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Sterol regulatory element-binding protein 2 (SREBP-2) (Class D basic helix-loop-helix protein 2) (bHLHd2) (Sterol regulatory element-binding transcription factor 2) [Cleaved into: Processed sterol regulatory element-binding protein 2]

 SRBP2_HUMAN             Reviewed;        1141 AA.
Q12772; Q05BD5; Q6GTH7; Q86V36; Q9UH04;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
31-JAN-2018, entry version 184.
RecName: Full=Sterol regulatory element-binding protein 2;
Short=SREBP-2;
AltName: Full=Class D basic helix-loop-helix protein 2;
Short=bHLHd2;
AltName: Full=Sterol regulatory element-binding transcription factor 2;
Contains:
RecName: Full=Processed sterol regulatory element-binding protein 2;
Name=SREBF2; Synonyms=BHLHD2, SREBP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-595.
PubMed=7903453; DOI=10.1073/pnas.90.24.11603;
Hua X., Yokoyama C., Wu J., Briggs M.R., Brown M.S., Goldstein J.L.,
Wang X.;
"SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that
stimulates transcription by binding to a sterol regulatory element.";
Proc. Natl. Acad. Sci. U.S.A. 90:11603-11607(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lymph, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 91-109.
PubMed=8402897; DOI=10.1016/S0092-8674(05)80095-9;
Yokoyama C., Wang X., Briggs M.R., Admon A., Wu J., Hua X.,
Goldstein J.L., Brown M.S.;
"SREBP-1, a basic-helix-loop-helix-leucine zipper protein that
controls transcription of the low density lipoprotein receptor gene.";
Cell 75:187-197(1993).
[6]
CHARACTERIZATION, AND MUTAGENESIS OF ASP-478; ARG-519 AND
478-ASP--ARG-481.
PubMed=8626610; DOI=10.1074/jbc.271.17.10379;
Hua X., Sakai J., Brown M.S., Goldstein J.L.;
"Regulated cleavage of sterol regulatory element binding proteins
requires sequences on both sides of the endoplasmic reticulum
membrane.";
J. Biol. Chem. 271:10379-10384(1996).
[7]
CLEAVAGE AT ASP-468 BY CASPASES.
PubMed=8643593; DOI=10.1073/pnas.93.11.5437;
Pai J.-T., Brown M.S., Goldstein J.L.;
"Purification and cDNA cloning of a second apoptosis-related cysteine
protease that cleaves and activates sterol regulatory element binding
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 93:5437-5442(1996).
[8]
CLEAVAGE BY S2P, AND MUTAGENESIS OF ARG-479; ARG-481; LEU-484;
CYS-485; 478-ASP--ARG-481; 479-ARG--ARG-481 AND 484-LEU-CYS-485.
PubMed=9651382; DOI=10.1074/jbc.273.28.17801;
Duncan E.A., Dave U.P., Sakai J., Goldstein J.L., Brown M.S.;
"Second-site cleavage in sterol regulatory element-binding protein
occurs at transmembrane junction as determined by cysteine panning.";
J. Biol. Chem. 273:17801-17809(1998).
[9]
CLEAVAGE BY S2P, AND MUTAGENESIS OF ASN-495; PRO-496; 490-LEU-CYS-491
AND 495-ASN-PRO-496.
PubMed=10805775; DOI=10.1073/pnas.97.10.5123;
Ye J., Dave U.P., Grishin N.V., Goldstein J.L., Brown M.S.;
"Asparagine-proline sequence within membrane-spanning segment of SREBP
triggers intramembrane cleavage by site-2 protease.";
Proc. Natl. Acad. Sci. U.S.A. 97:5123-5128(2000).
[10]
INTERACTION WITH RNF139.
PubMed=19706601; DOI=10.1074/jbc.M109.041376;
Irisawa M., Inoue J., Ozawa N., Mori K., Sato R.;
"The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8
hampers ER to Golgi transport of sterol regulatory element-binding
protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces
SREBP-2 cleavage.";
J. Biol. Chem. 284:28995-29004(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-855 AND SER-1098, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-464, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[13]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 343-403.
PubMed=14645851; DOI=10.1126/science.1088372;
Lee S.J., Sekimoto T., Yamashita E., Nagoshi E., Nakagawa A.,
Imamoto N., Yoshimura M., Sakai H., Chong K.T., Tsukihara T.,
Yoneda Y.;
"The structure of importin-beta bound to SREBP-2: nuclear import of a
transcription factor.";
Science 302:1571-1575(2003).
