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NPASH_CAEEL
ID   NPASH_CAEEL             Reviewed;         676 AA.
AC   G5EFL9;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=PAS domain-containing protein cky-1 {ECO:0000305};
DE   AltName: Full=CKY homolog {ECO:0000312|WormBase:C15C8.2};
DE   AltName: Full=bHLH-PAS transcription factor cky-1 {ECO:0000303|PubMed:17628356};
GN   Name=cky-1 {ECO:0000312|WormBase:C15C8.2};
GN   Synonyms=cNXFL {ECO:0000312|EMBL:BAE53417.1};
GN   ORFNames=C15C8.2 {ECO:0000312|WormBase:C15C8.2};
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|EMBL:BAE53417.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INTERACTION WITH AHA-1, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=17628356; DOI=10.1016/j.gene.2007.06.005;
RA   Ooe N., Saito K., Oeda K., Nakatuka I., Kaneko H.;
RT   "Characterization of Drosophila and Caenorhabditis elegans NXF-like-
RT   factors, putative homologs of mammalian NXF.";
RL   Gene 400:122-130(2007).
RN   [2] {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).
CC   -!- FUNCTION: Transcription factor (PubMed:17628356). Efficient DNA binding
CC       requires dimerization with another bHLH protein, such as ARNT homolog
CC       aha-1 (PubMed:17628356). Regulates transcription of target genes,
CC       probably acting in complex with aha-1 (PubMed:17628356).
CC       {ECO:0000269|PubMed:17628356}.
CC   -!- SUBUNIT: Heterodimer; efficient DNA binding requires dimerization with
CC       another bHLH protein (PubMed:17628356). Forms a heterodimer with ARNT
CC       homolog aha-1; binds DNA as heterodimer (PubMed:17628356).
CC       {ECO:0000269|PubMed:17628356}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC       ECO:0000303|PubMed:17628356}.
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DR   EMBL; AB096001; BAE53417.1; -; mRNA.
DR   EMBL; BX284605; CAP46770.1; -; Genomic_DNA.
DR   PIR; T19307; T19307.
DR   RefSeq; NP_001122849.1; NM_001129377.2.
DR   RefSeq; NP_506184.2; NM_073783.4.
DR   SMR; G5EFL9; -.
DR   IntAct; G5EFL9; 3.
DR   STRING; 6239.C15C8.2b; -.
DR   EnsemblMetazoa; C15C8.2.1; C15C8.2.1; WBGene00000521.
DR   GeneID; 179743; -.
DR   KEGG; cel:CELE_C15C8.2; -.
DR   CTD; 179743; -.
DR   WormBase; C15C8.2; CE41867; WBGene00000521; cky-1.
DR   eggNOG; ENOG502QRXX; Eukaryota.
DR   GeneTree; ENSGT00530000064165; -.
DR   HOGENOM; CLU_430370_0_0_1; -.
DR   OMA; MLMVTRS; -.
DR   OrthoDB; 572843at2759; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000521; Expressed in pharyngeal muscle cell (C elegans) and 2 other tissues.
DR   GO; GO:0005634; C:nucleus; IC:WormBase.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:WormBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00130; PAS; 2.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..676
FT                   /note="PAS domain-containing protein cky-1"
FT                   /id="PRO_0000456247"
FT   DOMAIN          76..129
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   DOMAIN          165..215
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   REGION          76..89
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          90..129
FT                   /note="Helix-loop-helix motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
SQ   SEQUENCE   676 AA;  75796 MW;  C5A399EC78BA315C CRC64;
     MSTTVPLHAS SFSSGTTGAG GGVQQALQLQ HCAYHVGASV GSSGSALNNN SINVPNNNTM
     GMSSAGSSNG SNLVNGQQRS TRGASKQRRD QINVEIQKLR DLLPLSDLIK DRLFQLQVMS
     LGCIFIRKHR YQQTVLQPQL QMLQMQMSSP MPRGIDICKA LRGFMLMVTR SGKILHVSDN
     ASEYLGHSVE EIMCQGDSIY DLVDGRDHGA VQAELASGPP GAATFPEERV FICRLNLART
     AKRQLQYHKF VLFQGRYIQP AEFYQQLNAQ NSQPDCDQPV FSAYCQPLIN PENAEGMSTG
     NTHVFSTQHY LDMKFKEADT MASQHLGFSK EQLKGMSWYG MIHPNHVPEI AHKHRLLCQE
     KEGSVLALIR LQAANGEWIW LHTVFSIRPN NELNSDGKRL RHVIHCFHQK LTDLEAATLQ
     ANSWIYSMRH TYPTVFSCQD SPPPSEEQQP SSPQTPPFTE QPPMLVEQKP LIGAGIAPGF
     PSLDYNQIKV EIPMRPINTQ IPLFTPESSS PESSASLHTS LLPHHNAFPL DILEDILPSN
     DVLPELKDEV DEILRQVEQS PATSPAHSFP SNVNFGHRHS MPNAFDSAEL YKYLGPALFD
     GNFAMQHQHH LQQQHQSQPN HPLQMTPIPP MSCPPSNYGQ SNFLFHHQHL NQHLHHSQPP
     HPYHFDYYNR KRSWAV
 
 
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