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Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)

 SCAP_CRIGR              Reviewed;        1276 AA.
P97260; Q2WEK9;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
25-OCT-2017, entry version 120.
RecName: Full=Sterol regulatory element-binding protein cleavage-activating protein;
Short=SCAP;
Short=SREBP cleavage-activating protein;
Name=SCAP;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF ASP-443.
TISSUE=Ovary;
PubMed=8898195; DOI=10.1016/S0092-8674(00)81362-8;
Hua X., Nohturfft A., Goldstein J.L., Brown M.S.;
"Sterol resistance in CHO cells traced to point mutation in SREBP
cleavage-activating protein.";
Cell 87:415-426(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 56-522, FUNCTION, INTERACTION WITH
INSIG1 AND INSIG2, AND MUTAGENESIS OF TYR-298; LEU-315 AND ASP-443.
TISSUE=Ovary;
PubMed=12482938; DOI=10.1073/pnas.262669399;
Yabe D., Xia Z.-P., Adams C.M., Rawson R.B.;
"Three mutations in sterol-sensing domain of SCAP block interaction
with insig and render SREBP cleavage insensitive to sterols.";
Proc. Natl. Acad. Sci. U.S.A. 99:16672-16677(2002).
[3]
INTERACTION WITH SREBF2.
PubMed=9488713; DOI=10.1074/jbc.273.10.5785;
Sakai J., Nohturfft A., Goldstein J.L., Brown M.S.;
"Cleavage of sterol regulatory element-binding proteins (SREBPs) at
site-1 requires interaction with SREBP cleavage-activating protein.
Evidence from in vivo competition studies.";
J. Biol. Chem. 273:5785-5793(1998).
[4]
TOPOLOGY, AND GLYCOSYLATION AT ASN-263; ASN-590 AND ASN-641.
PubMed=9642295; DOI=10.1074/jbc.273.27.17243;
Nohturfft A., Brown M.S., Goldstein J.L.;
"Topology of SREBP cleavage-activating protein, a polytopic membrane
protein with a sterol-sensing domain.";
J. Biol. Chem. 273:17243-17250(1998).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10497220; DOI=10.1074/jbc.274.40.28549;
Rawson R.B., DeBose-Boyd R., Goldstein J.L., Brown M.S.;
"Failure to cleave sterol regulatory element-binding proteins (SREBPs)
causes cholesterol auxotrophy in Chinese hamster ovary cells with
genetic absence of SREBP cleavage-activating protein.";
J. Biol. Chem. 274:28549-28556(1999).
[6]
SUBCELLULAR LOCATION, CLEAVAGE BY MBTPS1, AND MUTAGENESIS OF TYR-298.
TISSUE=Ovary;
PubMed=10500160; DOI=10.1073/pnas.96.20.11235;
Nohturfft A., DeBose-Boyd R.A., Scheek S., Goldstein J.L., Brown M.S.;
"Sterols regulate cycling of SREBP cleavage-activating protein (SCAP)
between endoplasmic reticulum and Golgi.";
Proc. Natl. Acad. Sci. U.S.A. 96:11235-11240(1999).
[7]
SUBCELLULAR LOCATION.
PubMed=10896675; DOI=10.1074/jbc.M005439200;
Yang T., Goldstein J.L., Brown M.S.;
"Overexpression of membrane domain of SCAP prevents sterols from
inhibiting SCAP.SREBP exit from endoplasmic reticulum.";
J. Biol. Chem. 275:29881-29886(2000).
[8]
INTERACTION WITH THE SEC23/SEC24 COMPLEX.
PubMed=12193656; DOI=10.1073/pnas.182412799;
Espenshade P.J., Li W.-P., Yabe D.;
"Sterols block binding of COPII proteins to SCAP, thereby controlling
SCAP sorting in ER.";
Proc. Natl. Acad. Sci. U.S.A. 99:11694-11699(2002).
[9]
SUBUNIT, INTERACTION WITH CHOLESTEROL, AND MUTAGENESIS OF TYR-298.
PubMed=15260976; DOI=10.1016/j.molcel.2004.06.019;
Radhakrishnan A., Sun L.-P., Kwon H.J., Brown M.S., Goldstein J.L.;
"Direct binding of cholesterol to the purified membrane region of
SCAP: mechanism for a sterol-sensing domain.";
Mol. Cell 15:259-268(2004).
[10]
FUNCTION, ER EXPORT SIGNAL, AND MUTAGENESIS OF TYR-298; LEU-449;
445-ARG-ARG-446; 447-MET-GLU-448 AND 451-ASP-LEU-452.