[14]
VARIANTS [LARGE SCALE ANALYSIS] SER-273 AND LYS-347.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: 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. {ECO:0000250}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:19706601}.
-!- INTERACTION:
Q92793:CREBBP; NbExp=2; IntAct=EBI-465059, EBI-81215;
P41235:HNF4A; NbExp=2; IntAct=EBI-465059, EBI-1049011;
Q96RN5:MED15; NbExp=2; IntAct=EBI-465059, EBI-394506;
P08047:SP1; NbExp=3; IntAct=EBI-465059, EBI-298336;
P04637:TP53; NbExp=3; IntAct=EBI-465059, EBI-366083;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein. Golgi apparatus membrane; Multi-pass membrane
protein. Cytoplasmic vesicle, COPII-coated vesicle membrane;
Multi-pass membrane protein. Note=Moves from the endoplasmic
reticulum to the Golgi in the absence of sterols.
-!- SUBCELLULAR LOCATION: Processed sterol regulatory element-binding
protein 2: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q12772-1; Sequence=Displayed;
Name=2;
IsoId=Q12772-2; Sequence=VSP_054283, VSP_054284, VSP_054285;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed in adult and fetal
tissues.
-!- PTM: 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. {ECO:0000269|PubMed:10805775,
ECO:0000269|PubMed:8643593, ECO:0000269|PubMed:9651382}.
-!- PTM: Phosphorylated by AMPK, leading to suppress protein
processing and nuclear translocation, and repress target gene
expression. {ECO:0000250}.
-!- SIMILARITY: Belongs to the SREBP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH51799.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; U02031; AAA50746.1; -; mRNA.
EMBL; CT841522; CAJ86452.1; -; mRNA.
EMBL; AL021453; CAI22917.1; -; Genomic_DNA.
EMBL; Z99716; CAI22917.1; JOINED; Genomic_DNA.
EMBL; Z99716; CAI41688.1; -; Genomic_DNA.
EMBL; AL021453; CAI41688.1; JOINED; Genomic_DNA.
EMBL; BC051385; AAH51385.1; -; mRNA.
EMBL; BC051799; AAH51799.1; ALT_INIT; mRNA.
EMBL; BC056158; AAH56158.1; -; mRNA.
CCDS; CCDS14023.1; -. [Q12772-1]
PIR; A49397; A54962.
RefSeq; NP_004590.2; NM_004599.3. [Q12772-1]
UniGene; Hs.443258; -.
PDB; 1UKL; X-ray; 3.00 A; C/D/E/F=343-403.
PDBsum; 1UKL; -.
ProteinModelPortal; Q12772; -.
SMR; Q12772; -.
BioGrid; 112599; 71.
DIP; DIP-263N; -.
ELM; Q12772; -.
IntAct; Q12772; 48.
MINT; MINT-144301; -.
STRING; 9606.ENSP00000354476; -.
BindingDB; Q12772; -.
ChEMBL; CHEMBL1795166; -.
iPTMnet; Q12772; -.
PhosphoSitePlus; Q12772; -.
BioMuta; SREBF2; -.
DMDM; 116242800; -.
EPD; Q12772; -.
MaxQB; Q12772; -.
PaxDb; Q12772; -.
PeptideAtlas; Q12772; -.
PRIDE; Q12772; -.
DNASU; 6721; -.
Ensembl; ENST00000361204; ENSP00000354476; ENSG00000198911. [Q12772-1]
GeneID; 6721; -.
KEGG; hsa:6721; -.
UCSC; uc003bbi.5; human. [Q12772-1]
CTD; 6721; -.
DisGeNET; 6721; -.
EuPathDB; HostDB:ENSG00000198911.11; -.
GeneCards; SREBF2; -.
HGNC; HGNC:11290; SREBF2.
HPA; HPA031962; -.
HPA; HPA031963; -.
MIM; 600481; gene.
neXtProt; NX_Q12772; -.
OpenTargets; ENSG00000198911; -.
PharmGKB; PA336; -.
eggNOG; KOG2588; Eukaryota.
eggNOG; ENOG410XSVP; LUCA.
GeneTree; ENSGT00390000017651; -.
HOGENOM; HOG000186198; -.
HOVERGEN; HBG061592; -.
InParanoid; Q12772; -.
KO; K09107; -.
OMA; GEVDAWP; -.
OrthoDB; EOG091G01RE; -.
PhylomeDB; Q12772; -.
TreeFam; TF313894; -.
Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
SIGNOR; Q12772; -.
EvolutionaryTrace; Q12772; -.
GeneWiki; SREBF2; -.
