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ATF1_BOVIN
ID   ATF1_BOVIN              Reviewed;         270 AA.
AC   Q08DA8;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Cyclic AMP-dependent transcription factor ATF-1;
DE            Short=cAMP-dependent transcription factor ATF-1;
DE   AltName: Full=Activating transcription factor 1;
GN   Name=ATF1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Brain cortex;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein binds the cAMP response element (CRE)
CC       (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral
CC       and cellular promoters. Mediates PKA-induced stimulation of CRE-
CC       reporter genes. Represses the expression of FTH1 and other antioxidant
CC       detoxification genes. Triggers cell proliferation and transformation
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as a dimer. Interacts with HIPK2 and CDK3. Interacts
CC       with MOTS-c, a peptide produced by the mitochondrially encoded 12S rRNA
CC       MT-RNR1; the interaction occurs in the nucleus following metabolic
CC       stress. {ECO:0000250|UniProtKB:P18846}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00312,
CC       ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- PTM: Phosphorylated at Ser-197 by HIPK2 in response to genotoxic
CC       stress. This phosphorylation promotes transcription repression of FTH1
CC       and other antioxidant detoxification genes. The CDK3-mediated
CC       phosphorylation at Ser-63 promotes its transactivation and
CC       transcriptional activities. Phosphorylated at Ser-63 by RPS6KA4 and
CC       RPS6KA5 in response to mitogenic or stress stimuli (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR   EMBL; BC123855; AAI23856.1; -; mRNA.
DR   RefSeq; NP_001068757.1; NM_001075289.1.
DR   RefSeq; XP_005206335.1; XM_005206278.3.
DR   AlphaFoldDB; Q08DA8; -.
DR   STRING; 9913.ENSBTAP00000024135; -.
DR   iPTMnet; Q08DA8; -.
DR   PaxDb; Q08DA8; -.
DR   PRIDE; Q08DA8; -.
DR   Ensembl; ENSBTAT00000024135; ENSBTAP00000024135; ENSBTAG00000018131.
DR   GeneID; 506967; -.
DR   KEGG; bta:506967; -.
DR   CTD; 466; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018131; -.
DR   VGNC; VGNC:26239; ATF1.
DR   eggNOG; KOG3584; Eukaryota.
DR   GeneTree; ENSGT00940000158200; -.
DR   HOGENOM; CLU_042675_1_0_1; -.
DR   InParanoid; Q08DA8; -.
DR   OrthoDB; 957343at2759; -.
DR   TreeFam; TF106464; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000018131; Expressed in milk and 105 other tissues.
DR   ExpressionAtlas; Q08DA8; baseline and differential.
DR   GO; GO:1990589; C:ATF4-CREB1 transcription factor complex; IBA:GO_Central.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR029825; ATF1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR003102; Coactivator_CBP_pKID.
DR   InterPro; IPR001630; Leuzip_CREB.
DR   PANTHER; PTHR45879; PTHR45879; 1.
DR   PANTHER; PTHR45879:SF2; PTHR45879:SF2; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF02173; pKID; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
DR   PROSITE; PS50953; KID; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..270
FT                   /note="Cyclic AMP-dependent transcription factor ATF-1"
FT                   /id="PRO_0000285214"
FT   DOMAIN          31..90
FT                   /note="KID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00312"
FT   DOMAIN          212..270
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..238
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          240..261
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        8..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         63
FT                   /note="Phosphoserine; by CaMK1, CDK3, RPS6KA4 and RPS6KA5"
FT                   /evidence="ECO:0000250|UniProtKB:P18846,
FT                   ECO:0000255|PROSITE-ProRule:PRU00312"
FT   MOD_RES         197
FT                   /note="Phosphoserine; by HIPK2"
FT                   /evidence="ECO:0000250|UniProtKB:P18846,
FT                   ECO:0000255|PROSITE-ProRule:PRU00312"
FT   CROSSLNK        207
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P18846"
FT   CROSSLNK        214
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P18846"
SQ   SEQUENCE   270 AA;  29261 MW;  4DC5B06A6CBC7103 CRC64;
     MEDSHKSNTS ETAPQSGSTV QAAHISHIAQ QVSSLSESEE SQDSSDSIGS SQKTHGILAR
     RPSYRKILKD LSSEDIRGRK GDGENPGVSA VTSMSVPTPI YQTSTGQYIA IAPNGALQLA
     SPGTDGVQGL QTLTMTNSGS TQQGTTILQY AQTSDGQQIL VPSNQVVVQT ASGDMQTYQI
     RTTPSATSLP QTVVMTSPVT LTSQTSKTDD PQLKREIRLM KNREAARECR RKKKEYVKCL
     ENRVAVLENQ NKTLIEELKT LKDLYSNKSV
 
 
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