SRBP1_HUMAN
ID SRBP1_HUMAN Reviewed; 1147 AA.
AC P36956; B0I4X3; B0I4X4; D3DXC4; Q16062; Q59F52; Q6P4R7; Q6PFW7; Q6PJ36;
AC Q8TAK9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Sterol regulatory element-binding protein 1 {ECO:0000303|PubMed:8402897};
DE Short=SREBP-1 {ECO:0000303|PubMed:8402897};
DE AltName: Full=Class D basic helix-loop-helix protein 1;
DE Short=bHLHd1;
DE AltName: Full=Sterol regulatory element-binding transcription factor 1 {ECO:0000303|PubMed:8402897};
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:0000303|PubMed:7759101, ECO:0000312|HGNC:HGNC:11289};
GN Synonyms=BHLHD1, SREBP1 {ECO:0000303|PubMed:8402897};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SREBP-1A), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 1-29 (ISOFORM SREBP-1C), NUCLEOTIDE SEQUENCE [MRNA] OF 1035-1147
RP (ISOFORMS SREBP-1B AND SREBP-1C), PARTIAL PROTEIN SEQUENCE, VARIANT
RP ALA-1000, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=8402897; DOI=10.1016/s0092-8674(05)80095-9;
RA Yokoyama C., Wang X., Briggs M.R., Admon A., Wu J., Hua X., Goldstein J.L.,
RA Brown M.S.;
RT "SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls
RT transcription of the low density lipoprotein receptor gene.";
RL Cell 75:187-197(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-1000.
RC TISSUE=Fetal brain;
RX PubMed=7759101; DOI=10.1016/0888-7543(95)80009-b;
RA Hua X., Wu J., Goldstein J.L., Brown M.S., Hobbs H.H.;
RT "Structure of the human gene encoding sterol regulatory element binding
RT protein-1 (SREBF1) and localization of SREBF1 and SREBF2 to chromosomes
RT 17p11.2 and 22q13.";
RL Genomics 25:667-673(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SREBP-1ADELTA AND SREBP-1CDELTA),
RP SUBCELLULAR LOCATION (ISOFORMS SREBP-1ADELTA AND SREBP-1CDELTA), AND
RP FUNCTION (ISOFORMS SREBP-1ADELTA AND SREBP-1CDELTA).
RC TISSUE=Liver;
RX PubMed=18267114; DOI=10.1016/j.bbrc.2008.02.004;
RA Harada N., Yonemoto H., Yoshida M., Yamamoto H., Yin Y., Miyamoto A.,
RA Hattori A., Wu Q., Nakagawa T., Nakano M., Teshigawara K., Mawatari K.,
RA Hosaka T., Takahashi A., Nakaya Y.;
RT "Alternative splicing produces a constitutively active form of human SREBP-
RT 1.";
RL Biochem. Biophys. Res. Commun. 368:820-826(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM SREBP-1A).
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SREBP-1A AND 4), AND
RP VARIANTS SER-306 AND LEU-834.
RC TISSUE=Brain, Placenta, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-1147 (ISOFORM SREBP-1A/4).
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=11477106; DOI=10.1074/jbc.m105200200;
RA Hirano Y., Yoshida M., Shimizu M., Sato R.;
RT "Direct demonstration of rapid degradation of nuclear sterol regulatory
RT element-binding proteins by the ubiquitin-proteasome pathway.";
RL J. Biol. Chem. 276:36431-36437(2001).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12202038; DOI=10.1016/s0092-8674(02)00872-3;
RA Yang T., Espenshade P.J., Wright M.E., Yabe D., Gong Y., Aebersold R.,
RA Goldstein J.L., Brown M.S.;
RT "Crucial step in cholesterol homeostasis: sterols promote binding of SCAP
RT to INSIG-1, a membrane protein that facilitates retention of SREBPs in
RT ER.";
RL Cell 110:489-500(2002).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF SER-455; ASP-456; SER-457; ASP-460; ASP-466;
RP GLY-481; MET-482; LEU-483; ASP-484; 484-ASP--ARG-487; ARG-485 AND ARG-527.
RX PubMed=8626610; DOI=10.1074/jbc.271.17.10379;
RA Hua X., Sakai J., Brown M.S., Goldstein J.L.;
RT "Regulated cleavage of sterol regulatory element binding proteins requires
RT sequences on both sides of the endoplasmic reticulum membrane.";
RL J. Biol. Chem. 271:10379-10384(1996).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF TYR-335.
