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Protein

Sterol regulatory element-binding protein 2

Gene

Srebf2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Transcriptional activator required for lipid homeostasis. Regulates transcription of the LDL receptor gene as well as the cholesterol and to a lesser degree the fatty acid synthesis pathway (By similarity). Binds the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3') found in the flanking region of the LDRL and HMG-CoA synthase genes (By similarity).By similarity

GO - Molecular functioni

  • chromatin binding Source: RGD
  • sequence-specific DNA binding Source: MGI

GO - Biological processi

  • aging Source: RGD
  • cholesterol metabolic process Source: UniProtKB-KW
  • lipid biosynthetic process Source: RGD
  • positive regulation of transcription, DNA-templated Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • response to drug Source: RGD
  • response to hormone Source: RGD
  • response to lead ion Source: RGD
  • response to lipid Source: RGD
  • spermatogenesis Source: RGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol regulatory element-binding protein 2
Short name:
SREBP-2
Alternative name(s):
Sterol regulatory element-binding transcription factor 2
Cleaved into the following chain:
Gene namesi
Name:Srebf2Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1307751. Srebf2.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  • Golgi apparatus membrane By similarity; Multi-pass membrane protein By similarity
  • Cytoplasmic vesicleCOPII-coated vesicle membrane By similarity; Multi-pass membrane protein By similarity

  • Note: Moves from the endoplasmic reticulum to the Golgi in the absence of sterols.By similarity
Processed sterol regulatory element-binding protein 2 :
  • Nucleus PROSITE-ProRule annotationBy similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 473473CytoplasmicSequence analysisAdd
BLAST
Transmembranei474 – 49421HelicalSequence analysisAdd
BLAST
Topological domaini495 – 52531LumenalSequence analysisAdd
BLAST
Transmembranei526 – 54621HelicalSequence analysisAdd
BLAST
Topological domaini547 – 1133587CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • ER to Golgi transport vesicle membrane Source: UniProtKB-SubCell
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11331133Sterol regulatory element-binding protein 2PRO_0000317061Add
BLAST
Chaini1 – 476476Processed sterol regulatory element-binding protein 2By similarityPRO_0000317062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1090 – 10901PhosphoserineBy similarity

Post-translational modificationi

At low cholesterol the SCAP/SREBP complex is recruited into COPII vesicles for export from the ER. In the Golgi complex SREBPs are cleaved sequentially by site-1 and site-2 protease. The first cleavage by site-1 protease occurs within the luminal loop, the second cleavage by site-2 protease occurs within the first transmembrane domain and releases the transcription factor from the Golgi membrane. Apoptosis triggers cleavage by the cysteine proteases caspase-3 and caspase-7 (By similarity).By similarity
Phosphorylated by AMPK, leading to suppress protein processing and nuclear translocation, and repress target gene expression.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei460 – 4612Cleavage; by caspase-3 and caspase-7By similarity
Sitei476 – 4772Cleavage; by S2PBy similarity
Sitei514 – 5152Cleavage; by S1PBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ3T1I5.
PRIDEiQ3T1I5.

Interactioni

Subunit structurei

Forms a tight complex with SCAP in the ER membrane. Efficient DNA binding of the soluble transcription factor fragment requires dimerization with another bHLH protein. Interacts with LMNA. Component of SCAP/SREBP complex composed of SREBF2, SCAP and RNF139; the complex hampers the interaction between SCAP and SEC24B, thereby reducing SREBF2 proteolytic processing. Interacts (via C-terminal domain) with RNF139 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000052893.

