Reviewed; 348 AA. AC P50464; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 163. DE RecName: Full=LIM domain-containing protein unc-97; DE AltName: Full=PINCH homolog; DE AltName: Full=Uncoordinated protein 97; GN Name=unc-97 {ECO:0000312|WormBase:F14D12.2}; GN ORFNames=F14D12.2 {ECO:0000312|WormBase:F14D12.2}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Bristol N2; RX PubMed=9885243; DOI=10.1083/jcb.144.1.45; RA Hobert O., Moerman D.G., Clark K.A., Beckerle M.C., Ruvkun G.; RT "A conserved LIM protein that affects muscular adherens junction integrity RT and mechanosensory function in Caenorhabditis elegans."; RL J. Cell Biol. 144:45-57(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [3] RP INTERACTION WITH UNC-98. RX PubMed=12808046; DOI=10.1091/mbc.e02-10-0676; RA Mercer K.B., Flaherty D.B., Miller R.K., Qadota H., Tinley T.L., RA Moerman D.G., Benian G.M.; RT "Caenorhabditis elegans UNC-98, a C2H2 Zn finger protein, is a novel RT partner of UNC-97/PINCH in muscle adhesion complexes."; RL Mol. Biol. Cell 14:2492-2507(2003). RN [4] RP FUNCTION, COMPONENT OF AN INTEGRIN CONTAINING ATTACHMENT COMPLEX, AND RP DISRUPTION PHENOTYPE. RX PubMed=22253611; DOI=10.1371/journal.pgen.1002471; RA Etheridge T., Oczypok E.A., Lehmann S., Fields B.D., Shephard F., RA Jacobson L.A., Szewczyk N.J.; RT "Calpains mediate integrin attachment complex maintenance of adult muscle RT in Caenorhabditis elegans."; RL PLoS Genet. 8:E1002471-E1002471(2012). CC -!- FUNCTION: Component of an integrin containing attachment complex, which CC is required for muscle development and maintenance (PubMed:22253611). CC Probably function in adherens junction (PubMed:12808046). Affects the CC structural integrity of the integrin containing muscle adherens CC junctions and contributes to the mechanosensory functions of touch CC neurons (PubMed:12808046). {ECO:0000269|PubMed:12808046, CC ECO:0000269|PubMed:22253611}. CC -!- SUBUNIT: Interacts with unc-98 (PubMed:12808046). Component of an CC integrin containing attachment complex, composed of at least pat-2, CC pat-3, pat-4, pat-6, unc-52, unc-97 and unc-112 (PubMed:22253611). CC {ECO:0000269|PubMed:12808046, ECO:0000269|PubMed:22253611}. CC -!- INTERACTION: CC P50464; Q09497: rsu-1; NbExp=5; IntAct=EBI-319593, EBI-319599; CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Nucleus. CC -!- TISSUE SPECIFICITY: Restricted to tissue types that attach to the CC hypodermis, specifically body wall muscles, vulval muscles, and CC mechanosensory neurons. CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in impaired CC mobility, mitochondrial fragmentation and disrupted integrin attachment CC complexes in muscle. This leads to degradation of muscle proteins in CC the cytosol, myofibrillar defects and disruption of sarcomere CC organization. {ECO:0000269|PubMed:22253611}. 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; AF035583; AAD09435.1; -; mRNA. DR EMBL; BX284606; CCD83467.1; -; Genomic_DNA. DR PIR; T16076; T16076. DR RefSeq; NP_508943.3; NM_076542.5. DR AlphaFoldDB; P50464; -. DR SMR; P50464; -. DR BioGRID; 45760; 24. DR DIP; DIP-24818N; -. DR IntAct; P50464; 5. DR STRING; 6239.F14D12.2.1; -. DR EPD; P50464; -. DR PaxDb; 6239-F14D12-2-1; -. DR PeptideAtlas; P50464; -. DR EnsemblMetazoa; F14D12.2.1; F14D12.2.1; WBGene00006826. DR GeneID; 180827; -. DR KEGG; cel:CELE_F14D12.2; -. DR UCSC; F14D12.2.1; c. elegans. DR AGR; WB:WBGene00006826; -. DR WormBase; F14D12.2; CE04392; WBGene00006826; unc-97. DR eggNOG; KOG2272; Eukaryota. DR GeneTree; ENSGT00940000153518; -. DR HOGENOM; CLU_001357_0_0_1; -. DR InParanoid; P50464; -. DR OMA; VCAQCFE; -. DR OrthoDB; 370973at2759; -. DR PhylomeDB; P50464; -. DR Reactome; R-CEL-446353; Cell-extracellular matrix interactions. DR Reactome; R-CEL-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components. DR PRO; PR:P50464; -. DR Proteomes; UP000001940; Chromosome X. DR Bgee; WBGene00006826; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues. DR GO; GO:0005912; C:adherens junction; IDA:WormBase. DR GO; GO:0009925; C:basal plasma membrane; IDA:WormBase. DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central. DR GO; GO:0031430; C:M band; IDA:WormBase. DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase. DR GO; GO:0005634; C:nucleus; IDA:WormBase. DR GO; GO:0055120; C:striated muscle dense body; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017022; F:myosin binding; IPI:UniProtKB. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0045216; P:cell-cell junction organization; IMP:WormBase. DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB. DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB. DR GO; GO:0007517; P:muscle organ development; IMP:WormBase. DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB. DR GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:UniProtKB. DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IBA:GO_Central. DR GO; GO:0050954; P:sensory perception of mechanical stimulus; IMP:WormBase. 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; LIM DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR24210:SF0; 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. PE 1: Evidence at protein level; KW Cell junction; LIM domain; Metal-binding; Nucleus; Reference proteome; KW Repeat; Zinc. FT CHAIN 1..348 FT /note="LIM domain-containing protein unc-97" FT /id="PRO_0000075909" FT DOMAIN 21..73 FT /note="LIM zinc-binding 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 82..132 FT /note="LIM zinc-binding 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 146..196 FT /note="LIM zinc-binding 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 205..255 FT /note="LIM zinc-binding 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 264..315 FT /note="LIM zinc-binding 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" SQ SEQUENCE 348 AA; 40308 MW; 0CD22C39628ECEDA CRC64; MDSDHNHING DLAHGFENMV CVRCNDGFSM QDQMVNSSGQ VWHSECFVCA QCFEPFPDGI YFEYEGRKYC EHDFHVLFSP CCGKCNEFIV GRVIKAMNAS WHPGCFCCEI CNKQLADVGF LRNAGRALCR ECNEREKAAG HGRYVCHKCH AMIDDGQHIK FRGDSFHPYH FKCKRCNNEL TTASREVNGE LYCLRCHDTM GIPICGACHR PIEERVIAAL GKHWHVEHFV CSVCEKPFLG HRHYERKGLP YCEQHFHKLF GNLCFKCGDP CCGEVFQALQ KTWCVKCFSC SFCDKKLDQK TKFYEFDMKP TCKRCYDRFP TELKKRISES LKDRDVENQR RSMSPGPK //