GenomeRNAi; 6721; -.
PMAP-CutDB; Q12772; -.
PRO; PR:Q12772; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000198911; -.
CleanEx; HS_SREBF2; -.
ExpressionAtlas; Q12772; baseline and differential.
Genevisible; Q12772; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032937; C:SREBP-SCAP-Insig complex; IDA:UniProtKB.
GO; GO:0070888; F:E-box binding; IDA:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0071499; P:cellular response to laminar fluid shear stress; NAS:BHF-UCL.
GO; GO:0009267; P:cellular response to starvation; IMP:ParkinsonsUK-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0090370; P:negative regulation of cholesterol efflux; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0010886; P:positive regulation of cholesterol storage; IDA:BHF-UCL.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; TAS:Reactome.
GO; GO:2000188; P:regulation of cholesterol homeostasis; IEA:Ensembl.
GO; GO:0072368; P:regulation of lipid transport by negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0055098; P:response to low-density lipoprotein particle stimulus; IEP:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Cholesterol metabolism;
Complete proteome; Cytoplasmic vesicle; Direct protein sequencing;
DNA-binding; Endoplasmic reticulum; Golgi apparatus; Isopeptide bond;
Lipid metabolism; Membrane; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Steroid metabolism; Sterol metabolism;
Transcription; Transcription regulation; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 1141 Sterol regulatory element-binding protein
2.
/FTId=PRO_0000127452.
CHAIN 1 484 Processed sterol regulatory element-
binding protein 2.
/FTId=PRO_0000314033.
TOPO_DOM 1 479 Cytoplasmic. {ECO:0000255}.
TRANSMEM 480 500 Helical. {ECO:0000255}.
TOPO_DOM 501 533 Lumenal. {ECO:0000255}.
TRANSMEM 534 554 Helical. {ECO:0000255}.
TOPO_DOM 555 1139 Cytoplasmic. {ECO:0000255}.
DOMAIN 330 380 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 1 50 Transcriptional activation (acidic).
REGION 237 491 Interaction with LMNA. {ECO:0000250}.
REGION 380 401 Leucine-zipper.
COMPBIAS 52 124 Gly/Pro/Ser-rich.
COMPBIAS 125 244 Gln-rich.
SITE 468 469 Cleavage; by caspase-3 and caspase-7.
SITE 484 485 Cleavage; by S2P.
SITE 522 523 Cleavage; by S1P.
MOD_RES 855 855 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1098 1098 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 464 464 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 273 275 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054283.
VAR_SEQ 589 684 DFAAAAGNLQTCLAVLGRALPTSRLDLACSLSWNVIRYSLQ
KLRLVRWLLKKVFQCRRATPATEAGFEDEAKTSARDAALAY
HRLHQLHITGKLPA -> VYGKKSGATHSIEEELNIHISRG
TRTRTLLSSRRFCSCCRQPTNLPGSFGPGTAHLPPGPGLQP
LLERDPLQPAEATPGALAAQESLPVPAGHASH (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054284.
VAR_SEQ 685 1141 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054285.
VARIANT 273 273 A -> S (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036394.
VARIANT 347 347 N -> K (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036395.
VARIANT 536 536 M -> L (in dbSNP:rs17002714).
/FTId=VAR_049550.
VARIANT 595 595 G -> A (in dbSNP:rs2228314).
{ECO:0000269|PubMed:7903453}.
/FTId=VAR_028440.
VARIANT 623 623 V -> M (in dbSNP:rs2229440).
/FTId=VAR_028441.
VARIANT 860 860 R -> S (in dbSNP:rs2228313).
/FTId=VAR_049551.
MUTAGEN 478 481 DRSR->AAAA: Loss of cleavage by S2P.
{ECO:0000269|PubMed:8626610,
ECO:0000269|PubMed:9651382}.
MUTAGEN 478 481 DRSR->AS: Loss of cleavage by S2P.
{ECO:0000269|PubMed:8626610,
ECO:0000269|PubMed:9651382}.
MUTAGEN 478 478 D->A: No effect on proteolytic processing
in response to low sterol.
{ECO:0000269|PubMed:8626610}.
MUTAGEN 479 481 RSR->AAA: Loss of cleavage by S2P.
{ECO:0000269|PubMed:9651382}.
MUTAGEN 479 479 R->A: No effect on cleavage by S2P.
{ECO:0000269|PubMed:9651382}.
MUTAGEN 481 481 R->A: No effect on cleavage by S2P.
{ECO:0000269|PubMed:9651382}.
