SRBP1_RAT
ID SRBP1_RAT Reviewed; 1134 AA.
AC P56720; Q99PI6; Q99PI7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Sterol regulatory element-binding protein 1 {ECO:0000303|PubMed:11309661};
DE Short=SREBP-1 {ECO:0000303|PubMed:11309661};
DE AltName: Full=Adipocyte determination- and differentiation-dependent factor 1 {ECO:0000303|PubMed:11309661};
DE Short=ADD1 {ECO:0000303|PubMed:11309661};
DE AltName: Full=Sterol regulatory element-binding transcription factor 1 {ECO:0000303|PubMed:11309661};
DE Contains:
DE RecName: Full=Processed sterol regulatory element-binding protein 1 {ECO:0000305};
DE AltName: Full=Transcription factor SREBF1 {ECO:0000305};
GN Name=Srebf1 {ECO:0000312|RGD:69423};
GN Synonyms=Srebp1 {ECO:0000303|PubMed:11309661};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1046 (ISOFORM SREBP-1C), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Adipocyte;
RX PubMed=8336713; DOI=10.1128/mcb.13.8.4753-4759.1993;
RA Tontonoz P., Kim J.B., Graves R.A., Spiegelman B.M.;
RT "ADD1: a novel helix-loop-helix transcription factor associated with
RT adipocyte determination and differentiation.";
RL Mol. Cell. Biol. 13:4753-4759(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1012 (ISOFORM SREBP-1C), AND VARIANT
RP MET-779.
RC STRAIN=BN-Lx/Cub, and SHR/Ola;
RX PubMed=11309661; DOI=10.1007/s003350010273;
RA Pravenec M., Jansa P., Kostka V., Zidek V., Kren V., Forejt J., Kurtz T.W.;
RT "Identification of a mutation in ADD1/SREBP-1 in the spontaneously
RT hypertensive rat.";
RL Mamm. Genome 12:295-298(2001).
RN [4]
RP DNA-BINDING.
RX PubMed=7739539; DOI=10.1128/mcb.15.5.2582;
RA Kim J.B., Spotts G.D., Halvorsen Y.D., Shih H.M., Ellenberger T.,
RA Towle H.C., Spiegelman B.M.;
RT "Dual DNA binding specificity of ADD1/SREBP1 controlled by a single amino
RT acid in the basic helix-loop-helix domain.";
RL Mol. Cell. Biol. 15:2582-2588(1995).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-448, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: [Sterol regulatory element-binding protein 1]: Precursor of
CC the transcription factor form (Processed sterol regulatory element-
CC binding protein 1), which is embedded in the endoplasmic reticulum
CC membrane (By similarity). Low sterol concentrations promote processing
CC of this form, releasing the transcription factor form that translocates
CC into the nucleus and activates transcription of genes involved in
CC cholesterol biosynthesis and lipid homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:P36956, ECO:0000250|UniProtKB:Q9WTN3}.
CC -!- FUNCTION: [Processed sterol regulatory element-binding protein 1]: Key
CC transcription factor that regulates expression of genes involved in
CC cholesterol biosynthesis and lipid homeostasis (By similarity). Binds
CC to the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3')
CC (PubMed:7739539). Has dual sequence specificity binding to both an E-
CC box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3') (By
CC similarity). Regulates the promoters of genes involved in cholesterol
CC biosynthesis and the LDL receptor (LDLR) pathway of sterol regulation
CC (By similarity). {ECO:0000250|UniProtKB:P36956,
CC ECO:0000269|PubMed:7739539}.
CC -!- FUNCTION: [Isoform SREBP-1A]: Isoform expressed only in select tissues,
CC which has higher transcriptional activity compared to SREBP-1C (By
CC similarity). Able to stimulate both lipogenic and cholesterogenic gene
CC expression (By similarity). Has a role in the nutritional regulation of
CC fatty acids and triglycerides in lipogenic organs such as the liver.
CC Required for innate immune response in macrophages by regulating lipid
CC metabolism (By similarity). {ECO:0000250|UniProtKB:P36956,
CC ECO:0000250|UniProtKB:Q9WTN3}.
