Scap
entrez
235623
canonical
uniprot
Q6GQT6
canonical
ensembl
ENSMUSG00000032485
resolver
ensp
ENSMUSP00000095953
resolver
ensp
ENSMUSP00000186012
resolver
ensp
ENSMUSP00000186036
resolver
ensp
ENSMUSP00000186042
resolver
enst
ENSMUST00000098350
resolver
genesymbol
Scap
resolver
genesymbol_syn
Kiaa0199
resolver
uniprot
Q6A0A6
resolver
uniprot
Q6NS67
resolver
uniprot
Q7TNG7
resolver
uniprot
Q80UI6
resolver
uniprot_entry
SCAP_MOUSE
resolver
uniprot_sec
Q6A0A6
resolver
uniprot_sec
Q6NS67
resolver
uniprot_sec
Q7TNG7
resolver
uniprot_sec
Q80UI6
resolver
amino_acid_sequence
MTLTERLREKISQAFYNHGLLCASYPIPIILFTGLCILACCYPLLKLPLPGTGPVEFSTPVKGYSPPPADSDHKQGEPSEQPEWYVGAPVAYIQQIFVKSSVSPWHRNLLAVDVFRSPLSRAFQLVEEIRNHVLRDSSGTKSLEEVCLQVTDLLPGLRKLRSLLPEHGCLLLSPGNFWQNDWERFHADPDIIGTIHQHEPKTLQTSATLKDLLFGVPGKYSGVSLYTRKRMVSYTITLVFQRYHAKFLSSLRARLMLLHPSPNCSLRAENLVHVHFKEEIGIAELIPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSSESWSIMKNAATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRMELADLNKRLPPESCLPSAKPVGRPARYERQQAVRPSTPHTITLQPSSFRNLRLPKRLRVIYFLARTRLAQRLIMAGTVVWIGILVYTDPAGLRTYLAAQVTEQSPLGEGSLGPMPVPSGVLPASHPDPAFSIFPPDAPKLPENQTLPGELPEHAGPAEGVHDSRAPEVTWGPEDEELWRKLSFRHWPTLFNYYNITLAKRYISLLPVIPVTLHLNPREALEGRHPQDGRSAWAPQEPLPAGLWESGPKGPGGTQTHGDITLYKVAALGLAAGIVLVLLLLCLYRVLCPRNYGQPGGGPGRRRRGELPCDDYGYAPPETEIVPLVLRGHLMDIECLASDGMLLVSCCLAGQVCVWDAQTGDCLTRIPRPGPRRDSCGGGAFETQENWERLSDGGKASPEEPGDSPPLRRRPRGPPPPSLFGDQPDLTCLIDTNFSVQLPPEPTQPEPRHRVGCGRSRDSGYDFSRLVQRVYQEEGLAAMRMPALRPPSPGPPLPQASQEEGTAPEKGSPPLAWTPSTAGSIWSLELQGNLIVVGRSSGRLEVWDAIEGVLCCSNEEISSGITALVFLDRRIVAARLNGSLDFFSLETHTSLSPLQFRGTPGRGSSPSSSVYSSSNTVTCHRTHTVPCAHQKPITALRAAAGRLVTGSQDHTLRVFRLDDSCCLFTLKGHSGAITAVYIDQTMVLASGGQDGAICLWDVLTGSRVSQTFAHRGDVTSLTCTASCVISSGLDDFISIWDRSTGIKLYSIQQDLGCGASLGVISDNLLVTGGQGCVSFWDLNYGDLLQTVYLGKNSEAQPARQILVLDNAAIVCNFGSELSLVYVPSVLEKLD
uniprot
proteins
function
FUNCTION: Escort protein required for cholesterol as well as lipid homeostasis (PubMed:11358865, PubMed:9854040). Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:11358865, PubMed:29068315, PubMed:9854040). At high sterol concentrations, formation of a ternary complex with INSIG (INSIG1 or INSIG2) leads to mask the ER export signal in SCAP, promoting retention of the complex in the endoplasmic reticulum (By similarity). Low sterol concentrations trigger release of INSIG, a conformational change in the SSD domain of SCAP, unmasking of the ER export signal, promoting recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi: in the Golgi, SREBPs are then processed, releasing the transcription factor fragment of SREBPs from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway (By similarity). Binds cholesterol via its SSD domain (By similarity). {ECO:0000250|UniProtKB:P97260, ECO:0000269|PubMed:11358865, ECO:0000269|PubMed:29068315, ECO:0000269|PubMed:9854040}.
uniprot
proteins
mass_dalton
139611
uniprot
proteins
mutagenesis
MUTAGEN 443; /note="D->N: Higher level of processed SREBF1 and SREBF2 when expressed in liver."; /evidence="ECO:0000269|PubMed:9854040"; MUTAGEN 454; /note="K->R: Loss of ubiquitination; when associated with R-466."; /evidence="ECO:0000269|PubMed:29068315"; MUTAGEN 466; /note="K->R: Loss of ubiquitination; when associated with R-454."; /evidence="ECO:0000269|PubMed:29068315
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated at Lys-454 and Lys-466. RNF145 triggers ubiquitination of SCAP, likely inhibiting SCAP-SREBP complex transport to the Golgi apparatus and the subsequent processing/maturation of SREBF2/SREBP2. {ECO:0000269|PubMed:29068315}.
uniprot
proteins
protein_family
WD repeat SCAP family
uniprot
proteins
pubmed
11358865
uniprot
proteins
pubmed
15368895
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
26311497
uniprot
proteins
pubmed
28849786
uniprot
proteins
pubmed
29068315
uniprot
proteins
pubmed
9854040
uniprot
proteins
sequence_length
1276
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:26311497}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000255}. Note=Moves from the endoplasmic reticulum to the Golgi in the absence of sterols. Requires the presence of SPRING for proper localization to endoplasmic reticulum. {ECO:0000250|UniProtKB:P97260, ECO:0000250|UniProtKB:Q12770}.
uniprot
proteins
transmembrane_region
TRANSMEM 19..39; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 280..300; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 313..333; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 345..365; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 402..422; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 424..444; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 519..539; /note="Helical; Name=7"; /evidence="ECO:0000255"; TRANSMEM 708..728; /note="Helical; Name=8"; /evidence="ECO:0000255
uniprot
proteins