PubMed=15899885; DOI=10.1074/jbc.M504041200;
Sun L.-P., Li L., Goldstein J.L., Brown M.S.;
"Insig required for sterol-mediated inhibition of Scap/SREBP binding
to COPII proteins in vitro.";
J. Biol. Chem. 280:26483-26490(2005).
[11]
FUNCTION, INTERACTION WITH INSIG1 AND INSIG2, AND MUTAGENESIS OF
ASP-428.
PubMed=15728349; DOI=10.1073/pnas.0500206102;
Feramisco J.D., Radhakrishnan A., Ikeda Y., Reitz J., Brown M.S.,
Goldstein J.L.;
"Intramembrane aspartic acid in SCAP protein governs cholesterol-
induced conformational change.";
Proc. Natl. Acad. Sci. U.S.A. 102:3242-3247(2005).
[12]
FUNCTION, AND MUTAGENESIS OF VAL-439; ARG-446; ASN-453;
437-THR-THR-438; 439-VAL-LEU-440; 444-ILE-ARG-445 AND
363-PRO--PRO-492.
PubMed=17428919; DOI=10.1073/pnas.0700907104;
Sun L.-P., Seemann J., Goldstein J.L., Brown M.S.;
"Sterol-regulated transport of SREBPs from endoplasmic reticulum to
Golgi: Insig renders sorting signal in Scap inaccessible to COPII
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 104:6519-6526(2007).
-!- FUNCTION: Escort protein required for cholesterol as well as lipid
homeostasis. Regulates export of the SCAP/SREBF complex from the
ER upon low cholesterol. Formation of a ternary complex with INSIG
at high sterol concentrations leads to masking of an ER-export
signal in SCAP and retention of the complex in the ER. Low sterol
concentrations trigger release of INSIG, a conformational change
in the SSC domain of SCAP, unmasking of the ER export signal,
recruitment into COPII-coated vesicles, transport to the Golgi
complex, proteolytic cleavage of SREBF in the Golgi, release of
the transcription factor fragment of SREBF from the membrane, its
import into the nucleus and up-regulation of LDLR, INSIG1 and the
mevalonate pathway. {ECO:0000269|PubMed:10497220,
ECO:0000269|PubMed:12482938, ECO:0000269|PubMed:15728349,
ECO:0000269|PubMed:15899885, ECO:0000269|PubMed:17428919}.
-!- SUBUNIT: Membrane region forms a homotetramer. Forms a stable
complex with SREBF1/SREBP1 or SREBF2/SREBP2 through its C-terminal
cytoplasmic domain. Forms a ternary complex with INSIG1 or INSIG2
through its transmembrane domains at high sterol concentrations.
Interacts with the SEC23/SEC24 complex in a SAR1-GTP-dependent
manner through an ER export signal in its third cytoplasmic loop.
Binds cholesterol through its SSC domain. 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 with RNF139; the interaction
inhibits the interaction of SCAP with SEC24B and hampering the ER
to Golgi transport of the SCAP/SREBP complex (By similarity).
{ECO:0000250}.
-!- 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.
-!- DOMAIN: Cholesterol bound to SSC domain of SCAP or oxysterol bound
to INSIG1/2 leads to masking of an ER export signal on SCAP
possibly by moving the signal further away from the ER membrane.
-!- DISRUPTION PHENOTYPE: CHO cells show loss of site-1 cleavage of
SREBF1/2, reduced synthesis of cholesterol, a reduced level of
LDLR and cholesterol auxotrophy. {ECO:0000269|PubMed:10497220}.
-!- SIMILARITY: Belongs to the WD repeat SCAP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U67060; AAB19103.1; -; mRNA.
EMBL; AF541996; AAQ11376.1; -; mRNA.
PIR; T18526; T18526.
RefSeq; NP_001230965.1; NM_001244036.1.
ProteinModelPortal; P97260; -.
BioGrid; 1613731; 1.
DIP; DIP-60914N; -.
IntAct; P97260; 2.
TCDB; 2.A.6.6.4; the resistance-nodulation-cell division (rnd) superfamily.
iPTMnet; P97260; -.
GeneID; 100689048; -.
KEGG; cge:100689048; -.
CTD; 22937; -.
HOVERGEN; HBG019538; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0015485; F:cholesterol binding; IEA:InterPro.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0090110; P:cargo loading into COPII-coated vesicle; IDA:UniProtKB.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0032933; P:SREBP signaling pathway; ISS:UniProtKB.
GO; GO:0035105; P:sterol regulatory element binding protein import into nucleus; IMP:UniProtKB.
Gene3D; 2.130.10.10; -; 3.
InterPro; IPR030225; SCAP.
InterPro; IPR000731; SSD.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR10796:SF127; PTHR10796:SF127; 1.
Pfam; PF12349; Sterol-sensing; 1.
