ID A0A1S3FQV4_DIPOR Unreviewed; 451 AA.
AC A0A1S3FQV4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 3 {ECO:0000313|RefSeq:XP_012878227.1};
GN Name=Creb3l3 {ECO:0000313|RefSeq:XP_012878227.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012878227.1};
RN [1] {ECO:0000313|RefSeq:XP_012878227.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012878227.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004648}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
CC {ECO:0000256|ARBA:ARBA00009050}.
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DR RefSeq; XP_012878227.1; XM_013022773.1.
DR AlphaFoldDB; A0A1S3FQV4; -.
DR STRING; 10020.ENSDORP00000003118; -.
DR GeneID; 105990397; -.
DR KEGG; dord:105990397; -.
DR CTD; 84699; -.
DR InParanoid; A0A1S3FQV4; -.
DR OrthoDB; 5362396at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR CDD; cd14689; bZIP_CREB3; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR45996; AGAP001464-PB; 1.
DR PANTHER; PTHR45996:SF1; CYCLIC AMP-RESPONSIVE ELEMENT-BINDING PROTEIN 3-LIKE PROTEIN 3; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Unfolded protein response {ECO:0000256|ARBA:ARBA00023230}.
FT DOMAIN 230..293
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 57..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 255..296
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 63..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 47622 MW; B8D798D033C8D34C CRC64;
MASPTCAMGP MDSIELLDLL FDRQDGILRH VELGEDWGHI TEDQVLPGAD SDGFLNCYLG
PGDSAPSSPT WSPAASDSGI SEDLPSDPQD TPPHRGPAPT AAGGPPSEPG KELCPSLVPS
PPCPPARQPG TPALETSVAI DLELWSSAGT YSEEQAGSPS RFSLSVKQLL LSSSGGGDPQ
QHHLAAAHLL RPGTGHCQEL VLTEDEKKLL AKEGITLPTQ LPLTKYEERV LKKVRRKIRN
KQSAQESRRK KKEYIDGLET RMSACTAQNQ ELHRKVLHLE KQNLSLLEQL KKLQALVVQS
TSKSAQTGTC IAVLLLSFAL IVLPSVSPFA SGKAENPGDF TPVRVFSRTL HNDAASRVAP
EAPPGPAEAP GPRADTGAPW KASLGSGLGP AWGGFLDVPG QGTPVEELDH ATALVLSNST
EGLGRASLLD WASPDPRLSS GLAGLEAVGE L
//
