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Protein

Sterol regulatory element-binding protein cleavage-activating protein

Gene

Scap

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

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

  • cholesterol binding Source: InterPro
  • protein complex binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

ReactomeiR-RNO-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol regulatory element-binding protein cleavage-activating protein
Short name:
SCAP
Short name:
SREBP cleavage-activating protein
Gene namesi
Name:ScapImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi1309378. Scap.

Subcellular locationi

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

  • Note: Moves from the endoplasmic reticulum to the Golgi in the absence of sterols.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 18CytoplasmicBy similarityAdd BLAST18
Transmembranei19 – 39Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini40 – 279LumenalBy similarityAdd BLAST240
Transmembranei280 – 300Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini301 – 312CytoplasmicBy similarityAdd BLAST12
Transmembranei313 – 333Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini334 – 344LumenalBy similarityAdd BLAST11
Transmembranei345 – 365Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini366 – 401CytoplasmicBy similarityAdd BLAST36
Transmembranei402 – 422Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini423LumenalBy similarity1
Transmembranei424 – 444Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini445 – 518CytoplasmicBy similarityAdd BLAST74
Transmembranei519 – 539Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini540 – 707LumenalBy similarityAdd BLAST168
Transmembranei708 – 728Helical; Name=8Sequence analysisAdd BLAST21
Topological domaini729 – 1276CytoplasmicBy similarityAdd BLAST548

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003158721 – 1276Sterol regulatory element-binding protein cleavage-activating proteinAdd BLAST1276

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi263N-linked (GlcNAc...)Sequence analysis1
Glycosylationi590N-linked (GlcNAc...)Sequence analysis1
Glycosylationi641N-linked (GlcNAc...)Sequence analysis1
Modified residuei821PhosphoserineBy similarity1
Modified residuei837PhosphoserineBy similarity1
Modified residuei843PhosphoserineBy similarity1
Modified residuei850PhosphoserineBy similarity1
Modified residuei905PhosphoserineBy similarity1
Modified residuei934PhosphoserineBy similarity1
Modified residuei1048Omega-N-methylarginineBy similarity1

Keywords - PTMi

Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiA2RRU4.
PeptideAtlasiA2RRU4.
PRIDEiA2RRU4.

PTM databases

iPTMnetiA2RRU4.
PhosphoSitePlusiA2RRU4.

Expressioni

Gene expression databases

BgeeiENSRNOG00000020853.
GenevisibleiA2RRU4. RN.

Interactioni

Subunit structurei

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).By similarity

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028295.

Structurei

3D structure databases

ProteinModelPortaliA2RRU4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini284 – 442SSDPROSITE-ProRule annotationAdd BLAST159
Repeati771 – 811WD 1Sequence analysisAdd BLAST41
Repeati949 – 999WD 2Sequence analysisAdd BLAST51
Repeati1002 – 1039WD 3Sequence analysisAdd BLAST38
Repeati1074 – 1111WD 4Sequence analysisAdd BLAST38
Repeati1114 – 1152WD 5Sequence analysisAdd BLAST39
Repeati1155 – 1192WD 6Sequence analysisAdd BLAST38
Repeati1194 – 1232WD 7Sequence analysisAdd BLAST39

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni447 – 452ER export signalBy similarity6
Regioni731 – 1276Interaction with SREBF2By similarityAdd BLAST546

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the WD repeat SCAP family.Curated
Contains 1 SSD (sterol-sensing) domain.PROSITE-ProRule annotation
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, WD repeat

