UNC95_CAEEL
ID UNC95_CAEEL Reviewed; 350 AA.
AC Q9NEZ5;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=LIM domain-containing protein unc-95 {ECO:0000303|PubMed:15210732};
GN Name=unc-95 {ECO:0000312|WormBase:Y105E8A.6};
GN ORFNames=Y105E8A.6 {ECO:0000312|WormBase:Y105E8A.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 144-GLN--ILE-350.
RX PubMed=15210732; DOI=10.1083/jcb.200401133;
RA Broday L., Kolotuev I., Didier C., Bhoumik A., Podbilewicz B., Ronai Z.;
RT "The LIM domain protein UNC-95 is required for the assembly of muscle
RT attachment structures and is regulated by the RING finger protein RNF-5 in
RT C. elegans.";
RL J. Cell Biol. 165:857-867(2004).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND UBIQUITINATION BY RNF-5.
RX PubMed=20385102; DOI=10.1016/j.bbrc.2010.04.049;
RA Zaidel-Bar R., Miller S., Kaminsky R., Broday L.;
RT "Molting-specific downregulation of C. elegans body-wall muscle attachment
RT sites: the role of RNF-5 E3 ligase.";
RL Biochem. Biophys. Res. Commun. 395:509-514(2010).
CC -!- FUNCTION: Required for the assembly and integrity of muscle dense
CC bodies, which establish the adhesion sites of the muscle cells to the
CC extracellular matrix (PubMed:15210732, PubMed:20385102). Decreased
CC localization of unc-95 to dense bodies and their subsequent
CC dissociation plays an important role in ecdysis during molting
CC (PubMed:20385102). Involved in the organization of the muscle
CC sarcomeric structure and thereby required for locomotion
CC (PubMed:15210732). {ECO:0000269|PubMed:15210732,
CC ECO:0000269|PubMed:20385102}.
CC -!- INTERACTION:
CC Q9NEZ5; Q17549: magu-2; NbExp=3; IntAct=EBI-2913259, EBI-317283;
CC Q9NEZ5; Q9NAN2: par-6; NbExp=3; IntAct=EBI-2913259, EBI-318782;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15210732,
CC ECO:0000269|PubMed:20385102}. Nucleus {ECO:0000269|PubMed:15210732,
CC ECO:0000269|PubMed:20385102}. Cell membrane
CC {ECO:0000269|PubMed:15210732, ECO:0000269|PubMed:20385102}; Peripheral
CC membrane protein {ECO:0000305}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:15210732}. Cell junction
CC {ECO:0000269|PubMed:15210732, ECO:0000269|PubMed:20385102}. Cell
CC junction, focal adhesion {ECO:0000269|PubMed:15210732,
CC ECO:0000269|PubMed:20385102}. Note=Localized in the cytoplasm in comma
CC stage embryos, and gradually becomes more localized at the membrane in
CC the 1.5- and 2-fold stage embryos. In the threefold embryo, associated
CC with dense bodies at the cell membrane, but also present in the
CC cytoplasm. Nuclear localization from the threefold stage embryo as
CC well. In adult animals, localized in dense bodies, M-lines, muscle-
CC muscle cell boundaries, cytoplasm and nucleus (PubMed:15210732).
CC Decreased localization to dense bodies during the L2/L3 molt
CC (PubMed:20385102). {ECO:0000269|PubMed:15210732,
CC ECO:0000269|PubMed:20385102}.
CC -!- TISSUE SPECIFICITY: Expressed in the body wall muscles, vulval muscles
CC and the anal muscles (PubMed:15210732, PubMed:20385102). Expressed in
CC the muscle arms of the head muscle cells that form neuromuscular
CC junctions and in the anal depressor muscle (PubMed:15210732).
CC {ECO:0000269|PubMed:15210732, ECO:0000269|PubMed:20385102}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis, in larvae and in
CC adult animals. {ECO:0000269|PubMed:15210732,
CC ECO:0000269|PubMed:20385102}.
CC -!- PTM: Ubiquitinated. Ubiquitination by rnf-5 leads to dissociation from
CC muscle dense bodies during molting and is required for ecdysis.
CC {ECO:0000269|PubMed:20385102}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown leads to disorganized
CC actin-containing I band filaments, disorganized dense bodies in the
CC muscles and reduced motility. {ECO:0000269|PubMed:15210732}.
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DR EMBL; BX284601; CAC48121.2; -; Genomic_DNA.
DR RefSeq; NP_740934.2; NM_170938.4.
DR AlphaFoldDB; Q9NEZ5; -.
DR IntAct; Q9NEZ5; 3.
DR STRING; 6239.Y105E8A.6; -.
DR EPD; Q9NEZ5; -.
DR PaxDb; Q9NEZ5; -.
DR PeptideAtlas; Q9NEZ5; -.
DR EnsemblMetazoa; Y105E8A.6.1; Y105E8A.6.1; WBGene00006824.
DR GeneID; 173301; -.
DR KEGG; cel:CELE_Y105E8A.6; -.
DR UCSC; Y105E8A.6; c. elegans.
DR CTD; 173301; -.
DR WormBase; Y105E8A.6; CE31857; WBGene00006824; unc-95.
DR eggNOG; KOG1703; Eukaryota.
DR HOGENOM; CLU_071917_0_0_1; -.
DR InParanoid; Q9NEZ5; -.
DR OMA; QKALNMH; -.
DR OrthoDB; 1015993at2759; -.
DR PRO; PR:Q9NEZ5; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006824; Expressed in larva and 3 other tissues.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0019904; F:protein domain specific binding; IPI:WormBase.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00132; LIM; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Coiled coil; Cytoplasm; LIM domain; Membrane;
KW Metal-binding; Nucleus; Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..350
FT /note="LIM domain-containing protein unc-95"
FT /id="PRO_0000445243"
FT DOMAIN 268..334
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 83..110
FT /evidence="ECO:0000255"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 144..350
FT /note="Missing: In su33; loss of localization to muscle-
FT muscle cell boundaries. Aberrant sarcomeric structure in
FT the muscle with disorganized actin-containing filaments (I
FT band), myosin-containing filaments (A band), M-lines and
FT disorganized dense bodies, indicating a failure to assemble
FT normal muscle adhesion structures. Loss of recruitment of
FT deb-1/vinculin to nascent muscle attachments during
FT embryogenesis."
FT /evidence="ECO:0000269|PubMed:15210732"
SQ SEQUENCE 350 AA; 40457 MW; B6C26EE60668A449 CRC64;
MTISPQPSHQ QFESYQWTTE SRSSQQRHGT GTPSQDGRLS AIPDPVERHV ARWRSESRNS
NKDKVFRNDE EFSQQDEIVN GTLTALKNDV EQTTEIIRRK QEQMRMERRQ FQTEMEVNGR
ISIDPTDDWL AARLKAVSSD DMNQQLVKLK QDQRQNAVTD TLAALVYDVN ATTEVLRRGQ
RGRDGEDGNK KKKEEIEYTL RLTPAPEEQI PQRPKIPEDD NMETDDYSRQ YGVQMSEETD
SLRRRRARST TPRRTLHISG SPPPPAAAVC AYCSEEIDGA ILTALAPNSE RAQKFHTYHF
MCTYCQKALN MHGTYREHDL KPYCHDCFYK LYNGLQYAPD DHQASIEKLI