CC -!- FUNCTION: [Isoform SREBP-1C]: Predominant isoform expressed in most
CC tissues, which has weaker transcriptional activity compared to isoform
CC SREBP-1A (By similarity). Primarily controls expression of lipogenic
CC gene (By similarity). Strongly activates global lipid synthesis in
CC rapidly growing cells (By similarity). {ECO:0000250|UniProtKB:P36956,
CC ECO:0000250|UniProtKB:Q9WTN3}.
CC -!- SUBUNIT: [Sterol regulatory element-binding protein 1]: Forms a tight
CC complex with SCAP, the SCAP-SREBP complex, in the endoplasmic reticulum
CC membrane. {ECO:0000250|UniProtKB:P36956}.
CC -!- SUBUNIT: [Processed sterol regulatory element-binding protein 1]:
CC Efficient DNA binding of the soluble transcription factor fragment
CC requires dimerization with another bHLH protein (By similarity).
CC Interacts with CEBPA, the interaction produces a transcriptional
CC synergy. Interacts with LMNA (By similarity).
CC {ECO:0000250|UniProtKB:P36956, ECO:0000250|UniProtKB:Q9WTN3}.
CC -!- SUBCELLULAR LOCATION: [Sterol regulatory element-binding protein 1]:
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P36956}; Multi-
CC pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9WTN3}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {ECO:0000250|UniProtKB:Q9WTN3}; Multi-pass membrane protein
CC {ECO:0000255}. Note=At high sterol concentrations, the SCAP-SREBP is
CC retained in the endoplasmic reticulum. Low sterol concentrations
CC promote recruitment into COPII-coated vesicles and transport of the
CC SCAP-SREBP to the Golgi, where it is processed.
CC {ECO:0000250|UniProtKB:Q9WTN3}.
CC -!- SUBCELLULAR LOCATION: [Processed sterol regulatory element-binding
CC protein 1]: Nucleus {ECO:0000250|UniProtKB:P36956}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=SREBP-1A;
CC IsoId=P56720-2; Sequence=Displayed;
CC Name=SREBP-1C; Synonyms=ADD1;
CC IsoId=P56720-1; Sequence=VSP_030860;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in brown adipose tissue.
CC {ECO:0000269|PubMed:8336713}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:P36956}.
CC -!- PTM: [Sterol regulatory element-binding protein 1]: Processed in the
CC Golgi apparatus, releasing the protein from the membrane. At low
CC cholesterol the SCAP-SREBP complex is recruited into COPII vesicles for
CC export from the endoplasmic reticulum. In the Golgi, complex SREBPs are
CC cleaved sequentially by site-1 (MBTPS1, S1P) and site-2 (MBTPS2, S2P)
CC proteases. The first cleavage by site-1 protease occurs within the
CC luminal loop, the second cleavage by site-2 protease occurs within the
CC first transmembrane domain, releasing the transcription factor from the
CC Golgi membrane. {ECO:0000250|UniProtKB:P36956}.
CC -!- PTM: Phosphorylated by AMPK, leading to suppress protein processing and
CC nuclear translocation, and repress target gene expression.
CC Phosphorylation at Ser-395 by SIK1 represses activity possibly by
CC inhibiting DNA-binding. {ECO:0000250|UniProtKB:Q9WTN3}.
CC -!- PTM: [Processed sterol regulatory element-binding protein 1]:
CC Ubiquitinated; the nuclear form has a rapid turnover and is rapidly
CC ubiquitinated and degraded by the proteasome in the nucleus.
CC {ECO:0000250|UniProtKB:P36956}.
CC -!- SIMILARITY: Belongs to the SREBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=L16995; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AABR03073826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03076830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L16995; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF286469; AAG28733.2; -; mRNA.
DR EMBL; AF286470; AAG28734.2; ALT_TERM; mRNA.
DR RefSeq; NP_001263636.1; NM_001276707.1. [P56720-2]
DR RefSeq; NP_001263637.1; NM_001276708.1. [P56720-1]
DR AlphaFoldDB; P56720; -.