MUTAGEN 484 485 LC->FF: No effect on cleavage by S2P.
{ECO:0000269|PubMed:9651382}.
MUTAGEN 484 484 L->A: No effect on cleavage by S2P.
{ECO:0000269|PubMed:9651382}.
MUTAGEN 485 485 C->A: No effect on cleavage by S2P.
{ECO:0000269|PubMed:9651382}.
MUTAGEN 490 491 LC->NP: Restores cleavage by S2P; when
associated with F-495 and L-496. No
effect on site of cleavage by S2P.
{ECO:0000269|PubMed:10805775}.
MUTAGEN 495 496 NP->FL: Loss of cleavage by S2P.
{ECO:0000269|PubMed:10805775}.
MUTAGEN 495 495 N->F: Reduced cleavage by S2P.
{ECO:0000269|PubMed:10805775}.
MUTAGEN 496 496 P->L: Reduced cleavage by S2P.
{ECO:0000269|PubMed:10805775}.
MUTAGEN 519 519 R->A: Loss of proteolytic processing in
response to low sterol.
{ECO:0000269|PubMed:8626610}.
MUTAGEN 519 519 R->K: No effect on proteolytic processing
in response to low sterol.
{ECO:0000269|PubMed:8626610}.
CONFLICT 961 961 A -> G (in Ref. 1; AAA50746).
{ECO:0000305}.
CONFLICT 1045 1045 A -> G (in Ref. 1; AAA50746).
{ECO:0000305}.
HELIX 346 357 {ECO:0000244|PDB:1UKL}.
TURN 366 368 {ECO:0000244|PDB:1UKL}.
HELIX 369 399 {ECO:0000244|PDB:1UKL}.
SEQUENCE 1141 AA; 123688 MW; 481B1D8E2A2306D2 CRC64;
MDDSGELGGL ETMETLTELG DELTLGDIDE MLQFVSNQVG EFPDLFSEQL CSSFPGSGGS
GSSSGSSGSS SSSSNGRGSS SGAVDPSVQR SFTQVTLPSF SPSAASPQAP TLQVKVSPTS
VPTTPRATPI LQPRPQPQPQ PQTQLQQQTV MITPTFSTTP QTRIIQQPLI YQNAATSFQV
LQPQVQSLVT SSQVQPVTIQ QQVQTVQAQR VLTQTANGTL QTLAPATVQT VAAPQVQQVP
VLVQPQIIKT DSLVLTTLKT DGSPVMAAVQ NPALTALTTP IQTAALQVPT LVGSSGTILT
TMPVMMGQEK VPIKQVPGGV KQLEPPKEGE RRTTHNIIEK RYRSSINDKI IELKDLVMGT
DAKMHKSGVL RKAIDYIKYL QQVNHKLRQE NMVLKLANQK NKLLKGIDLG SLVDNEVDLK
IEDFNQNVLL MSPPASDSGS QAGFSPYSID SEPGSPLLDD AKVKDEPDSP PVALGMVDRS
RILLCVLTFL CLSFNPLTSL LQWGGAHDSD QHPHSGSGRS VLSFESGSGG WFDWMMPTLL
LWLVNGVIVL SVFVKLLVHG EPVIRPHSRS SVTFWRHRKQ ADLDLARGDF AAAAGNLQTC
LAVLGRALPT SRLDLACSLS WNVIRYSLQK LRLVRWLLKK VFQCRRATPA TEAGFEDEAK
TSARDAALAY HRLHQLHITG KLPAGSACSD VHMALCAVNL AECAEEKIPP STLVEIHLTA
AMGLKTRCGG KLGFLASYFL SRAQSLCGPE HSAVPDSLRW LCHPLGQKFF MERSWSVKSA
AKESLYCAQR NPADPIAQVH QAFCKNLLER AIESLVKPQA KKKAGDQEEE SCEFSSALEY
LKLLHSFVDS VGVMSPPLSR SSVLKSALGP DIICRWWTSA ITVAISWLQG DDAAVRSHFT
KVERIPKALE VTESPLVKAI FHACRAMHAS LPGKADGQQS SFCHCERASG HLWSSLNVSG
ATSDPALNHV VQLLTCDLLL SLRTALWQKQ ASASQAVGET YHASGAELAG FQRDLGSLRR
LAHSFRPAYR KVFLHEATVR LMAGASPTRT HQLLEHSLRR RTTQSTKHGE VDAWPGQRER
ATAILLACRH LPLSFLSSPG QRAVLLAEAA RTLEKVGDRR SCNDCQQMIV KLGGGTAIAA
S


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