Pfam; PF00400; WD40; 1.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 3.
PROSITE; PS50156; SSD; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Cholesterol metabolism; Cytoplasmic vesicle; Endoplasmic reticulum;
Glycoprotein; Golgi apparatus; Lipid metabolism; Membrane;
Methylation; Phosphoprotein; Repeat; Steroid metabolism;
Sterol metabolism; Transmembrane; Transmembrane helix; WD repeat.
CHAIN 1 1276 Sterol regulatory element-binding protein
cleavage-activating protein.
/FTId=PRO_0000051207.
TOPO_DOM 1 18 Cytoplasmic.
{ECO:0000269|PubMed:9642295}.
TRANSMEM 19 39 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 40 279 Lumenal. {ECO:0000269|PubMed:9642295}.
TRANSMEM 280 300 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 301 312 Cytoplasmic.
{ECO:0000269|PubMed:9642295}.
TRANSMEM 313 333 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 334 344 Lumenal. {ECO:0000269|PubMed:9642295}.
TRANSMEM 345 365 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 366 401 Cytoplasmic.
{ECO:0000269|PubMed:9642295}.
TRANSMEM 402 422 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 423 423 Lumenal. {ECO:0000269|PubMed:9642295}.
TRANSMEM 424 444 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 445 518 Cytoplasmic.
{ECO:0000269|PubMed:9642295}.
TRANSMEM 519 539 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 540 708 Lumenal. {ECO:0000269|PubMed:9642295}.
TRANSMEM 709 729 Helical; Name=8. {ECO:0000255}.
TOPO_DOM 730 1276 Cytoplasmic.
{ECO:0000269|PubMed:9642295}.
DOMAIN 284 442 SSD. {ECO:0000255|PROSITE-
ProRule:PRU00199}.
REPEAT 771 811 WD 1.
REPEAT 949 999 WD 2.
REPEAT 1002 1039 WD 3.
REPEAT 1074 1111 WD 4.
REPEAT 1114 1152 WD 5.
REPEAT 1155 1192 WD 6.
REPEAT 1194 1232 WD 7.
REGION 447 452 ER export signal.
REGION 731 1276 Interaction with SREBF2.
{ECO:0000269|PubMed:9488713}.
COMPBIAS 722 729 Poly-Leu.
COMPBIAS 747 750 Poly-Arg.
MOD_RES 821 821 Phosphoserine.
{ECO:0000250|UniProtKB:Q12770}.
MOD_RES 837 837 Phosphoserine.
{ECO:0000250|UniProtKB:Q12770}.
MOD_RES 843 843 Phosphoserine.
{ECO:0000250|UniProtKB:Q6GQT6}.
MOD_RES 850 850 Phosphoserine.
{ECO:0000250|UniProtKB:Q12770}.
MOD_RES 905 905 Phosphoserine.
{ECO:0000250|UniProtKB:Q12770}.
MOD_RES 934 934 Phosphoserine.
{ECO:0000250|UniProtKB:Q12770}.
MOD_RES 1048 1048 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q6GQT6}.
CARBOHYD 263 263 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9642295}.
CARBOHYD 590 590 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9642295}.
CARBOHYD 641 641 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9642295}.
MUTAGEN 298 298 Y->C: Loss of sterol-dependent ER
retention due to loss of interaction with
INSIG. Constitutive interaction with
COPII coat and maturation of SREBF.
{ECO:0000269|PubMed:10500160,
ECO:0000269|PubMed:12482938,
ECO:0000269|PubMed:15260976,
ECO:0000269|PubMed:15899885}.
MUTAGEN 315 315 L->F: Loss of sterol-dependent ER
retention due to loss of interaction with
INSIG. Constitutive maturation of SREBF.
{ECO:0000269|PubMed:12482938}.
MUTAGEN 428 428 D->A,N,K: Loss of release from ER
retention and maturation of SREBF.
Constitutive interaction with INSIG.
{ECO:0000269|PubMed:15728349}.
MUTAGEN 428 428 D->E: Very mild reduction of SREBF
maturation. Slightly higher affinity for
INSIG in the absence of sterols.
{ECO:0000269|PubMed:15728349}.
MUTAGEN 437 438 TT->AA: No effect.
{ECO:0000269|PubMed:17428919}.
MUTAGEN 437 438 Missing: Loss of SREBF maturation and
interaction with COPII coat.
{ECO:0000269|PubMed:17428919}.
MUTAGEN 439 440 Missing: Loss of SREBF maturation.
{ECO:0000269|PubMed:17428919}.
MUTAGEN 439 439 V->VLL: Loss of SREBF maturation.
{ECO:0000269|PubMed:17428919}.