RX PubMed=12177166;
RA Amemiya-Kudo M., Shimano H., Hasty A.H., Yahagi N., Yoshikawa T.,
RA Matsuzaka T., Okazaki H., Tamura Y., Iizuka Y., Ohashi K., Osuga J.,
RA Harada K., Gotoda T., Sato R., Kimura S., Ishibashi S., Yamada N.;
RT "Transcriptional activities of nuclear SREBP-1a, -1c, and -2 to different
RT target promoters of lipogenic and cholesterogenic genes.";
RL J. Lipid Res. 43:1220-1235(2002).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1060, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP REVIEW.
RX PubMed=28849786; DOI=10.1038/nrendo.2017.91;
RA Shimano H., Sato R.;
RT "SREBP-regulated lipid metabolism: convergent physiology - divergent
RT pathophysiology.";
RL Nat. Rev. Endocrinol. 13:710-730(2017).
RN [15]
RP 9AATAD MOTIF.
RX PubMed=31375868; DOI=10.1007/s00018-019-03251-w;
RA Piskacek M., Havelka M., Jendruchova K., Knight A., Keegan L.P.;
RT "The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with
RT valines and intron reservoirs.";
RL Cell. Mol. Life Sci. 77:1793-1810(2020).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-527, VARIANTS IFAP2
RP CYS-527; ASN-528 DEL AND PRO-530, AND CHARACTERIZATION OF VARIANTS IFAP2
RP CYS-527; ASN-528 DEL AND PRO-530.
RX PubMed=32497488; DOI=10.1016/j.ajhg.2020.05.006;
RA Wang H., Humbatova A., Liu Y., Qin W., Lee M., Cesarato N., Kortuem F.,
RA Kumar S., Romano M.T., Dai S., Mo R., Sivalingam S., Motameny S., Wu Y.,
RA Wang X., Niu X., Geng S., Bornholdt D., Kroisel P.M., Tadini G.,
RA Walter S.D., Hauck F., Girisha K.M., Calza A.M., Bottani A., Altmueller J.,
RA Buness A., Yang S., Sun X., Ma L., Kutsche K., Grzeschik K.H., Betz R.C.,
RA Lin Z.;
RT "Mutations in SREBF1, Encoding Sterol Regulatory Element Binding
RT Transcription Factor 1, Cause Autosomal-Dominant IFAP Syndrome.";
RL Am. J. Hum. Genet. 107:34-45(2020).
RN [17]
RP VARIANT HMD CYS-527.
RX PubMed=32902915; DOI=10.1002/ajmg.a.61849;
RA Chacon-Camacho O.F., Arce-Gonzalez R., Ordaz-Robles T.,
RA Perezpena-Diazconti M., Nava-Castaneda A., Zenteno J.C.;
RT "Exome sequencing identifies a SREBF1 recurrent ARG557CYS mutation as the
RT cause of hereditary mucoepithelial dysplasia in a family with high clinical
RT variability.";
RL Am. J. Med. Genet. A 182:2773-2777(2020).
RN [18]
RP VARIANTS HMD CYS-527 AND HIS-527.
RX PubMed=31790666; DOI=10.1016/j.jid.2019.10.014;
RA Morice-Picard F., Michaud V., Lasseaux E., Rezvani H.R., Plaisant C.,
RA Bessis D., Leaute-Labreze C., Arveiler B., Taieb A., Trimouille A.,
RA Boralevi F.;
RT "Hereditary Mucoepithelial Dysplasia Results from Heterozygous Variants at
RT p.Arg557 Mutational Hotspot in SREBF1, Encoding a Transcription Factor
RT Involved in Cholesterol Homeostasis.";
RL J. Invest. Dermatol. 140:e2.1289-e2.1292(2020).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SCAP, AND PROTEOLYTIC
RP CLEAVAGE.
RX PubMed=32322062; DOI=10.1038/s41586-020-2183-2;
RA Xu D., Wang Z., Xia Y., Shao F., Xia W., Wei Y., Li X., Qian X., Lee J.H.,
RA Du L., Zheng Y., Lv G., Leu J.S., Wang H., Xing D., Liang T., Hung M.C.,
RA Lu Z.;
RT "The gluconeogenic enzyme PCK1 phosphorylates INSIG1/2 for lipogenesis.";
RL Nature 580:530-535(2020).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 319-394.