DR SMR; P56720; -.
DR BioGRID; 249376; 9.
DR STRING; 10116.ENSRNOP00000050057; -.
DR iPTMnet; P56720; -.
DR PhosphoSitePlus; P56720; -.
DR PaxDb; P56720; -.
DR PRIDE; P56720; -.
DR Ensembl; ENSRNOT00000004753; ENSRNOP00000004753; ENSRNOG00000003463. [P56720-1]
DR Ensembl; ENSRNOT00000047053; ENSRNOP00000050057; ENSRNOG00000003463. [P56720-2]
DR GeneID; 78968; -.
DR KEGG; rno:78968; -.
DR UCSC; RGD:69423; rat. [P56720-2]
DR CTD; 6720; -.
DR RGD; 69423; Srebf1.
DR eggNOG; KOG2588; Eukaryota.
DR GeneTree; ENSGT00940000159156; -.
DR InParanoid; P56720; -.
DR OMA; QLCQHIP; -.
DR OrthoDB; 330300at2759; -.
DR PhylomeDB; P56720; -.
DR TreeFam; TF313894; -.
DR Reactome; R-RNO-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
DR Reactome; R-RNO-191273; Cholesterol biosynthesis.
DR PRO; PR:P56720; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003463; Expressed in liver and 19 other tissues.
DR Genevisible; P56720; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:HGNC-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:RGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0032810; F:sterol response element binding; ISS:HGNC-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0009267; P:cellular response to starvation; IDA:HGNC-UCL.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; IMP:RGD.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0008610; P:lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010876; P:lipid localization; IEP:RGD.
DR GO; GO:0030324; P:lung development; IEP:RGD.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:RGD.
DR GO; GO:0045089; P:positive regulation of innate immune response; ISO:RGD.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISO:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:RGD.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; ISO:RGD.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; ISO:RGD.
DR GO; GO:0003062; P:regulation of heart rate by chemical signal; ISO:RGD.
DR GO; GO:0050796; P:regulation of insulin secretion; ISO:RGD.
DR GO; GO:0010883; P:regulation of lipid storage; IEP:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:1903214; P:regulation of protein targeting to mitochondrion; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR GO; GO:0032094; P:response to food; IEP:RGD.
DR GO; GO:0033762; P:response to glucagon; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; ISO:RGD.
DR GO; GO:0032868; P:response to insulin; TAS:BHF-UCL.
DR GO; GO:0033993; P:response to lipid; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0032933; P:SREBP signaling pathway; ISS:UniProtKB.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cholesterol metabolism;
KW Cytoplasmic vesicle; DNA-binding; Endoplasmic reticulum; Golgi apparatus;
KW Lipid metabolism; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Steroid metabolism; Sterol metabolism; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..1134
FT /note="Sterol regulatory element-binding protein 1"
FT /id="PRO_0000127450"
FT CHAIN 1..480
FT /note="Processed sterol regulatory element-binding protein
FT 1"
FT /evidence="ECO:0000250|UniProtKB:Q12772"
FT /id="PRO_0000314031"
FT TOPO_DOM 1..481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..536