MUTAGEN 443 443 D->N: Loss of sterol-dependent ER
retention due to loss of interaction with
INSIG. {ECO:0000269|PubMed:12482938,
ECO:0000269|PubMed:8898195}.
MUTAGEN 444 445 Missing: Loss of SREBF maturation.
{ECO:0000269|PubMed:17428919}.
MUTAGEN 445 446 RR->AA: No effect.
{ECO:0000269|PubMed:15899885}.
MUTAGEN 446 446 R->RA,RAAAAA,RG,RGG,RGS: Loss of SREBF
maturation.
{ECO:0000269|PubMed:17428919}.
MUTAGEN 446 446 R->RAA: Loss of SREBF maturation and
interaction with COPII coat.
{ECO:0000269|PubMed:17428919}.
MUTAGEN 447 448 ME->AA: Loss of SREBF maturation and
interaction with COPII coat.
{ECO:0000269|PubMed:15899885}.
MUTAGEN 449 449 L->A: Loss of SREBF maturation and
interaction with COPII coat.
{ECO:0000269|PubMed:15899885}.
MUTAGEN 451 452 DL->AA: Loss of SREBF maturation,
interaction with COPII coat and
recruitment into COPII-coated vesicles.
{ECO:0000269|PubMed:15899885}.
MUTAGEN 453 453 N->NAAAAA: No effect.
{ECO:0000269|PubMed:17428919}.
MUTAGEN 463 492 Missing: No effect.
SEQUENCE 1276 AA; 139514 MW; A8693F7157FF5FFC CRC64;
MTLTERLREK ISQAFYNHGL LCASYPIPII LFTGLCILAC CYPLLKLPLP GTGPVEFSTP
VKDYSPPPVD SDHKQGEPSE QPEWYVGAPV AYIQQIFVKS SVSPWHKNLL AVDVFRLPLS
RAFQLVEEIR NHVLRDSSGT KSLEEVCLQV TDLLPGLRKL RNLLPEHGCL LLSPGNFWQN
DWERFHADPD IIGTIHQHEP KTLQTSATLK DLLFGVPGKY SGVSLYTRKR TVSYTITLVF
QRYHAKFLSS LRARLMLLHP SPNCSLRAEN LVHVHFKEEI GIAELIPLVT TYIILFAYIY
FSTRKIDMVK SKWGLALAAV VTVLSSLLMS VGLCTLFGLT PTLNGGEIFP YLVVVIGLEN
VLVLTKSVVS TPVDLEVKLR IAQGLSSESW SIMKNVATEL GIILIGYFTL VPAIQEFCLF
AVVGLVSDFF LQMFFFTTVL SIDIRRMELA DLNKRLPPES CLPSAKPVGR PARYERQLAV
RPAMPHTITL QPSSFRNLRL PKRLRVIYFL ARTRLAQRLI MAGTVVWIGI LVYTDPAGLR
TYLAAQVTEQ SPLGEGSLGP MPVPSGVLPA SRPDPAFSIF PPDAPKLPEN QTVPGELPEH
AAPAEGVHDS RAPEVTWGPE DEELWRRLSF RHWPTLFNYY NITLAKRYIS LLPVIPVTLR
LNPQEALEGR QPQDGRSAWA PPESLPAGLW EAGPKGPGGT QAHGDITLYK VAALGLAAGI
VLVLLLLCLY RVLCPRNYGQ PGGGAGRRRR GELPCDDYGY APPETEIVPL VLRGHLMDIE
CLASDGMLLV SCCLAGQVCV WDAQTGDCLT RIPRPGSRRD SCGGGAFETQ ENWERLSDGG
KTSPEEPGES PPLRHRPRGP PQPALFGDQP DLTCLIDTNF SVQLPPEPTQ PEPRHRAGCG
RARDSGYDFS RLVQRVYQEE GLAAVRMPAL RPPSPGSPLP QASQEDGAAP EKGSPPLAWA
PSTAGSIWSL ELQGNLIVVG RSSGRLEVWD AIEGVLCCSN DEVSSGITAL VFLDRRIVAA
RLNGSLDFFS LETHTSLSPL QFRGTPGRGS SPSSSVYSSS NTVACHLTHT VPCAHQKPIT
ALRAAAGRLV TGSQDHTLRV FRLEDSCCLF TLQGHSGAIT TVYIDQTMVL ASGGQDGAIC
LWDVLTGSRV SHTFAHRGDV TSLTCTTSCV ISSGLDDLIN IWDRSTGIKL YSIQQDLGCG
ASLGVISDNL LVTGGQGCVS FWDLNYGDLL QTVYLGKNSE AQPARQILVL DNAAIVCNFG
SELSLVYVPS VLEKLD


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