RX PubMed=9634703; DOI=10.1016/s0969-2126(98)00067-7;
RA Parraga A., Bellsolell L., Ferre-D'Amare A.R., Burley S.K.;
RT "Co-crystal structure of sterol regulatory element binding protein 1a at
RT 2.3-A resolution.";
RL Structure 6:661-672(1998).
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 (PubMed:32322062). Low sterol concentrations promote
CC processing of this form, releasing the transcription factor form that
CC translocates into the nucleus and activates transcription of genes
CC involved in cholesterol biosynthesis and lipid homeostasis (By
CC similarity). {ECO:0000250|UniProtKB:Q9WTN3,
CC ECO:0000269|PubMed:32322062}.
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 (PubMed:8402897,
CC PubMed:12177166, PubMed:32322062). Binds to the sterol regulatory
CC element 1 (SRE-1) (5'-ATCACCCCAC-3'). Has dual sequence specificity
CC binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-
CC ATCACCCCAC-3') (PubMed:8402897, PubMed:12177166). Regulates the
CC promoters of genes involved in cholesterol biosynthesis and the LDL
CC receptor (LDLR) pathway of sterol regulation (PubMed:8402897,
CC PubMed:12177166, PubMed:32322062). {ECO:0000269|PubMed:12177166,
CC ECO:0000269|PubMed:32322062, ECO:0000269|PubMed:8402897}.
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 (PubMed:12177166, PubMed:32497488). Has a role in the
CC nutritional regulation of fatty acids and triglycerides in lipogenic
CC organs such as the liver (By similarity). Required for innate immune
CC response in macrophages by regulating lipid metabolism (By similarity).
CC {ECO:0000250|UniProtKB:Q9WTN3, ECO:0000269|PubMed:12177166,
CC ECO:0000269|PubMed:32497488}.
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 (PubMed:12177166). Strongly activates global lipid synthesis in
CC rapidly growing cells (By similarity). {ECO:0000250|UniProtKB:Q9WTN3,
CC ECO:0000269|PubMed:12177166}.
CC -!- FUNCTION: [Isoform SREBP-1aDelta]: The absence of Golgi proteolytic
CC processing requirement makes this isoform constitutively active in
CC transactivation of lipogenic gene promoters.
CC {ECO:0000305|PubMed:7759101}.
CC -!- FUNCTION: [Isoform SREBP-1cDelta]: The absence of Golgi proteolytic
CC processing requirement makes this isoform constitutively active in
CC transactivation of lipogenic gene promoters.
CC {ECO:0000305|PubMed:7759101}.
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:0000269|PubMed:32322062}.
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 (PubMed:8402897).
CC Interacts with CEBPA, the interaction produces a transcriptional
CC synergy (By similarity). Interacts with LMNA (By similarity).
CC {ECO:0000250|UniProtKB:Q9WTN3, ECO:0000269|PubMed:8402897}.
CC -!- INTERACTION:
CC P36956; P54253: ATXN1; NbExp=5; IntAct=EBI-948313, EBI-930964;
CC P36956; P42858: HTT; NbExp=3; IntAct=EBI-948313, EBI-466029;
CC P36956-1; Q92793: CREBBP; NbExp=3; IntAct=EBI-948328, EBI-81215;
CC P36956-1; Q96RN5: MED15; NbExp=7; IntAct=EBI-948328, EBI-394506;
CC P36956-1; P19659: GAL11; Xeno; NbExp=3; IntAct=EBI-948328, EBI-7305;
CC P36956-3; Q92793: CREBBP; NbExp=2; IntAct=EBI-948338, EBI-81215;
CC P36956-3; Q96RN5: MED15; NbExp=2; IntAct=EBI-948338, EBI-394506;
CC P36956-3; Q96EB6: SIRT1; NbExp=2; IntAct=EBI-948338, EBI-1802965;
CC PRO_0000314029; P02545-1: LMNA; NbExp=6; IntAct=EBI-22057616, EBI-351949;
CC -!- SUBCELLULAR LOCATION: [Sterol regulatory element-binding protein 1]:
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:12202038}; 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:0000269|PubMed:11477106,
CC ECO:0000269|PubMed:32322062}.