Structurei

3D structure databases

ProteinModelPortaliQ3T1I5.
SMRiQ3T1I5. Positions 335-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini322 – 37251bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5050Transcriptional activation (acidic)Sequence analysisAdd
BLAST
Regioni229 – 483255Interaction with LMNABy similarityAdd
BLAST
Regioni372 – 39322Leucine-zipperAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi98 – 13437Pro-richSequence analysisAdd
BLAST
Compositional biasi124 – 238115Gln-richSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the SREBP family.Sequence analysis
Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2588. Eukaryota.
ENOG410XSVP. LUCA.
HOGENOMiHOG000007091.
HOVERGENiHBG061592.
InParanoidiQ3T1I5.
KOiK09107.
PhylomeDBiQ3T1I5.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR003006. Ig/MHC_CS.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3T1I5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDENSELGGL ETMETLTELG DELTLGDIDE MLQFVSNQVG EFSDLFSEQL
60 70 80 90 100
CSSFPGGGGG SGSGGTSNNS SGRGTSGGAA DPAVQRSFSQ VPLSTFSPSS
110 120 130 140 150
TSPQAPALQV KVSPTPPRAT PVLQPRPQPQ PQPPAQLQQQ TVMITPTFST
160 170 180 190 200
APQTRIIQQP LIYQNAATSF QVLQPQVQSL VTSSQVQPVT IQQQVQTVQA
210 220 230 240 250
QRVLTQTANG TLQTLAPATV QTVATPQVQQ VPVLVQPQII KTDSLVLTTL
260 270 280 290 300
KTDGSPVMAA VQNPALTALT APIQTAALQV PTLVGSNGAI LTTMPVMMGQ
310 320 330 340 350
EKVPIKQVPG GVKQLEPPKE GERRTTHNII EKRYRSSIND KIIELKDLVM
360 370 380 390 400
GTDAKMHKSG VLRKAIDYIK YLQQVNHKLR QENMVLKLAN QKNKLLKGID
410 420 430 440 450
LGSLVDSDVD LKIDDFNQNV LLMSPPASDS GSQAGFSPYS IDSEPGSPLL
460 470 480 490 500
DDAKVKDEPD SPPVALGMVD RSRILLCVLT FLGLSFNPLT SLLQWGGAHN
510 520 530 540 550
PDQHPYSGSG RNVLSLESGS GGWFDWMMPT LLLWLLNGVI VLSVFVKLLV
560 570 580 590 600
HGEPVIRPHS RSSVTFWRHR KQADLDLAKG DFAAAAANLQ TCLSVLGRAL
610 620 630 640 650
PTSRLDLACS LSWNVIRYSL QKLRLVRWLL KKVFQRWRAT PATAAGFEDE
660 670 680 690 700
AKSSARDAAL AYHRLHQLHI TGKLPAGSAC SDVHMALCAV NLAECAEEKI
710 720 730 740 750
PPSTLVEIHL TAAMGLKTRC GGKLGFLASY FLNRAQSLCG PEHSAVPDSL
760 770 780 790 800
RWLCHPLGQK FFMERSWSIK SAAKDSLYCA QRNPADPIAQ VHQAFCKHLL
810 820 830 840 850
ERAVEALVKP QAKKKAGDRE EESCEFSSAL EFLKLLHSFV DSVGFVASPF
860 870 880 890 900
SSSSVLRSAL GPDVVCRWWT SAITVAISWL QGDDAAVRSH FTEVERVPKA
910 920 930 940 950
LEVTESPLVK AVFYACRAMH ASLSGKADGQ QNSFCHCERA SGHLWSSLNV
960 970 980 990 1000
SGTTSDPSLN HVVQLLTCDL LLSLRTTLWQ KQASASQLLG ETYHASGTEL
1010 1020 1030 1040 1050
AGFQRDLGSL RRLAHSFRPA YRKVFLHEAT VRLMAGASPT RTHQLLEHSL
1060 1070 1080 1090 1100
RRRTTQNTKH GEVDTWPGQR ERATAILLAC RHLPLSFLSS PGQRAVLLAE
1110 1120 1130
AARTLEKVGD RRSCSDCQQM IVKLGGGTAI AAS
Length:1,133
Mass (Da):122,976
Last modified:October 11, 2005 - v1
Checksum:i148A5DA3165A0236
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC101902 mRNA. Translation: AAI01903.1.
RefSeqiNP_001028866.1. NM_001033694.1.
UniGeneiRn.41063.

Genome annotation databases

GeneIDi300095.
KEGGirno:300095.
UCSCiRGD:1307751. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC101902 mRNA. Translation: AAI01903.1.
RefSeqiNP_001028866.1. NM_001033694.1.
UniGeneiRn.41063.

3D structure databases

ProteinModelPortaliQ3T1I5.
SMRiQ3T1I5. Positions 335-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000052893.

Proteomic databases

PaxDbiQ3T1I5.
PRIDEiQ3T1I5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi300095.
KEGGirno:300095.
UCSCiRGD:1307751. rat.

Organism-specific databases

CTDi6721.
RGDi1307751. Srebf2.

Phylogenomic databases

eggNOGiKOG2588. Eukaryota.
ENOG410XSVP. LUCA.
HOGENOMiHOG000007091.
HOVERGENiHBG061592.
InParanoidiQ3T1I5.
KOiK09107.
PhylomeDBiQ3T1I5.

Miscellaneous databases

PROiQ3T1I5.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR003006. Ig/MHC_CS.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSRBP2_RAT
AccessioniPrimary (citable) accession number: Q3T1I5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 11, 2005
Last modified: July 6, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.