(data stored in ACNUC3554 zone)

HOGENOM: RAT7_PE1524

ID   RAT7_PE1524                          STANDARD;      PRT;   1133 AA.
AC   RAT7_PE1524; Q3T1I5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Sterol regulatory element-binding protein 2;
DE   Short=SREBP-2;AltName: Full=Sterol regulatory element-binding
DE   transcription factor 2;Contains: RecName: Full=Processed sterol
DE   regulatory element-binding protein 2; (RAT7.PE1524).
GN   Name=Srebf2;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT7.PE1524.
CC       Rattus norvegicus chromosome 7 RGSC3.4  sequence 1..143002779
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:SRBP2_RAT
CC   -!- FUNCTION: Transcriptional activator required for lipid
CC       homeostasis. Regulates transcription of the LDL receptor gene as
CC       well as the cholesterol and to a lesser degree the fatty acid
CC       synthesis pathway (By similarity). Binds the sterol regulatory
CC       element 1 (SRE-1) (5'-ATCACCCCAC-3') found in the flanking region
CC       of the LDRL and HMG-CoA synthase genes (By similarity).
CC   -!- SUBUNIT: Forms a tight complex with SCAP in the ER membrane.
CC       Efficient DNA binding of the soluble transcription factor fragment
CC       requires dimerization with another bHLH protein. Interacts with
CC       LMNA. Component of SCAP/SREBP complex composed of SREBF2, SCAP and
CC       RNF139; the complex hampers the interaction between SCAP and
CC       SEC24B, thereby reducing SREBF2 proteolytic processing. Interacts
CC       (via C-terminus domain) with RNF139 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity). Golgi apparatus membrane; Multi-
CC       pass membrane protein (By similarity). Cytoplasmic vesicle, COPII-
CC       coated vesicle membrane; Multi-pass membrane protein (By
CC       similarity). Note=Moves from the endoplasmic reticulum to the
CC       Golgi in the absence of sterols (By similarity).
CC   -!- SUBCELLULAR LOCATION: Processed sterol regulatory element-binding
CC       protein 2: Nucleus (By similarity).
CC   -!- PTM: At low cholesterol the SCAP/SREBP complex is recruited into
CC       COPII vesicles for export from the ER. In the Golgi complex SREBPs
CC       are cleaved sequentially by site-1 and site-2 protease. The first
CC       cleavage by site-1 protease occurs within the luminal loop, the
CC       second cleavage by site-2 protease occurs within the first
CC       transmembrane domain and releases the transcription factor from
CC       the Golgi membrane. Apoptosis triggers cleavage by the cysteine
CC       proteases caspase-3 and caspase-7 (By similarity).
CC   -!- SIMILARITY: Belongs to the SREBP family.
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
CC   -!- GENE_FAMILY: HOG000007091 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000007400;ENSRNOT00000056041;ENSRNOP00000052893.
DR   EMBL; BC101902; - ;
DR   UniProtKB/Swiss-Prot; Q3T1I5; -.
DR   EMBL; BC101902; AAI01903.1; -; mRNA.
DR   IPI; IPI00366445; -.
DR   RefSeq; NP_001028866.1; NM_001033694.1.
