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ATF7_CAEEL
ID   ATF7_CAEEL              Reviewed;         509 AA.
AC   Q86MD3; B3GWA6; Q17801; Q9U3R1;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Transcription factor atf-7 {ECO:0000305};
DE   AltName: Full=cAMP-dependent transcription factor family member 7 {ECO:0000312|WormBase:C07G2.2c};
GN   Name=atf-7 {ECO:0000312|WormBase:C07G2.2c};
GN   ORFNames=C07G2.2 {ECO:0000312|WormBase:C07G2.2c};
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, INTERACTION WITH PMK-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-107.
RX   PubMed=20369020; DOI=10.1371/journal.pgen.1000892;
RA   Shivers R.P., Pagano D.J., Kooistra T., Richardson C.E., Reddy K.C.,
RA   Whitney J.K., Kamanzi O., Matsumoto K., Hisamoto N., Kim D.H.;
RT   "Phosphorylation of the conserved transcription factor ATF-7 by PMK-1 p38
RT   MAPK regulates innate immunity in Caenorhabditis elegans.";
RL   PLoS Genet. 6:e1000892-e1000892(2010).
RN   [3] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=23505381; DOI=10.1371/journal.pgen.1003324;
RA   Xie Y., Moussaif M., Choi S., Xu L., Sze J.Y.;
RT   "RFX transcription factor DAF-19 regulates 5-HT and innate immune responses
RT   to pathogenic bacteria in Caenorhabditis elegans.";
RL   PLoS Genet. 9:e1003324-e1003324(2013).
RN   [4] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=26016853; DOI=10.1371/journal.pgen.1005265;
RA   Block D.H., Twumasi-Boateng K., Kang H.S., Carlisle J.A., Hanganu A.,
RA   Lai T.Y., Shapira M.;
RT   "The developmental intestinal regulator ELT-2 controls p38-dependent immune
RT   responses in adult C. elegans.";
RL   PLoS Genet. 11:E1005265-E1005265(2015).
RN   [5] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28632756; DOI=10.1371/journal.pone.0177432;
RA   Hall J.A., McElwee M.K., Freedman J.H.;
RT   "Identification of ATF-7 and the insulin signaling pathway in the
RT   regulation of metallothionein in C. elegans suggests roles in aging and
RT   reactive oxygen species.";
RL   PLoS ONE 12:e0177432-e0177432(2017).
RN   [6] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=30789901; DOI=10.1371/journal.pgen.1007830;
RA   Fletcher M., Tillman E.J., Butty V.L., Levine S.S., Kim D.H.;
RT   "Global transcriptional regulation of innate immunity by ATF-7 in C.
RT   elegans.";
RL   PLoS Genet. 15:e1007830-e1007830(2019).
CC   -!- FUNCTION: Transcription factor which regulates the transcription of
CC       various genes, including those involved in innate immunity and
CC       oxidative stress responses (PubMed:20369020, PubMed:28632756,
CC       PubMed:30789901). Binds to promoter regions of genes, probably at 5'-
CC       [GACGTCA]-3' consensus sequences (PubMed:30789901). Together with
CC       transcription factor daf-19, involved in regulation of the serotonergic
CC       response of ADF neurons to pathogenic food (PubMed:23505381). Modulates
CC       response to infection by the Gram-negative bacterium P.aeruginosa,
CC       acting downstream of the p38 signal transduction pathway effector
CC       serine/threonine kinase pmk-1 (PubMed:20369020, PubMed:30789901). May
CC       act with transcription factor elt-2 to control p38 gene induction in
CC       response to bacterial infection (PubMed:26016853). May be
CC       phosphorylated by pmk-1 (PubMed:20369020). Regulates transcription of
CC       the metallothionein gene, mtl-1, perhaps acting downstream of pmk-1
CC       (PubMed:28632756). {ECO:0000269|PubMed:20369020,
CC       ECO:0000269|PubMed:23505381, ECO:0000269|PubMed:26016853,
CC       ECO:0000269|PubMed:28632756, ECO:0000269|PubMed:30789901}.
