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LE607_CAEEL
ID   LE607_CAEEL             Reviewed;         690 AA.
AC   O44743;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=CREB-H transcription factor homolog let-607 {ECO:0000303|PubMed:24811939};
DE   AltName: Full=Lethal 607 protein {ECO:0000312|WormBase:F57B10.1};
GN   Name=let-607 {ECO:0000312|WormBase:F57B10.1};
GN   ORFNames=F57B10.1 {ECO:0000312|WormBase:F57B10.1};
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, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=24811939; DOI=10.1002/dvdy.24146;
RA   Wong M.C., Kennedy W.P., Schwarzbauer J.E.;
RT   "Transcriptionally regulated cell adhesion network dictates distal tip cell
RT   directionality.";
RL   Dev. Dyn. 243:999-1010(2014).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27510972; DOI=10.1242/dev.140046;
RA   Weicksel S.E., Mahadav A., Moyle M., Cipriani P.G., Kudron M., Pincus Z.,
RA   Bahmanyar S., Abriola L., Merkel J., Gutwein M., Fernandez A.G., Piano F.,
RA   Gunsalus K.C., Reinke V.;
RT   "A novel small molecule that disrupts a key event during the oocyte-to-
RT   embryo transition in C. elegans.";
RL   Development 143:3540-3548(2016).
CC   -!- FUNCTION: Probable transcription factor, required during migration of
CC       the gonadal distal tip cells (DTC) (PubMed:24811939). Probably
CC       regulates cell adhesion of DTCs via modulation of expression of genes
CC       involved in integrin-mediated adhesion, including tln-1, src-1, and
CC       integrin pat-2 (PubMed:24811939). Modulates expression of genes
CC       involved in protein trafficking during embryogenesis, including emo-1,
CC       sec-61, calu-1, sec-24.1, enpl-1, sar-1 and tfg-1 (PubMed:27510972).
CC       {ECO:0000269|PubMed:24811939, ECO:0000269|PubMed:27510972}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the gonadal distal tip cells (DTC)
CC       during larval stages L2, L3 and L4. {ECO:0000269|PubMed:24811939}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown targeted to the gonadal
CC       distal tip cells (DTC) causes DTC migration defects (PubMed:24811939).
CC       Significant reduction in expression of src-1 and tln-1 in DTCs
CC       (PubMed:24811939). Causes slow growth after hatching (PubMed:27510972).
CC       {ECO:0000269|PubMed:24811939, ECO:0000269|PubMed:27510972}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR   EMBL; BX284601; CCD71470.1; -; Genomic_DNA.
DR   PIR; T32750; T32750.
DR   RefSeq; NP_491897.2; NM_059496.6.
DR   AlphaFoldDB; O44743; -.
DR   SMR; O44743; -.
DR   IntAct; O44743; 4.
DR   STRING; 6239.F57B10.1.1; -.
DR   EPD; O44743; -.
DR   PaxDb; O44743; -.
DR   PeptideAtlas; O44743; -.
DR   EnsemblMetazoa; F57B10.1.1; F57B10.1.1; WBGene00002783.
DR   EnsemblMetazoa; F57B10.1.2; F57B10.1.2; WBGene00002783.
DR   GeneID; 266837; -.
DR   KEGG; cel:CELE_F57B10.1; -.
DR   UCSC; F57B10.1.1; c. elegans.
DR   CTD; 266837; -.
DR   WormBase; F57B10.1; CE37244; WBGene00002783; let-607.
DR   eggNOG; KOG0709; Eukaryota.
DR   HOGENOM; CLU_401277_0_0_1; -.
DR   InParanoid; O44743; -.
DR   OMA; FEDQCDA; -.
DR   OrthoDB; 1007856at2759; -.
DR   Reactome; R-CEL-8874211; CREB3 factors activate genes.
DR   SignaLink; O44743; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00002783; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0000785; C:chromatin; IMP:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR   GO; GO:0090038; P:negative regulation of protein kinase C signaling; IGI:WormBase.
DR   GO; GO:0008361; P:regulation of cell size; IMP:WormBase.
DR   GO; GO:1903354; P:regulation of distal tip cell migration; IMP:UniProtKB.
DR   GO; GO:2000114; P:regulation of establishment of cell polarity; IGI:WormBase.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   Pfam; PF00170; bZIP_1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Developmental protein; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..690
FT                   /note="CREB-H transcription factor homolog let-607"
FT                   /id="PRO_0000452349"
FT   DOMAIN          284..347
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          87..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..321
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          326..333
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          451..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          295..350
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        91..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   690 AA;  75901 MW;  C3344DD9D95F0AA8 CRC64;
     MDQDFDLDEG AGQFNLKTTL MMFTSNDSQN DDGIWSPGSP YQALEDPSFL DKHFVSDPDR
     YTADELYSAL EKMDGKSDLI GMDDMDNDNC YSLSPPDSGS LPISPASTSP SSYHSSGGED
     LMDCYPSIDI LQQASEELLY SKDDDYEICS SGPLLAYTNA NSVATSAVHQ NQQQQQRRLN
     QAGFPHQNSN GLVRFKSSQP RVLNPASISL NAPSSSFNPQ STSSTPATSS SSSSSTNGGF
     VKSSTGERRK YPPLRLDEEE IKLCKKEGIC LPDFFPLTKA EERDLKRIRR KIRNKRSAQT
     SRKRKQDYIE QLEDRVSEST KENQALKQQI ERLSSENQSV ISQLKKLQAQ LGQNAKRTTQ
     AGRCLAVFML SACLLVSPQL SPLGNQDNQK VLECIEEACQ PSATSMNSAN SAQRAIAGVT
     APSVVIPSGG PVMVSTNANR QMNRNAVLNH HNNSKYPASG NQNHHPIALE DLNHPPPTLQ
     PKQSYQQQHQ PSMYRRSDET IAMAMAKIGA RKGSSTSSSS ASSVASSTST SSATSPIYRT
     SRTLGAFEDQ CDASSDDSNC ANMPSLVPMK MSAQPPKRKI VTMNGQPRVT YRAVPASSVN
     VEQAQYYKVP QQKVQYVTMD RPIKYEVLQL NDYIKMEEES TIRLPNSWST AGPRLHPQVN
     ASSRTVRPLT VATPVHYNGP SAKKIKTQMF
 
 
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