UNC98_CAEEL
ID UNC98_CAEEL Reviewed; 310 AA.
AC Q19203; Q8MUP9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Zinc finger protein unc-98;
DE AltName: Full=Uncoordinated protein 98;
GN Name=unc-98; ORFNames=F08C6.7;
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], FUNCTION, INTERACTION WITH HUM-6; MEP-1 AND
RP UNC-97, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
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 [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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7348600; DOI=10.1002/cm.970010107;
RA Zengel J.M., Epstein H.F.;
RT "Identification of genetic elements associated with muscle structure in the
RT nematode Caenorhabditis elegans.";
RL Cell Motil. 1:73-97(1980).
RN [4]
RP FUNCTION, INTERACTION WITH MYO-3, AND TISSUE SPECIFICITY.
RX PubMed=17158957; DOI=10.1083/jcb.200608043;
RA Miller R.K., Qadota H., Landsverk M.L., Mercer K.B., Epstein H.F.,
RA Benian G.M.;
RT "UNC-98 links an integrin-associated complex to thick filaments in
RT Caenorhabditis elegans muscle.";
RL J. Cell Biol. 175:853-859(2006).
RN [5]
RP INTERACTION WITH UNC-96.
RX PubMed=16790495; DOI=10.1091/mbc.e06-02-0144;
RA Mercer K.B., Miller R.K., Tinley T.L., Sheth S., Qadota H., Benian G.M.;
RT "Caenorhabditis elegans UNC-96 is a new component of M-lines that interacts
RT with UNC-98 and paramyosin and is required in adult muscle for assembly
RT and/or maintenance of thick filaments.";
RL Mol. Biol. Cell 17:3832-3847(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27123983; DOI=10.1371/journal.pgen.1006010;
RA D'Souza S.A., Rajendran L., Bagg R., Barbier L., van Pel D.M., Moshiri H.,
RA Roy P.J.;
RT "The MADD-3 LAMMER kinase interacts with a p38 MAP kinase pathway to
RT regulate the display of the EVA-1 guidance receptor in Caenorhabditis
RT elegans.";
RL PLoS Genet. 12:E1006010-E1006010(2016).
CC -!- FUNCTION: Probable transcription factor required for muscle structure
CC (PubMed:12808046, PubMed:7348600). Its dual subcellular localization
CC suggests that it may function both as a muscle adhesion complex protein
CC and as a transcription factor, or work together with transcription
CC factors, to influence gene expression (PubMed:12808046). Thought to act
CC as a molecular bridge between unc-97 and myo-3 at the M-line of
CC muscles, possibly in a signaling role (PubMed:17158957). Plays a role
CC in the formation of muscle connections, also called muscle arm
CC extensions, between the body wall and the motor axons in the dorsal and
CC ventral cord (PubMed:27123983). {ECO:0000269|PubMed:12808046,
CC ECO:0000269|PubMed:17158957, ECO:0000269|PubMed:27123983,
CC ECO:0000269|PubMed:7348600}.
CC -!- SUBUNIT: Interacts with hum-6, mep-1, myo-3, unc-96 and unc-97/PINCH.
CC {ECO:0000269|PubMed:12808046, ECO:0000269|PubMed:16790495,
CC ECO:0000269|PubMed:17158957}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12808046}. Cytoplasm
CC {ECO:0000269|PubMed:12808046}. Note=Localized in body wall muscle M-
CC lines, dense bodies and muscle nuclei.
CC -!- TISSUE SPECIFICITY: Expressed in embryos from 1.5- to 2-fold stage in
CC myofibrils. In larvae and adults, it is expressed in body wall muscle,
CC and in addition, anal depressor muscle and vulval muscles. More
CC specifically it is found in the thick filaments of muscle fibers.
CC {ECO:0000269|PubMed:12808046, ECO:0000269|PubMed:17158957}.
CC -!- DOMAIN: The N-terminal part (1-106) mediates the nuclear localization,
CC while the fourth zinc finger is required for the localization to M-
CC lines and dense bodies. {ECO:0000269|PubMed:12808046}.
CC -!- DISRUPTION PHENOTYPE: Disorganised A and I bands in body-wall muscle
CC structure (PubMed:7348600). Defective extension of body wall muscle
CC connections or arms towards the ventral nerve cord (PubMed:27123983).
CC Double knockout with madd-3 results in severe muscle arm extension
CC defects (PubMed:27123983). {ECO:0000269|PubMed:27123983,
CC ECO:0000269|PubMed:7348600}.
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DR EMBL; AF515600; AAM76039.1; -; mRNA.
DR EMBL; FO080866; CCD67350.1; -; Genomic_DNA.
DR PIR; T15974; T15974.
DR RefSeq; NP_509284.2; NM_076883.6.
DR AlphaFoldDB; Q19203; -.
DR BioGRID; 45944; 58.
DR DIP; DIP-25572N; -.
DR IntAct; Q19203; 50.
DR MINT; Q19203; -.
DR STRING; 6239.F08C6.7; -.
DR EPD; Q19203; -.
DR PaxDb; Q19203; -.
DR PeptideAtlas; Q19203; -.
DR PRIDE; Q19203; -.
DR EnsemblMetazoa; F08C6.7.1; F08C6.7.1; WBGene00006827.
DR GeneID; 181020; -.
DR KEGG; cel:CELE_F08C6.7; -.
DR UCSC; F08C6.7; c. elegans.
DR CTD; 181020; -.
DR WormBase; F08C6.7; CE31900; WBGene00006827; unc-98.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00970000196069; -.
DR HOGENOM; CLU_078605_0_0_1; -.
DR InParanoid; Q19203; -.
DR OMA; HERIHDV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q19203; -.
DR SignaLink; Q19203; -.
DR PRO; PR:Q19203; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006827; Expressed in larva and 3 other tissues.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
DR GO; GO:0040011; P:locomotion; IMP:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IMP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0030239; P:myofibril assembly; IMP:UniProtKB.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW Metal-binding; Muscle protein; Myogenesis; Nucleus; Reference proteome;
KW Repeat; Thick filament; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..310
FT /note="Zinc finger protein unc-98"
FT /id="PRO_0000046896"
FT ZN_FING 113..135
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 141..163
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 169..188
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 246..268
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 73..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..310
FT /note="Interaction with myo-3"
FT COMPBIAS 73..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 310 AA; 35353 MW; F052E8CD0BA3AAB1 CRC64;
MDDDIFKEAR KERDDFEELM NACDLAKMSV KNNEMVHGLE TFGINGESSE NGNKEKPKEI
MKVVAPTVEA YVGSSSAQTP TKSSGGALDG SDQQEVRQDG TSVQKDDNGF VFYKCRFCGL
TFNFMNTLRA HERIHDVSQP YVCGKCGDSF EFACQLEYHA AQHSEIDGYK CECGRTFFSY
TEMLYHKHTD DPLELIGAPE TTTIKVSKKR VLPVSEQDLP QPAFVTEGYE PKHPLRVYND
VRSKPYICEY CSKSYSDSRG LAYHMYSHRG EKYFNPRASR YMMGREGVGY TDSRSYYLFP
RTSGYVTPRF