Phylogenomic databases

eggNOGiKOG1933. Eukaryota.
ENOG410XR54. LUCA.
GeneTreeiENSGT00840000129955.
HOGENOMiHOG000230538.
HOVERGENiHBG019538.
InParanoidiA2RRU4.
OMAiNSEAQPA.
PhylomeDBiA2RRU4.
TreeFamiTF315236.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR030225. SCAP.
IPR000731. SSD.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR10796:SF127. PTHR10796:SF127. 2 hits.
PfamiPF12349. Sterol-sensing. 1 hit.
PF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 3 hits.
PROSITEiPS50156. SSD. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2RRU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLTERLREK ISQAFYNHGL LCASYPIPII LFTGLCILAC CYPLLKLPLP
60 70 80 90 100
GTGPVEFSTP VKGYSPPPAD SDHKQGEPSE QPEWYVGAPV AYIQQIFVKS
110 120 130 140 150
SVSPWHRNLL AVDVFRSPLS RAFQLVEEIR NHVLRDSSGT KSLEEVCLQV
160 170 180 190 200
TDLLPGLRKL RSLLPEHGCL LLSPGNFWQN DWERFHADPD IIGTIHQHEP
210 220 230 240 250
KTLQTSATLK DLLFGVPGKY SGVSLYTRKR MVSYTITLVF QRYHAKFLSS
260 270 280 290 300
LRARLMLLHP SPNCSLRAEN LVHVHFKEEI GIAELIPLVT TYIILFAYIY
310 320 330 340 350
FSTRKIDMVK SKWGLALAAV VTVLSSLLMS VGLCTLFGLT PTLNGGEIFP
360 370 380 390 400
YLVVVIGLEN VLVLTKSVVS TPVDLEVKLR IAQGLSSESW SIMKNVATEL
410 420 430 440 450
GIILIGYFTL VPAIQEFCLF AVVGLVSDFF LQMLFFTTVL SIDIRRMELA
460 470 480 490 500
DLNKRLPPES CLPSAKPVGR PARYERQLAV RPSTPHTITL QPSSFRNLRL
510 520 530 540 550
PKRLRVIYFL ARTRLAQRLI MAGTVVWIGI LVYTDPAGLR TYLAAQVTEQ
560 570 580 590 600
SPLGEGSLGP MPVPSGVLPA SHPDPAFSIF PPDAPKLPEN QTLPGELPEH
610 620 630 640 650
AVPAEGVQDS RAPEVTWGPE DEELWRKLSF RHWPTLFNYY NITLAKRYIS
660 670 680 690 700
LLPVIPVTLH LNPREALEGR HPQDGRTAWA PPEPLPAGLW ETGPKGPGGT
710 720 730 740 750
QTHGDITLYK VAALGLAAGI VLVLLLLCLY RVLCPRNYGQ PGGGAGRRRR
760 770 780 790 800
GELPCDDYGY APPETEIVPL VLRGHLMDIE CLASDGMLLV SCCLAGQVCV
810 820 830 840 850
WDAQTGDCLT RIPRPGPRRD SCGGGAFEAQ ENWERLSDGG KASPEEPGDS
860 870 880 890 900
PPLRRRPRGP PPPSLFGDQP DLTCLIDTNF SVQLPPEPTQ PEPRHRAGCG
910 920 930 940 950
RSRDSGYDFS RLVQRVYQEE GLAAVHMSAL RPPSPGPPLP QASQEEGTAP
960 970 980 990 1000
EKGSPPLAWA PSTAGSIWSL ELQGSLIVVG RSSGRLEVWD AIEGVLCCSN
1010 1020 1030 1040 1050
EEISSGITAL VFLDRRIVAA RLNGSLDFFS LETHTSLSPL QFRGTPGRGS
1060 1070 1080 1090 1100
SPSSPVYSSS NTVACHLTHT VPCAHQKPIT ALRAAAGRLV TGSQDHTLRV
1110 1120 1130 1140 1150
FRLEDSCCLF TLQGHSGAIT TVYIDQTMVL ASGGQDGAIC LWDVLTGSRV
1160 1170 1180 1190 1200
SHTFAHRGDV TSLTCTTSCV ISSGLDDFIN IWDRSTGIKL YSIQQDLGCG
1210 1220 1230 1240 1250
ASLGVISDNL LVTGGQGCVS FWDLNYGDLL QTVYLGKNSE AQPARQILVL
1260 1270
DNAAIVCNFG SELSLVYVPS VLEKLD
Length:1,276
Mass (Da):139,499
Last modified:March 6, 2007 - v1
Checksum:i12278757C1BDA3C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC131852 mRNA. Translation: AAI31853.1.
RefSeqiNP_001094436.1. NM_001100966.1.
XP_006243984.1. XM_006243922.3.
XP_006243985.1. XM_006243923.3.
XP_006243986.1. XM_006243924.3.
XP_006243987.1. XM_006243925.3.
XP_017451085.1. XM_017595596.1.
UniGeneiRn.99548.

Genome annotation databases

EnsembliENSRNOT00000028295; ENSRNOP00000028295; ENSRNOG00000020853.
ENSRNOT00000090238; ENSRNOP00000072003; ENSRNOG00000020853.
GeneIDi301024.
KEGGirno:301024.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC131852 mRNA. Translation: AAI31853.1.
RefSeqiNP_001094436.1. NM_001100966.1.
XP_006243984.1. XM_006243922.3.
XP_006243985.1. XM_006243923.3.
XP_006243986.1. XM_006243924.3.
XP_006243987.1. XM_006243925.3.
XP_017451085.1. XM_017595596.1.
UniGeneiRn.99548.

3D structure databases

ProteinModelPortaliA2RRU4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028295.

PTM databases

iPTMnetiA2RRU4.
PhosphoSitePlusiA2RRU4.

Proteomic databases

PaxDbiA2RRU4.
PeptideAtlasiA2RRU4.
PRIDEiA2RRU4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028295; ENSRNOP00000028295; ENSRNOG00000020853.
ENSRNOT00000090238; ENSRNOP00000072003; ENSRNOG00000020853.
GeneIDi301024.
KEGGirno:301024.

Organism-specific databases

CTDi22937.
RGDi1309378. Scap.

Phylogenomic databases

eggNOGiKOG1933. Eukaryota.
ENOG410XR54. LUCA.
GeneTreeiENSGT00840000129955.
HOGENOMiHOG000230538.
HOVERGENiHBG019538.
InParanoidiA2RRU4.
OMAiNSEAQPA.
PhylomeDBiA2RRU4.
TreeFamiTF315236.

Enzyme and pathway databases

ReactomeiR-RNO-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).

Miscellaneous databases

PROiA2RRU4.

Gene expression databases

BgeeiENSRNOG00000020853.
GenevisibleiA2RRU4. RN.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR030225. SCAP.
IPR000731. SSD.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR10796:SF127. PTHR10796:SF127. 2 hits.
PfamiPF12349. Sterol-sensing. 1 hit.
PF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 3 hits.
PROSITEiPS50156. SSD. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSCAP_RAT
AccessioniPrimary (citable) accession number: A2RRU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: November 30, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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