CC -!- SUBCELLULAR LOCATION: [Isoform SREBP-1aDelta]: Nucleus
CC {ECO:0000269|PubMed:18267114, ECO:0000269|PubMed:32497488}.
CC -!- SUBCELLULAR LOCATION: [Isoform SREBP-1cDelta]: Nucleus
CC {ECO:0000269|PubMed:18267114, ECO:0000269|PubMed:32497488}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=SREBP-1A;
CC IsoId=P36956-1; Sequence=Displayed;
CC Name=SREBP-1B;
CC IsoId=P36956-2; Sequence=VSP_002150;
CC Name=SREBP-1C;
CC IsoId=P36956-3; Sequence=VSP_002149, VSP_002150;
CC Name=4;
CC IsoId=P36956-4; Sequence=VSP_030859;
CC Name=SREBP-1aDelta;
CC IsoId=P36956-5; Sequence=VSP_047598, VSP_047599;
CC Name=SREBP-1cDelta;
CC IsoId=P36956-6; Sequence=VSP_002149, VSP_047598, VSP_047599;
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues, most
CC abundant in liver and adrenal gland (PubMed:8402897). In fetal tissues
CC lung and liver shows highest expression (PubMed:8402897).
CC {ECO:0000269|PubMed:8402897}.
CC -!- TISSUE SPECIFICITY: [Isoform SREBP-1A]: Predominates in hepatoma cell
CC lines (PubMed:8402897). Also expressed in kidney, brain, white fat, and
CC muscle (PubMed:8402897). {ECO:0000269|PubMed:8402897}.
CC -!- TISSUE SPECIFICITY: [Isoform SREBP-1C]: Predominantly expressed in
CC liver and adipose tissues (PubMed:8402897). Also expressed in kidney,
CC brain, white fat, and muscle (PubMed:8402897).
CC {ECO:0000269|PubMed:8402897}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:31375868}.
CC -!- PTM: [Sterol regulatory element-binding protein 1]: Processed in the
CC Golgi apparatus, releasing the protein from the membrane
CC (PubMed:8626610, PubMed:32322062). At low cholesterol the SCAP-SREBP
CC complex is recruited into COPII vesicles for export from the
CC endoplasmic reticulum (PubMed:8626610, PubMed:32322062). In the Golgi,
CC complex SREBPs are cleaved sequentially by site-1 (MBTPS1, S1P) and
CC site-2 (MBTPS2, S2P) protease (PubMed:8626610, PubMed:32322062). The
CC first 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, releasing the transcription factor from the Golgi
CC membrane (PubMed:32322062). {ECO:0000269|PubMed:32322062,
CC ECO:0000269|PubMed:8626610}.
CC -!- PTM: Phosphorylated by AMPK, leading to suppress protein processing and
CC nuclear translocation, and repress target gene expression (By
CC similarity). Phosphorylation at Ser-402 by SIK1 represses activity
CC possibly by inhibiting DNA-binding (By similarity).
CC {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:0000269|PubMed:11477106}.
CC -!- DISEASE: IFAP syndrome 2 (IFAP2) [MIM:619016]: An autosomal dominant
CC form of IFAP syndrome, a disease characterized by a peculiar triad of
CC follicular ichthyosis, total or subtotal atrichia, and photophobia of
CC varying degree. IFAP2 patients manifest ichthyosis follicularis or
CC follicular hyperkeratosis, hyperkeratotic plaques, sparse to no body
CC hair, and photophobia with punctate corneal epithelial defects, corneal
CC pannus, and complicated cataract. Ultrastructural hair analysis shows
CC trichorrhexis nodosa. {ECO:0000269|PubMed:32497488}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Mucoepithelial dysplasia, hereditary (HMD) [MIM:158310]: An
CC autosomal dominant genodermatosis mainly characterized by chronic
CC mucosal lesions associated with keratitis, non-scarring alopecia,
CC keratosis pilaris and perineal intertrigo.
CC {ECO:0000269|PubMed:31790666, ECO:0000269|PubMed:32902915}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the SREBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB28522.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD92846.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Sterol regulatory element-binding
CC protein entry;
CC URL="https://en.wikipedia.org/wiki/Sterol_regulatory_element_binding_protein";
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DR EMBL; U00968; AAC50051.2; -; mRNA.