DR   UniGene; Rn.41063; -.
DR   ProteinModelPortal; Q3T1I5; -.
DR   SMR; Q3T1I5; 335-395.
DR   STRING; Q3T1I5; -.
DR   PRIDE; Q3T1I5; -.
DR   GeneID; 300095; -.
DR   KEGG; rno:300095; -.
DR   UCSC; NM_001033694; rat.
DR   CTD; 6721; -.
DR   RGD; 1307751; Srebf2.
DR   eggNOG; roNOG08765; -.
DR   GeneTree; ENSGT00390000017651; -.
DR   InParanoid; Q3T1I5; -.
DR   OrthoDB; EOG40S0F2; -.
DR   NextBio; 646330; -.
DR   ArrayExpress; Q3T1I5; -.
DR   Genevestigator; Q3T1I5; -.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0007568; P:aging; IEP:RGD.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008610; P:lipid biosynthetic process; TAS:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0009725; P:response to hormone stimulus; IMP:RGD.
DR   GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR   GO; GO:0033993; P:response to lipid; IEP:RGD.
DR   GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR   InterPro; IPR011598; HLH_DNA-bd.
DR   InterPro; IPR001092; HLH_DNA-bd_dom.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   Gene3D; G3DSA:4.10.280.10; HLH_DNA_bd; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH_basic; 1.
DR   PROSITE; PS50888; HLH; 1.
DR   HOGENOMDNA; RAT7.PE1524; -.
KW   ENSRNOG00000007400820036002503210000011;
KW   Srebf2; SRBP2_RAT; BC101902;
KW   Activator; Cholesterol metabolism; Complete proteome;
KW   Cytoplasmic vesicle; DNA-binding; Endoplasmic reticulum;
KW   Golgi apparatus; Lipid metabolism; Membrane; Nucleus; Phosphoprotein;
KW   Reference proteome; Steroid metabolism; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   1133 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDENSELGGL ETMETLTELG DELTLGDIDE MLQFVSNQVG EFSDLFSEQL CSSFPGGGGG
     SGSGGTSNNS SGRGTSGGAA DPAVQRSFSQ VPLSTFSPSS TSPQAPALQV KVSPTPPRAT
     PVLQPRPQPQ PQPPAQLQQQ TVMITPTFST APQTRIIQQP LIYQNAATSF QVLQPQVQSL
     VTSSQVQPVT IQQQVQTVQA QRVLTQTANG TLQTLAPATV QTVATPQVQQ VPVLVQPQII
     KTDSLVLTTL KTDGSPVMAA VQNPALTALT APIQTAALQV PTLVGSNGAI LTTMPVMMGQ
     EKVPIKQVPG GVKQLEPPKE GERRTTHNII EKRYRSSIND KIIELKDLVM GTDAKMHKSG
     VLRKAIDYIK YLQQVNHKLR QENMVLKLAN QKNKLLKGID LGSLVDSDVD LKIDDFNQNV
     LLMSPPASDS GSQAGFSPYS IDSEPGSPLL DDAKVKDEPD SPPVALGMVD RSRILLCVLT
     FLGLSFNPLT SLLQWGGAHN PDQHPYSGSG RNVLSLESGS GGWFDWMMPT LLLWLLNGVI
     VLSVFVKLLV HGEPVIRPHS RSSVTFWRHR KQADLDLAKG DFAAAAANLQ TCLSVLGRAL
     PTSRLDLACS LSWNVIRYSL QKLRLVRWLL KKVFQRWRAT PATAAGFEDE AKSSARDAAL
     AYHRLHQLHI TGKLPAGSAC SDVHMALCAV NLAECAEEKI PPSTLVEIHL TAAMGLKTRC
     GGKLGFLASY FLNRAQSLCG PEHSAVPDSL RWLCHPLGQK FFMERSWSIK SAAKDSLYCA
     QRNPADPIAQ VHQAFCKHLL ERAVEALVKP QAKKKAGDRE EESCEFSSAL EFLKLLHSFV
     DSVGFVASPF SSSSVLRSAL GPDVVCRWWT SAITVAISWL QGDDAAVRSH FTEVERVPKA
     LEVTESPLVK AVFYACRAMH ASLSGKADGQ QNSFCHCERA SGHLWSSLNV SGTTSDPSLN
     HVVQLFTCDL LLSLRTTLWQ KQASASQLLG ETYHASGTEL AGFQRDLGSL RRLAHSFRPA
     YRKVFLHEAT VRLMAGASPT RTHQLLEHSL RRRTTQNTKH GEVDTWPGQR ERATAILLAC
     RHLPLSFLSS PGQRAVLLAE AARTLEKVGD RRSCSDCQQM IVKLGGGTAI AAS
//

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