UNC97_CAEEL
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 03-AUG-2022, entry version 156.
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}.
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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; 23.
DR DIP; DIP-24818N; -.
DR IntAct; P50464; 5.
DR STRING; 6239.F14D12.2.1; -.
DR EPD; P50464; -.
DR PaxDb; P50464; -.
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 CTD; 180827; -.
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; 1593918at2759; -.
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 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 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 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
