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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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1818CytoplasmicBy similarityAdd
BLAST
Transmembranei19 – 3921Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini40 – 279240LumenalBy similarityAdd
BLAST
Transmembranei280 – 30021Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini301 – 31212CytoplasmicBy similarityAdd
BLAST
Transmembranei313 – 33321Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini334 – 34411LumenalBy similarityAdd
BLAST
Transmembranei345 – 36521Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini366 – 40136CytoplasmicBy similarityAdd
BLAST
Transmembranei402 – 42221Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini423 – 4231LumenalBy similarity
Transmembranei424 – 44421Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini445 – 51874CytoplasmicBy similarityAdd
BLAST
Transmembranei519 – 53921Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini540 – 707168LumenalBy similarityAdd
BLAST
Transmembranei708 – 72821Helical; Name=8Sequence analysisAdd
BLAST
Topological domaini729 – 1276548CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12761276Sterol regulatory element-binding protein cleavage-activating proteinPRO_0000315872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence analysis
Glycosylationi590 – 5901N-linked (GlcNAc...)Sequence analysis
Glycosylationi641 – 6411N-linked (GlcNAc...)Sequence analysis
Modified residuei821 – 8211PhosphoserineBy similarity
Modified residuei843 – 8431PhosphoserineBy similarity
Modified residuei850 – 8501PhosphoserineBy similarity
Modified residuei905 – 9051PhosphoserineBy similarity
Modified residuei934 – 9341PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiA2RRU4.
PRIDEiA2RRU4.

PTM databases

iPTMnetiA2RRU4.

Expressioni

Gene expression databases

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)LengthDescriptionGraphical viewFeature identifierActions
Domaini284 – 442159SSDPROSITE-ProRule annotationAdd
BLAST
Repeati771 – 81141WD 1Sequence analysisAdd
BLAST
Repeati949 – 99951WD 2Sequence analysisAdd
BLAST
Repeati1002 – 103938WD 3Sequence analysisAdd
BLAST
Repeati1074 – 111138WD 4Sequence analysisAdd
BLAST
Repeati1114 – 115239WD 5Sequence analysisAdd
BLAST
Repeati1155 – 119238WD 6Sequence analysisAdd
BLAST
Repeati1194 – 123239WD 7Sequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni447 – 4526ER export signalBy similarity
Regioni731 – 1276546Interaction with SREBF2By similarityAdd
BLAST

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.
OrthoDBiEOG7992PX.
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_006243922.2.
XP_006243985.1. XM_006243923.2.
XP_006243986.1. XM_006243924.2.
XP_006243987.1. XM_006243925.2.
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_006243922.2.
XP_006243985.1. XM_006243923.2.
XP_006243986.1. XM_006243924.2.
XP_006243987.1. XM_006243925.2.
UniGeneiRn.99548.

3D structure databases

ProteinModelPortaliA2RRU4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028295.

PTM databases

iPTMnetiA2RRU4.

Proteomic databases

PaxDbiA2RRU4.
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.
OrthoDBiEOG7992PX.
PhylomeDBiA2RRU4.
TreeFamiTF315236.

Enzyme and pathway databases

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

Miscellaneous databases

PROiA2RRU4.

Gene expression databases

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...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: HeartImported.

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: June 8, 2016
This is version 76 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.