DR EMBL; S66167; AAB28522.2; ALT_INIT; mRNA.
DR EMBL; S66168; AAB28523.1; -; mRNA.
DR EMBL; AB373958; BAG06742.1; -; mRNA.
DR EMBL; AB373959; BAG06743.1; -; mRNA.
DR EMBL; AC122129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471196; EAW55689.1; -; Genomic_DNA.
DR EMBL; CH471196; EAW55690.1; -; Genomic_DNA.
DR EMBL; BC023621; AAH23621.1; -; mRNA.
DR EMBL; BC026962; AAH26962.1; -; mRNA.
DR EMBL; BC057388; AAH57388.1; -; mRNA.
DR EMBL; BC063281; AAH63281.1; -; mRNA.
DR EMBL; AB209609; BAD92846.1; ALT_SEQ; mRNA.
DR CCDS; CCDS11189.1; -. [P36956-1]
DR CCDS; CCDS32583.1; -. [P36956-4]
DR PIR; A48845; A48845.
DR RefSeq; NP_001005291.1; NM_001005291.2. [P36956-4]
DR RefSeq; NP_004167.3; NM_004176.4. [P36956-1]
DR PDB; 1AM9; X-ray; 2.30 A; A/B/C/D=319-400.
DR PDBsum; 1AM9; -.
DR AlphaFoldDB; P36956; -.
DR SMR; P36956; -.
DR BioGRID; 112598; 159.
DR CORUM; P36956; -.
DR DIP; DIP-331N; -.
DR IntAct; P36956; 29.
DR MINT; P36956; -.
DR STRING; 9606.ENSP00000348069; -.
DR ChEMBL; CHEMBL4630818; -.
DR DrugBank; DB03756; Doconexent.
DR DrugBank; DB13961; Fish oil.
DR DrugBank; DB11133; Omega-3 fatty acids.
DR DrugBank; DB09539; Omega-3-acid ethyl esters.
DR GlyGen; P36956; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P36956; -.
DR PhosphoSitePlus; P36956; -.
DR BioMuta; SREBF1; -.
DR DMDM; 166897633; -.
DR EPD; P36956; -.
DR jPOST; P36956; -.
DR MassIVE; P36956; -.
DR MaxQB; P36956; -.
DR PaxDb; P36956; -.
DR PeptideAtlas; P36956; -.
DR PRIDE; P36956; -.
DR ProteomicsDB; 2552; -.
DR ProteomicsDB; 55244; -. [P36956-1]
DR ProteomicsDB; 55245; -. [P36956-2]
DR ProteomicsDB; 55246; -. [P36956-3]
DR ProteomicsDB; 55247; -. [P36956-4]
DR Antibodypedia; 3952; 651 antibodies from 39 providers.
DR DNASU; 6720; -.
DR Ensembl; ENST00000261646.11; ENSP00000261646.5; ENSG00000072310.18. [P36956-1]
DR Ensembl; ENST00000355815.8; ENSP00000348069.4; ENSG00000072310.18. [P36956-4]
DR Ensembl; ENST00000395757.6; ENSP00000379106.2; ENSG00000072310.18. [P36956-2]
DR GeneID; 6720; -.
DR KEGG; hsa:6720; -.
DR MANE-Select; ENST00000261646.11; ENSP00000261646.5; NM_004176.5; NP_004167.3.
DR UCSC; uc002grt.3; human. [P36956-1]
DR CTD; 6720; -.
DR DisGeNET; 6720; -.
DR GeneCards; SREBF1; -.
DR HGNC; HGNC:11289; SREBF1.
DR HPA; ENSG00000072310; Tissue enhanced (adrenal).
DR MalaCards; SREBF1; -.
DR MIM; 158310; phenotype.
DR MIM; 184756; gene.
DR MIM; 619016; phenotype.
DR neXtProt; NX_P36956; -.
DR OpenTargets; ENSG00000072310; -.
DR Orphanet; 388; Hirschsprung disease.
DR PharmGKB; PA335; -.
DR VEuPathDB; HostDB:ENSG00000072310; -.
DR eggNOG; KOG2588; Eukaryota.
DR GeneTree; ENSGT00940000159156; -.
DR InParanoid; P36956; -.
DR OMA; QLCQHIP; -.
