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Database: UniProt
Entry: G3UDR3_LOXAF
LinkDB: G3UDR3_LOXAF
Original site: G3UDR3_LOXAF 
ID   G3UDR3_LOXAF            Unreviewed;       508 AA.
AC   G3UDR3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Cyclic AMP-responsive element-binding protein 5 {ECO:0000256|PIRNR:PIRNR003153};
GN   Name=CREB5 {ECO:0000313|Ensembl:ENSLAFP00000025971.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000025971.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000025971.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000025971.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000025971.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000025971.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Binds to the cAMP response element and activates
CC       transcription. {ECO:0000256|PIRNR:PIRNR003153}.
CC   -!- SUBUNIT: Binds DNA as a homodimer or as a heterodimer with JUN or
CC       ATF2/CREBP1. {ECO:0000256|PIRNR:PIRNR003153}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR003153}.
CC   -!- SIMILARITY: Belongs to the bZIP family.
CC       {ECO:0000256|PIRNR:PIRNR003153}.
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DR   AlphaFoldDB; G3UDR3; -.
DR   STRING; 9785.ENSLAFP00000025971; -.
DR   Ensembl; ENSLAFT00000036186.1; ENSLAFP00000025971.1; ENSLAFG00000029453.1.
DR   eggNOG; KOG1414; Eukaryota.
DR   GeneTree; ENSGT00940000156420; -.
DR   HOGENOM; CLU_021564_0_0_1; -.
DR   InParanoid; G3UDR3; -.
DR   OMA; MEMMPSR; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR   CDD; cd14687; bZIP_ATF2; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR016378; TF_CRE-BP1-typ.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR19304:SF8; CYCLIC AMP-RESPONSIVE ELEMENT-BINDING PROTEIN 5; 1.
DR   PANTHER; PTHR19304; CYCLIC-AMP RESPONSE ELEMENT BINDING PROTEIN; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PIRSF; PIRSF003153; ATF2_CRE-BP1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|PIRNR:PIRNR003153};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|PIRNR:PIRNR003153};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR003153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   Transcription {ECO:0000256|PIRNR:PIRNR003153};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR003153};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          16..40
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          375..438
FT                   /note="BZIP"
FT                   /evidence="ECO:0000259|PROSITE:PS50217"
FT   REGION          265..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          400..434
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        292..326
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..389
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  56957 MW;  26509F7845C3200E CRC64;
     QIYEESKMNL EQERPFVCSA PGCSQRFPTE DHLMIHRHKH EMTLKFPSIK TDNMLSDQTP
     TPTRFLKNCE EVGLFNELDC SLEHEFRKAQ EEESSKRNIS MHNTVGGAMT GPGAHQLGGS
     RMPNHDTSVV IQQAMPSPQS SSVITQAPST NRQIGPVPGS LSSLLHLHNR QRQPMPASMP
     GTLPNPTMPG SSAVLMPMER QMSVNSNIMG MQGPNLNNPC ASPQVQPMHS EAKMRLKAAL
     THHPAAMSNG NMNTMGHMME MMGSRQDQTP HHHMHTHPHQ HQTLPPHHPY PHQHQHPAHH
     PHPQPHHQQN HPHHHSHSHL HAHPAHHQTS PHPPLHTGNQ AQVSPATQQM QPTQTIQPPQ
     PTGGRRRRVV DEDPDERRRK FLERNRAAAT RCRQKRKVWV MSLEKKAEEL TQTNMQLQNE
     VSMLKNEVAQ LKQLLLTHKD CPITAMQKES QGYLSPESSP PASPVPACSQ QQVIQHNTIT
     TSSSVSEVVG SSTLSQLTTH RTDLNPIL
//
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