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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
 
 
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