DR OrthoDB; 330300at2759; -.
DR PhylomeDB; P36956; -.
DR TreeFam; TF313894; -.
DR PathwayCommons; P36956; -.
DR Reactome; R-HSA-1368082; RORA activates gene expression.
DR Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
DR Reactome; R-HSA-191273; Cholesterol biosynthesis.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation. [P36956-1]
DR Reactome; R-HSA-9029558; NR1H2 & NR1H3 regulate gene expression linked to lipogenesis. [P36956-3]
DR Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
DR SignaLink; P36956; -.
DR SIGNOR; P36956; -.
DR BioGRID-ORCS; 6720; 181 hits in 1112 CRISPR screens.
DR ChiTaRS; SREBF1; human.
DR EvolutionaryTrace; P36956; -.
DR GeneWiki; SREBF1; -.
DR GenomeRNAi; 6720; -.
DR Pharos; P36956; Tbio.
DR PRO; PR:P36956; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P36956; protein.
DR Bgee; ENSG00000072310; Expressed in left adrenal gland and 103 other tissues.
DR ExpressionAtlas; P36956; baseline and differential.
DR Genevisible; P36956; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:HGNC-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0032810; F:sterol response element binding; IDA:HGNC-UCL.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; ISS:HGNC-UCL.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010876; P:lipid localization; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IEA:Ensembl.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; IEA:Ensembl.
DR GO; GO:0003062; P:regulation of heart rate by chemical signal; IEA:Ensembl.
DR GO; GO:0010883; P:regulation of lipid storage; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903214; P:regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0032094; P:response to food; IEA:Ensembl.
DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0032933; P:SREBP signaling pathway; IDA:UniProtKB.
DR Gene3D; 4.10.280.10; -; 1.
DR IDEAL; IID00235; -.
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 3D-structure; Activator; Alternative splicing; Cholesterol metabolism;
KW Cytoplasmic vesicle; Direct protein sequencing; Disease variant;
KW DNA-binding; Endoplasmic reticulum; Golgi apparatus; Ichthyosis;
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..1147
FT /note="Sterol regulatory element-binding protein 1"
FT /id="PRO_0000127447"
FT CHAIN 1..490
FT /note="Processed sterol regulatory element-binding protein
FT 1"
FT /evidence="ECO:0000250|UniProtKB:Q12772"
FT /id="PRO_0000314029"
FT TOPO_DOM 1..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..547
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..1147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 323..373
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..60
FT /note="Transcriptional activation (acidic)"
FT /evidence="ECO:0000305|PubMed:8402897"
FT REGION 39..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..497
FT /note="Interaction with LMNA"
FT /evidence="ECO:0000250|UniProtKB:Q9WTN3"
FT REGION 373..394
FT /note="Leucine-zipper"
FT REGION 421..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 27..35
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:31375868"
FT COMPBIAS 60..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..113
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 460..461
FT /note="Cleavage; by caspase-3 and caspase-7"
FT /evidence="ECO:0000250|UniProtKB:Q12772"
FT SITE 490..491
FT /note="Cleavage; by MBTPS2"
FT /evidence="ECO:0000250|UniProtKB:Q12772"
FT SITE 530..531
FT /note="Cleavage; by MBTPS1"
FT /evidence="ECO:0000305|PubMed:8626610"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56720"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 337
FT /note="Phosphoserine; by SIK1"
FT /evidence="ECO:0000250|UniProtKB:Q9WTN3"
