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Protein

Sterol regulatory element-binding protein cleavage-activating protein

Gene

SCAP

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

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:SCAPBy similarity
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

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 – 1278550CytoplasmicBy 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 – 12781278Sterol regulatory element-binding protein cleavage-activating proteinPRO_0000315869Add
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 residuei850 – 8501PhosphoserineBy similarity
Modified residuei905 – 9051PhosphoserineBy similarity
Modified residuei935 – 9351PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiA6QM06.
PRIDEiA6QM06.

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020961.

Structurei

3D structure databases

ProteinModelPortaliA6QM06.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini284 – 442159SSDPROSITE-ProRule annotationAdd
BLAST
Repeati771 – 81141WD 1Sequence analysisAdd
BLAST
Repeati951 – 100151WD 2Sequence analysisAdd
BLAST
Repeati1004 – 104138WD 3Sequence analysisAdd
BLAST
Repeati1076 – 111338WD 4Sequence analysisAdd
BLAST
Repeati1116 – 115439WD 5Sequence analysisAdd
BLAST
Repeati1157 – 119438WD 6Sequence analysisAdd
BLAST
Repeati1196 – 123439WD 7Sequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni447 – 4526ER export signalBy similarity
Regioni731 – 1278548Interaction 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.
HOGENOMiHOG000230538.
HOVERGENiHBG019538.
InParanoidiA6QM06.

Family and domain databases

Gene3Di2.130.10.10. 2 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. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A6QM06-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLTERLREK ISQAFYNHGL FCASYPIPII LFTGLCILAC CYPLLKLPLP
60 70 80 90 100
GTGPVEFTTP VKDYSPPPLT SDHKPGEPNE QPEWYVGAPV AYIQQIFVKS
110 120 130 140 150
SVSPWHKNLL AVDVFRSPLS RAFQLVEEIR NHVLKDSSGT RSLEDVCLQV
160 170 180 190 200
TDLLPGLRKL RNLLPEHGCL LLSPGNFWQN DRERFHADPD IIRTIHQHEP
210 220 230 240 250
KTLQTSATLK DLLFGVPGKY SGVSLYTRKR LVSYTITLVF QHYHAKFLGS
260 270 280 290 300
LRARLMLLHP SPNCSLRAES LVHVHFKEEI GIAELIPLVT TYIILFAYIY
310 320 330 340 350
FSTRKIDMVK SKWGLALAAV VTVLSSLLMS VGLCTLFGLT PTLNGGEIFP
360 370 380 390 400
YLVVVIGLEN VLVLTKSVVS TPVDLEVKLR IAQGLSSESW SIMKNMATEL
410 420 430 440 450
GIVLIGYFTL VPAIQEFCLF AVVGLVSDFF LQMLFFTTVL SIDIRRMELA
460 470 480 490 500
DLNKRLPPEA CLPPAKPVGR PTRFERQPTV RPSMPHTITL QPSSFRNLRL
510 520 530 540 550
PKRLRVIYFL ARTRLAQRLI MAGTVVWIGI LVYTDPAGLR TYLAAQVTEQ
560 570 580 590 600
SPLGEGALAP LPVPSGVLPA SHPDPAFSIF PPDASKLPEN QTLPGEPPEP
610 620 630 640 650
GGLAEGVHDS PAPEVTWGPE DEELWRKLSF RHWPTLFSYY NITLAKRYVS
660 670 680 690 700
LLPVIPVTLR LNPREALEGR HPQDGRSAWP PPRPGQGGLW EAGPKGPGTA
710 720 730 740 750
QAQRDLTLYK VAALGLASGI VLVLLLLCLY RVLCPRNYGQ PGAGPGRRRR
760 770 780 790 800
GELPCDDYGY APPETEIVPL VLRGHLMDIE CLASDGMLLV SCCLAGHVCV
810 820 830 840 850
WDAQTGDCLT RIPHPGQRRD SGVGSGLETQ ETWERLSDGG KGGPEEPGDS
860 870 880 890 900
PPLRHRPRGP PPPALFGDQP DLTCLIDTNF SARPQLPEPA QPEPRYRAGR
910 920 930 940 950
RAQDSAGYDF SRLVQRVYQE GGMAPVHTPA LRPPSPGPTF PLAPEDEAGF
960 970 980 990 1000
PPEKSCPSLA WAPSTDGSIW SLELQGSLIV VGRSSGRLEV WDAIEGTLRC
1010 1020 1030 1040 1050
SSEEVSSGIT ALVFLDRRIV AARLNGSLDF FSLETHTALS PLQFRGAPGR
1060 1070 1080 1090 1100
GSSPASPACS SSDRVACHLT HTVPCAHQKP ITALKAAAGR LVTGSQDHTL
1110 1120 1130 1140 1150
RVFRLEDSCC LFTLQGHSGA ITTVYIDQTM VLASGGQDGA ICLWDVLTGS
1160 1170 1180 1190 1200
RVSHMFAHRG DVTSLTCTTS CVISSGLDDL ISIWDRSTGI KLYSIQQDLG
1210 1220 1230 1240 1250
CGASLGVISD NLLVTGGQGC VSFWDLNYGD LLQTVYLGKN SEAQPARQIL
1260 1270
VLDNAAIVCN FGSELSLVYV PSVLEKLD
Length:1,278
Mass (Da):139,701
Last modified:August 21, 2007 - v1
Checksum:i9C579F7A3E6B5BAA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC148152 mRNA. Translation: AAI48153.1.
RefSeqiNP_001095359.1. NM_001101889.1.
UniGeneiBt.18085.

Genome annotation databases

GeneIDi507878.
KEGGibta:507878.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC148152 mRNA. Translation: AAI48153.1.
RefSeqiNP_001095359.1. NM_001101889.1.
UniGeneiBt.18085.

3D structure databases

ProteinModelPortaliA6QM06.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020961.

Proteomic databases

PaxDbiA6QM06.
PRIDEiA6QM06.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi507878.
KEGGibta:507878.

Organism-specific databases

CTDi22937.

Phylogenomic databases

eggNOGiKOG1933. Eukaryota.
ENOG410XR54. LUCA.
HOGENOMiHOG000230538.
HOVERGENiHBG019538.
InParanoidiA6QM06.

Miscellaneous databases

NextBioi20868256.

Family and domain databases

Gene3Di2.130.10.10. 2 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. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: HerefordImported.
    Tissue: ThymusImported.

Entry informationi

Entry nameiSCAP_BOVIN
AccessioniPrimary (citable) accession number: A6QM06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: January 20, 2016
This is version 62 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.