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Database: UniProt
Entry: A0A2K5TR28_MACFA
LinkDB: A0A2K5TR28_MACFA
Original site: A0A2K5TR28_MACFA 
ID   A0A2K5TR28_MACFA        Unreviewed;       501 AA.
AC   A0A2K5TR28;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Cyclic AMP-responsive element-binding protein 5 {ECO:0000256|PIRNR:PIRNR003153};
GN   Name=CREB5 {ECO:0000313|Ensembl:ENSMFAP00000002526.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000002526.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000002526.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000002526.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   RefSeq; XP_005549963.1; XM_005549906.2.
DR   AlphaFoldDB; A0A2K5TR28; -.
DR   Ensembl; ENSMFAT00000027672.2; ENSMFAP00000002526.2; ENSMFAG00000037539.2.
DR   GeneID; 102123367; -.
DR   KEGG; mcf:102123367; -.
DR   CTD; 9586; -.
DR   VEuPathDB; HostDB:ENSMFAG00000037539; -.
DR   GeneTree; ENSGT00940000156420; -.
DR   OrthoDB; 1361169at2759; -.
DR   Proteomes; UP000233100; Chromosome 3.
DR   Bgee; ENSMFAG00000037539; Expressed in heart and 8 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
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:UP000233100};
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          9..33
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          368..431
FT                   /note="BZIP"
FT                   /evidence="ECO:0000259|PROSITE:PS50217"
FT   REGION          258..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          393..427
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        285..319
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  56010 MW;  994DBA946AD8A5A7 CRC64;
     MNLEQERPFV CSAPGCSQRF PTEDHLMIHR HKHEMTLKFP SIKTDNMLSD QTPTPTRFLK
     NCEEVGLFSE LDCSLEHEFR KAQEEESSKR NISMHNAVGG AMTGPGTHQL SSARLPNHDT
     SVVIQQAMPS PQSSSVITQA PSTNRQIGPV PGSLSSLLHL HNRQRQPMPA SMPGTLPNPT
     MPGSSAVLMP MERQMSVNSS IMGMQGPNLS NPCASPQVQP MHSEAKMRLK AALTHHPAAM
     SNGNMNTMGH MMEMMGSRQD QTPHHHMHSH PHQHQTLPPH HPYPHQHQHP AHHPHPQPHH
     QQNHPHHHSH SHLHAHPAHH QTSPHPPLHT GNQAQVSPAT QQMQPTQTIQ PPQPTGGRRR
     RVVDEDPDER RRKFLERNRA AATRCRQKRK VWVMSLEKKA EELTQTNMQL QNEVSMLKNE
     VAQLKQLLLT HKDCPITAMQ KESQGYLSPE SSPPASPVPA CSQQQVIQHN TITTSSSVSE
     VVGSSTLSQL TTHRTDLNPI L
//
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