FT MOD_RES 338
FT /note="Phosphoserine; by SIK1"
FT /evidence="ECO:0000250|UniProtKB:Q9WTN3"
FT MOD_RES 396
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:Q9WTN3"
FT MOD_RES 402
FT /note="Phosphoserine; by SIK1"
FT /evidence="ECO:0000250|UniProtKB:Q9WTN3"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTN3"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..29
FT /note="MDEPPFSEAALEQALGEPCDLDAALLTDI -> MDCTF (in isoform
FT SREBP-1C and isoform SREBP-1cDelta)"
FT /evidence="ECO:0000303|PubMed:18267114,
FT ECO:0000303|PubMed:8402897"
FT /id="VSP_002149"
FT VAR_SEQ 30
FT /note="E -> EGEVGAGRGRANGLDAPRAGADRGAMDCTFE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030859"
FT VAR_SEQ 469..470
FT /note="AK -> TE (in isoform SREBP-1aDelta and isoform
FT SREBP-1cDelta)"
FT /evidence="ECO:0000303|PubMed:18267114"
FT /id="VSP_047598"
FT VAR_SEQ 471..1147
FT /note="Missing (in isoform SREBP-1aDelta and isoform SREBP-
FT 1cDelta)"
FT /evidence="ECO:0000303|PubMed:18267114"
FT /id="VSP_047599"
FT VAR_SEQ 1035..1147
FT /note="VFLHEATARLMAGASPTRTHQLLDRSLRRRAGPGGKGGAVAELEPRPTRREH
FT AEALLLASCYLPPGFLSAPGQRVGMLAEAARTLEKLGDRRLLHDCQQMLMRLGGGTTVT
FT SS -> LMDVLTSESAWALPQHLGKGFPSPSGHKVPGWHGRMD (in isoform
FT SREBP-1B and isoform SREBP-1C)"
FT /evidence="ECO:0000303|PubMed:8402897"
FT /id="VSP_002150"
FT VARIANT 306
FT /note="N -> S (in dbSNP:rs17855793)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038468"
FT VARIANT 309
FT /note="A -> T (in dbSNP:rs35188700)"
FT /id="VAR_038469"
FT VARIANT 417
FT /note="V -> M (in dbSNP:rs2229590)"
FT /id="VAR_038470"
FT VARIANT 527
FT /note="R -> C (in IFAP2 and HMD; loss of sterol-regulated
FT protein processing; loss of localization to the nucleus;
FT decreased DNA-binding transcription factor activity RNA
FT polymerase II-specific)"
FT /evidence="ECO:0000269|PubMed:31790666,
FT ECO:0000269|PubMed:32497488, ECO:0000269|PubMed:32902915"
FT /id="VAR_085079"
FT VARIANT 527
FT /note="R -> H (in HMD; dbSNP:rs1428621525)"
FT /evidence="ECO:0000269|PubMed:31790666"
FT /id="VAR_085080"
FT VARIANT 528
FT /note="Missing (in IFAP2; loss of sterol-regulated protein
FT processing; loss of localization to the nucleus; decreased
FT DNA-binding transcription factor activity RNA polymerase
FT II-specific)"
FT /evidence="ECO:0000269|PubMed:32497488"
FT /id="VAR_085081"
FT VARIANT 530
FT /note="L -> P (in IFAP2; loss of sterol-regulated protein
FT processing; loss of localization to the nucleus; decreased
FT DNA-binding transcription factor activity RNA polymerase
FT II-specific)"
FT /evidence="ECO:0000269|PubMed:32497488"
FT /id="VAR_085082"
FT VARIANT 580
FT /note="V -> M (in dbSNP:rs36215896)"
FT /id="VAR_038471"
FT VARIANT 746
FT /note="R -> H (in dbSNP:rs2228461)"
FT /id="VAR_038472"
FT VARIANT 834
FT /note="S -> L (in dbSNP:rs17855792)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038473"
FT VARIANT 1000
FT /note="T -> A (in dbSNP:rs1042017)"
FT /evidence="ECO:0000269|PubMed:7759101,
FT ECO:0000269|PubMed:8402897"
FT /id="VAR_038474"
FT VARIANT 1008
FT /note="A -> P (in dbSNP:rs35014224)"
FT /id="VAR_038475"
FT MUTAGEN 335
FT /note="Y->R: Abolished transactivation activity."
FT /evidence="ECO:0000269|PubMed:12177166"
FT MUTAGEN 455
FT /note="S->A: No effect on proteolytic processing."
FT /evidence="ECO:0000269|PubMed:8626610"
FT MUTAGEN 456
FT /note="D->A: No effect on proteolytic processing."
FT /evidence="ECO:0000269|PubMed:8626610"
FT MUTAGEN 457
FT /note="S->A: No effect on proteolytic processing."
FT /evidence="ECO:0000269|PubMed:8626610"
FT MUTAGEN 460
FT /note="D->A: No effect on proteolytic processing."
FT /evidence="ECO:0000269|PubMed:8626610"
FT MUTAGEN 466
FT /note="D->A: No effect on proteolytic processing."