CC   -!- SUBUNIT: Interacts with serine/threonine kinase pmk-1; perhaps in a
CC       manner dependent on dual specificity protein kinase sek-1.
CC       {ECO:0000269|PubMed:20369020}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20369020}. Chromosome
CC       {ECO:0000269|PubMed:30789901}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=c {ECO:0000312|WormBase:C07G2.2c};
CC         IsoId=Q86MD3-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:C07G2.2b};
CC         IsoId=Q86MD3-2; Sequence=VSP_061039;
CC       Name=a {ECO:0000312|WormBase:C07G2.2a};
CC         IsoId=Q86MD3-3; Sequence=VSP_061039, VSP_061041;
CC       Name=d {ECO:0000312|WormBase:C07G2.2d};
CC         IsoId=Q86MD3-4; Sequence=VSP_061038, VSP_061040, VSP_061042;
CC   -!- TISSUE SPECIFICITY: Expressed in intestinal cells.
CC       {ECO:0000269|PubMed:20369020}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown increases susceptibility
CC       to infection by the Gram-negative bacterium P.aeruginosa
CC       (PubMed:20369020). Up-regulates expression of metallothionein mtl-1
CC       (PubMed:28632756). {ECO:0000269|PubMed:20369020,
CC       ECO:0000269|PubMed:28632756}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR   EMBL; BX284603; CAA83680.1; -; Genomic_DNA.
DR   EMBL; BX284603; CAB63430.2; -; Genomic_DNA.
DR   EMBL; BX284603; CAD88215.1; -; Genomic_DNA.
DR   EMBL; BX284603; CAQ58094.1; -; Genomic_DNA.
DR   PIR; T19062; T19062.
DR   RefSeq; NP_001021161.1; NM_001025990.3.
DR   RefSeq; NP_001129834.1; NM_001136362.2.
DR   RefSeq; NP_497913.1; NM_065512.3. [Q86MD3-2]
DR   RefSeq; NP_497914.2; NM_065513.4. [Q86MD3-3]
DR   AlphaFoldDB; Q86MD3; -.
DR   SMR; Q86MD3; -.
DR   IntAct; Q86MD3; 5.
DR   STRING; 6239.C07G2.2c.1; -.
DR   PaxDb; Q86MD3; -.
DR   EnsemblMetazoa; C07G2.2a.1; C07G2.2a.1; WBGene00000223. [Q86MD3-3]
DR   EnsemblMetazoa; C07G2.2b.1; C07G2.2b.1; WBGene00000223. [Q86MD3-2]
DR   EnsemblMetazoa; C07G2.2b.2; C07G2.2b.2; WBGene00000223. [Q86MD3-2]
DR   EnsemblMetazoa; C07G2.2c.1; C07G2.2c.1; WBGene00000223. [Q86MD3-1]
DR   EnsemblMetazoa; C07G2.2d.1; C07G2.2d.1; WBGene00000223. [Q86MD3-4]
DR   EnsemblMetazoa; C07G2.2d.2; C07G2.2d.2; WBGene00000223. [Q86MD3-4]
DR   EnsemblMetazoa; C07G2.2d.3; C07G2.2d.3; WBGene00000223. [Q86MD3-4]
DR   EnsemblMetazoa; C07G2.2d.4; C07G2.2d.4; WBGene00000223. [Q86MD3-4]
DR   GeneID; 175587; -.
DR   KEGG; cel:CELE_C07G2.2; -.
DR   UCSC; C07G2.2a.2; c. elegans.
DR   CTD; 175587; -.
DR   WormBase; C07G2.2a; CE33597; WBGene00000223; atf-7.
DR   WormBase; C07G2.2b; CE19688; WBGene00000223; atf-7.
