CREM_CANLF
ID CREM_CANLF Reviewed; 360 AA.
AC P79145;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=cAMP-responsive element modulator;
GN Name=CREM;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-177 (ISOFORM TAU).
RC STRAIN=Beagle; TISSUE=Thymus;
RA Staten N.R.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-360 (ISOFORM TAU), AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Thyroid;
RX PubMed=9266832; DOI=10.1006/bbrc.1997.7078;
RA Uyttersprot N., Miot F.;
RT "Dog CREM transcription factors: cloning, tissue distribution, and
RT identification of new isoforms.";
RL Biochem. Biophys. Res. Commun. 237:74-78(1997).
CC -!- FUNCTION: Transcriptional regulator that binds the cAMP response
CC element (CRE), a sequence present in many viral and cellular promoters.
CC Isoforms are either transcriptional activators or repressors. Isoform
CC Tau is a transcriptional activator. Plays a role in spermatogenesis and
CC is involved in spermatid maturation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a dimer. Interacts with FHL5. Interacts with
CC CDC34. May interact with TSSK4. {ECO:0000250|UniProtKB:P27699,
CC ECO:0000250|UniProtKB:Q03060}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=Tau;
CC IsoId=P79145-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=P79145-2; Sequence=Not described;
CC Name=Beta;
CC IsoId=P79145-3; Sequence=Not described;
CC Name=Gamma;
CC IsoId=P79145-4; Sequence=Not described;
CC -!- PTM: Stimulated by phosphorylation. Phosphorylated on Ser-118 by TSSK4
CC in vitro. {ECO:0000250|UniProtKB:P27699, ECO:0000250|UniProtKB:Q01147}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; DN354960; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X99115; CAA67563.1; -; mRNA.
DR PIR; JC5601; JC5601.
DR PIR; JC5602; JC5602.
DR RefSeq; NP_001003221.1; NM_001003221.1.
DR RefSeq; XP_005616964.1; XM_005616907.2. [P79145-1]
DR RefSeq; XP_013976471.1; XM_014120996.1.
DR AlphaFoldDB; P79145; -.
DR SMR; P79145; -.
DR STRING; 9612.ENSCAFP00000005495; -.
DR PaxDb; P79145; -.
DR Ensembl; ENSCAFT00030006201; ENSCAFP00030005462; ENSCAFG00030002923. [P79145-1]
DR Ensembl; ENSCAFT00040001416; ENSCAFP00040001208; ENSCAFG00040000475. [P79145-1]
DR Ensembl; ENSCAFT00845003241; ENSCAFP00845002571; ENSCAFG00845001664. [P79145-1]
DR GeneID; 403887; -.
DR KEGG; cfa:403887; -.
DR CTD; 1390; -.
DR VEuPathDB; HostDB:ENSCAFG00845001664; -.
DR eggNOG; KOG3584; Eukaryota.
DR GeneTree; ENSGT00940000156952; -.
DR HOGENOM; CLU_042675_0_1_1; -.
DR InParanoid; P79145; -.
DR OMA; MSKCSRK; -.
DR OrthoDB; 957343at2759; -.
DR TreeFam; TF106464; -.
DR Proteomes; UP000002254; Chromosome 2.
DR Bgee; ENSCAFG00000003685; Expressed in granulocyte and 48 other tissues.
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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
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; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR003102; Coactivator_CBP_pKID.
DR InterPro; IPR001630; Leuzip_CREB.
DR PANTHER; PTHR45879; PTHR45879; 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; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..360
FT /note="cAMP-responsive element modulator"
FT /id="PRO_0000076606"
FT DOMAIN 104..163
FT /note="KID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00312"
FT DOMAIN 302..360
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 20..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..328
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 330..351
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27699"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03060"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03060,
FT ECO:0000255|PROSITE-ProRule:PRU00312"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03060,
FT ECO:0000255|PROSITE-ProRule:PRU00312"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03060,
FT ECO:0000255|PROSITE-ProRule:PRU00312"
FT CONFLICT 128
FT /note="R -> K (in Ref. 1; DN354960)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 38882 MW; A8AB21AF472EBDA1 CRC64;
MSKCSRKKYI KTNLRQMTMD TMESQQDGSV TDSVAENESA HMQNQTGQNS IPTLTQVSVA
GSGTGRGSPA VTLVQLPSGQ TVHVQGIIQT PQPSVIQSPQ IQTVQVATIA ETDESAESEG
VIDSHKRREI LSRRPSYRKI LNELSSDVPG VPKIEEEKSE EEGTPPNIAT MAVPTSIYQT
STGQYIAIAQ GGTIQISNPG SDGVQGLQAL TMTNSGAPPP GATIVQYAAQ SADGTQQFFV
PGSQVVVQDE ETELAPSHMA AATGDMPTYQ IRAPTTALPQ GVVMAASPGS LHSPQQLAEE
ATRKRELRLM KNREAARECR RKKKEYVKCL ENRVAVLENQ NKTLIEELKA LKDLYCHKAE