FT /evidence="ECO:0000269|PubMed:8626610"
FT MUTAGEN 481
FT /note="G->A: No effect on proteolytic processing."
FT /evidence="ECO:0000269|PubMed:8626610"
FT MUTAGEN 482
FT /note="M->A: No effect on proteolytic processing."
FT /evidence="ECO:0000269|PubMed:8626610"
FT MUTAGEN 483
FT /note="L->A: No effect on proteolytic processing."
FT /evidence="ECO:0000269|PubMed:8626610"
FT MUTAGEN 484..487
FT /note="DRSR->AS: Strong reduction of proteolytic processing
FT in response to low sterol."
FT /evidence="ECO:0000269|PubMed:8626610"
FT MUTAGEN 484
FT /note="D->A: Loss of proteolytic processing in response to
FT low sterol."
FT /evidence="ECO:0000269|PubMed:8626610"
FT MUTAGEN 485
FT /note="R->A: No effect on proteolytic processing."
FT /evidence="ECO:0000269|PubMed:8626610"
FT MUTAGEN 527
FT /note="R->A: Loss of proteolytic processing in response to
FT low sterol. Transcriptionally inactive."
FT /evidence="ECO:0000269|PubMed:32497488,
FT ECO:0000269|PubMed:8626610"
FT HELIX 321..350
FT /evidence="ECO:0007829|PDB:1AM9"
FT HELIX 359..396
FT /evidence="ECO:0007829|PDB:1AM9"
SQ SEQUENCE 1147 AA; 121675 MW; 58F28870739FF259 CRC64;
MDEPPFSEAA LEQALGEPCD LDAALLTDIE DMLQLINNQD SDFPGLFDPP YAGSGAGGTD
PASPDTSSPG SLSPPPATLS SSLEAFLSGP QAAPSPLSPP QPAPTPLKMY PSMPAFSPGP
GIKEESVPLS ILQTPTPQPL PGALLPQSFP APAPPQFSST PVLGYPSPPG GFSTGSPPGN
TQQPLPGLPL ASPPGVPPVS LHTQVQSVVP QQLLTVTAAP TAAPVTTTVT SQIQQVPVLL
QPHFIKADSL LLTAMKTDGA TVKAAGLSPL VSGTTVQTGP LPTLVSGGTI LATVPLVVDA
EKLPINRLAA GSKAPASAQS RGEKRTAHNA IEKRYRSSIN DKIIELKDLV VGTEAKLNKS
AVLRKAIDYI RFLQHSNQKL KQENLSLRTA VHKSKSLKDL VSACGSGGNT DVLMEGVKTE
VEDTLTPPPS DAGSPFQSSP LSLGSRGSGS GGSGSDSEPD SPVFEDSKAK PEQRPSLHSR
GMLDRSRLAL CTLVFLCLSC NPLASLLGAR GLPSPSDTTS VYHSPGRNVL GTESRDGPGW
AQWLLPPVVW LLNGLLVLVS LVLLFVYGEP VTRPHSGPAV YFWRHRKQAD LDLARGDFAQ
AAQQLWLALR ALGRPLPTSH LDLACSLLWN LIRHLLQRLW VGRWLAGRAG GLQQDCALRV
DASASARDAA LVYHKLHQLH TMGKHTGGHL TATNLALSAL NLAECAGDAV SVATLAEIYV
AAALRVKTSL PRALHFLTRF FLSSARQACL AQSGSVPPAM QWLCHPVGHR FFVDGDWSVL
STPWESLYSL AGNPVDPLAQ VTQLFREHLL ERALNCVTQP NPSPGSADGD KEFSDALGYL
QLLNSCSDAA GAPAYSFSIS SSMATTTGVD PVAKWWASLT AVVIHWLRRD EEAAERLCPL
VEHLPRVLQE SERPLPRAAL HSFKAARALL GCAKAESGPA SLTICEKASG YLQDSLATTP
ASSSIDKAVQ LFLCDLLLVV RTSLWRQQQP PAPAPAAQGT SSRPQASALE LRGFQRDLSS
LRRLAQSFRP AMRRVFLHEA TARLMAGASP TRTHQLLDRS LRRRAGPGGK GGAVAELEPR
PTRREHAEAL LLASCYLPPG FLSAPGQRVG MLAEAARTLE KLGDRRLLHD CQQMLMRLGG
GTTVTSS