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..1134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 317..367
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..60
FT /note="Transcriptional activation (acidic)"
FT /evidence="ECO:0000250|UniProtKB:P36956"
FT REGION 46..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..487
FT /note="Interaction with LMNA"
FT /evidence="ECO:0000250|UniProtKB:Q9WTN3"
FT REGION 367..388
FT /note="Leucine-zipper"
FT REGION 415..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 27..35
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P36956"
FT COMPBIAS 60..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 451..452
FT /note="Cleavage; by caspase-3 and caspase-7"
FT /evidence="ECO:0000250|UniProtKB:Q12772"
FT SITE 480..481
FT /note="Cleavage; by MBTPS2"
FT /evidence="ECO:0000250|UniProtKB:Q12772"
FT SITE 519..520
FT /note="Cleavage; by MBTPS1"
FT /evidence="ECO:0000250|UniProtKB:P36956"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36956"
FT MOD_RES 331
FT /note="Phosphoserine; by SIK1"
FT /evidence="ECO:0000250|UniProtKB:Q9WTN3"
FT MOD_RES 332
FT /note="Phosphoserine; by SIK1"
FT /evidence="ECO:0000250|UniProtKB:Q9WTN3"
FT MOD_RES 389
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:Q9WTN3"
FT MOD_RES 395
FT /note="Phosphoserine; by SIK1"
FT /evidence="ECO:0000250|UniProtKB:Q9WTN3"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1047
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36956"
FT VAR_SEQ 1..29
FT /note="MDELPFGEAALEQALAEVCEMDAALLTDI -> MDCTF (in isoform
FT SREBP-1C)"
FT /evidence="ECO:0000303|PubMed:11309661,
FT ECO:0000303|PubMed:8336713"
FT /id="VSP_030860"
FT VARIANT 779
FT /note="V -> M (in spontaneously hypertensive rats)"
FT /evidence="ECO:0000269|PubMed:11309661"
FT CONFLICT 267
FT /note="G -> A (in Ref. 1; L16995)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="R -> P (in Ref. 1; L16995)"
FT /evidence="ECO:0000305"
FT CONFLICT 817
FT /note="D -> H (in Ref. 1; L16995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1134 AA; 120521 MW; 1D31A9AD3C36AB29 CRC64;
MDELPFGEAA LEQALAEVCE MDAALLTDIE DMLQLINNQD SDFPGLFDAP YAGGETGDTG
PSSPGASSPE SFSSPASLGS SLEAFLGGPK VTPAPLSPPP SAPTAVKMYP SVPPFSPGPG
IKEEPVPLTI LQPPAPQPSP GTLLPPSFPP PPVQLSPAPV LGYSSLPSGF SGTLPGNTQQ
TPSSLPLGST PGISPTPLHT QVQSSAAQQP PPASAAPRMS TVASQIQQVP VVLQPHFIKA
DSLLLTAVKT DTGATMKTAG INTLAPGTAV QAGPLQTLVS GGTILATVPL VVDTDKLPIH
RLAAGGKALG SAQSRGEKRT AHNAIEKRYR SSINDKIVEL KDLVVGTEAK LNKSAVLRKA
IDYIRFLQHS NQKLKQENLT LRSAHKSKSL KDLVSACGSG GGTDVSMEGM KPEVVETLTP
PPSDAGSPSQ SSPLSLGSRG SSSGGSDSEP DSPAFEDNQV KAQRLPSHSR GMLDRSRLAL
CVLVFLCLTC NPLASLFGWG ILTPSDASGV HRSSGRSMLE AESRDGSNWT QWLLPPLVWL
ANGLLVLACL ALLFVYGEPV TRPHSGPAVH FWRHRKQADL DLARGDFAQA AQQLWLALQA
LGRPLPTSNL DLACSLLWNL VRHLLQRLWV GRWLAGQAGG LQRDYRLRKD ARASARDAAV
VYHKLHQLHA MGKYTGGHLV ASNLALSALN LAECAGDAIS MATLAEIYVA AALRVKTSLP
RALHFLTRFF LSSARQACLA QSGAVPLAMQ WLCHPVGHRF FVDGDWAVHG APQESLYSVA
GNPVDPLAQV TRLFCEHLLE RALNCIAQPS PGAADGDREF SDALGYLQLL NSCSDAVGAP
ACSFSVSSSM ATTTGTDPVA KWWASLTAVV IHWLRRDEEA AERLYPLVEH IPQVLQETER
PLPRAALYSF KAARALLDHR KVESSPASLA ICEKASGYLR DSLASTSTAS SIDKAMQLLL
CDLLLVARTS LWRRQQSAAS AQGAHGTSNG PQASALELRG FQHDLSSLRR LAQSFRPAMR
RVFLHEATAR LMAGASPART HQLLDRSLRR RAGSSGKGGA AAELEPRPTW REHTEALLLA
SCYLPPAFLS APGQRVSMLA EAARTVEKLG DHRLLLDCQQ MLLRLGGGTT VTSS