DR   WormBase; C07G2.2c; CE33598; WBGene00000223; atf-7.
DR   WormBase; C07G2.2d; CE42659; WBGene00000223; atf-7.
DR   eggNOG; KOG1414; Eukaryota.
DR   GeneTree; ENSGT00940000176028; -.
DR   HOGENOM; CLU_598848_0_0_1; -.
DR   InParanoid; Q86MD3; -.
DR   OMA; CLAVNPF; -.
DR   OrthoDB; 935883at2759; -.
DR   Reactome; R-CEL-3214847; HATs acetylate histones.
DR   Reactome; R-CEL-450341; Activation of the AP-1 family of transcription factors.
DR   SignaLink; Q86MD3; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00000223; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   ExpressionAtlas; Q86MD3; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0035497; F:cAMP response element binding; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:WormBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:WormBase.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR   GO; GO:0071248; P:cellular response to metal ion; IMP:UniProtKB.
DR   GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR   GO; GO:0045824; P:negative regulation of innate immune response; IMP:WormBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR   GO; GO:0045089; P:positive regulation of innate immune response; IMP:WormBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0042427; P:serotonin biosynthetic process; IMP:UniProtKB.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   Pfam; PF07716; bZIP_2; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromosome; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..509
FT                   /note="Transcription factor atf-7"
FT                   /id="PRO_0000452693"
FT   DOMAIN          391..464
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          283..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..413
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          419..450
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        283..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..68
FT                   /note="Missing (in isoform d)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_061038"
FT   VAR_SEQ         1..63
FT                   /note="MATTMMTSSASPPESGELDVASAVASAAAALISPMVMPTSMTNGKDMTKTSQ
FT                   ILNEYFNMMVG -> MSVVTTTSMQSDSK (in isoform b and isoform a)"
FT                   /id="VSP_061039"
FT   VAR_SEQ         435..441
FT                   /note="AIQTQNQ -> VRNEILY (in isoform d)"
FT                   /id="VSP_061040"
FT   VAR_SEQ         435..437
FT                   /note="Missing (in isoform a)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_061041"
FT   VAR_SEQ         442..509
FT                   /note="Missing (in isoform d)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_061042"
FT   MUTAGEN         107
FT                   /note="P->S: In qd22; increases level of activated MAP
FT                   kinase pmk-1 compared to wild-type. Simultaneous RNA-
FT                   imediated knockdown of atf-7 confers increased resistance
FT                   to Gram-negative bacterium P.aeruginosa."
FT                   /evidence="ECO:0000269|PubMed:20369020"
SQ   SEQUENCE   509 AA;  54727 MW;  7CD869FAB173950D CRC64;
     MATTMMTSSA SPPESGELDV ASAVASAAAA LISPMVMPTS MTNGKDMTKT SQILNEYFNM
     MVGKRVQLMG DTTSPFSLDT PNPKLMFTPL DLPTTAELMQ RCLAVNPFEA KFREANQKIS
     SGSMQPNTSG ANQSLEALEA NGGSQFSGSN AGTMSDLLLK IPQASLQHSP GIFSNMLLNA
     GDSEGTTREN LKTADISKLL SVAGDFSAQA PRTADVLNAV LDMHSDRLHT INYLNNKPDF
     SALLRSPSSS APNSASVLTN AMAIPSTSGA PFPGTTLLVP PKTVSSYHSP LGASSQPPST
     QKSPADGSWD HINGEKQIKK EIPYFNDDAM MLMERSNMSS SGSDQDQSAD MSNAGSTAST
     STGNPVGRPQ NGTPGRGRGR GRSTTADMQP DERRNTILER NKAAAVRYRK RKKEEHDDMM
     GRVQAMEAEK NQLLAIQTQN QVLRRELERV TALLTERESR CVCLKGVPMS DEQHADHHHR
     NTNGMYSGSD MLNGLGQING MQLKLPKLQ
 
 
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