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Protein

Sterol regulatory element-binding protein cleavage-activating protein

Gene

Scap

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 similarity2 Publications

GO - Molecular functioni

  • cholesterol binding Source: MGI

GO - Biological processi

  • aging Source: Ensembl
  • cholesterol metabolic process Source: MGI
  • regulation of cholesterol biosynthetic process Source: MGI
  • regulation of fatty acid biosynthetic process Source: MGI
  • regulation of fatty acid metabolic process Source: MGI
  • response to hypoxia Source: MGI
  • response to insulin Source: MGI
  • SREBP signaling pathway Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

ReactomeiR-MMU-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
Synonyms:Kiaa0199Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:2135958. 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

Pathology & Biotechi

Disruption phenotypei

Mice lacking Scap in their liver show an 80% reduction in cholesterol and fatty acid synthesis in the liver as well as a lack of regulation of target gene expression in response to cholesterol deprivation or insulin elevation. Mice expressing dominant negative mutant Scap in their liver show higher levels of mature Srebf1 and Srebf2 as well as transcripts encoding proteins involved in uptake and synthesis of cholesterol and fatty acids. They show an 1.6-fold increase in liver size as well as a six-fold increase in cholesterol and a nine-fold increase in triglyceride content of the liver. Their plasma levels of cholesterol and triglycerides are reduced by 50%. They show reduced down-regulation of mature Srebf1/2 when fed a high cholesterol diet.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi443 – 4431D → N: Higher level of processed SREBF1 and SREBF2 when expressed in liver. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12761276Sterol regulatory element-binding protein cleavage-activating proteinPRO_0000315870Add
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 – 8211PhosphoserineCombined sources
Modified residuei843 – 8431PhosphoserineCombined sources
Modified residuei850 – 8501PhosphoserineCombined sources
Modified residuei905 – 9051PhosphoserineBy similarity
Modified residuei934 – 9341PhosphoserineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ6GQT6.
MaxQBiQ6GQT6.
PaxDbiQ6GQT6.
PRIDEiQ6GQT6.

PTM databases

iPTMnetiQ6GQT6.
PhosphoSiteiQ6GQT6.

Expressioni

Gene expression databases

BgeeiQ6GQT6.
CleanExiMM_SCAP.
ExpressionAtlasiQ6GQT6. baseline and differential.
GenevisibleiQ6GQT6. MM.

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

BioGridi231694. 2 interactions.
DIPiDIP-61666N.
STRINGi10090.ENSMUSP00000095953.

Structurei

3D structure databases

ProteinModelPortaliQ6GQT6.
SMRiQ6GQT6. Positions 965-1268.
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.
InParanoidiQ6GQT6.
OMAiNSEAQPA.
OrthoDBiEOG7992PX.
PhylomeDBiQ6GQT6.
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.

Q6GQT6-1 [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 SIMKNAATEL
410 420 430 440 450
GIILIGYFTL VPAIQEFCLF AVVGLVSDFF LQMLFFTTVL SIDIRRMELA
460 470 480 490 500
DLNKRLPPES CLPSAKPVGR PARYERQQAV 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
AGPAEGVHDS RAPEVTWGPE DEELWRKLSF RHWPTLFNYY NITLAKRYIS
660 670 680 690 700
LLPVIPVTLH LNPREALEGR HPQDGRSAWA PQEPLPAGLW ESGPKGPGGT
710 720 730 740 750
QTHGDITLYK VAALGLAAGI VLVLLLLCLY RVLCPRNYGQ PGGGPGRRRR
760 770 780 790 800
GELPCDDYGY APPETEIVPL VLRGHLMDIE CLASDGMLLV SCCLAGQVCV
810 820 830 840 850
WDAQTGDCLT RIPRPGPRRD SCGGGAFETQ ENWERLSDGG KASPEEPGDS
860 870 880 890 900
PPLRRRPRGP PPPSLFGDQP DLTCLIDTNF SVQLPPEPTQ PEPRHRVGCG
910 920 930 940 950
RSRDSGYDFS RLVQRVYQEE GLAAMRMPAL RPPSPGPPLP QASQEEGTAP
960 970 980 990 1000
EKGSPPLAWT PSTAGSIWSL ELQGNLIVVG RSSGRLEVWD AIEGVLCCSN
1010 1020 1030 1040 1050
EEISSGITAL VFLDRRIVAA RLNGSLDFFS LETHTSLSPL QFRGTPGRGS
1060 1070 1080 1090 1100
SPSSSVYSSS NTVTCHRTHT VPCAHQKPIT ALRAAAGRLV TGSQDHTLRV
1110 1120 1130 1140 1150
FRLDDSCCLF TLKGHSGAIT AVYIDQTMVL ASGGQDGAIC LWDVLTGSRV
1160 1170 1180 1190 1200
SQTFAHRGDV TSLTCTASCV ISSGLDDFIS IWDRSTGIKL YSIQQDLGCG
1210 1220 1230 1240 1250
ASLGVISDNL LVTGGQGCVS FWDLNYGDLL QTVYLGKNSE AQPARQILVL
1260 1270
DNAAIVCNFG SELSLVYVPS VLEKLD
Length:1,276
Mass (Da):139,611
Last modified:July 19, 2004 - v1
Checksum:i4EE7DDCEEB6F3331
GO

Sequence cautioni

The sequence BAD32190.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti247 – 2471Missing in BAD32190 (PubMed:15368895).Curated
Sequence conflicti619 – 6191P → L in AAH70437 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK172912 Transcribed RNA. Translation: BAD32190.1. Different initiation.
AK146658 mRNA. Translation: BAE27338.1.
AK150275 mRNA. Translation: BAE29431.1.
AK152478 mRNA. Translation: BAE31252.1.
AK153330 mRNA. Translation: BAE31909.1.
BC051066 mRNA. Translation: AAH51066.1.
BC055472 mRNA. Translation: AAH55472.1.
BC069955 mRNA. Translation: AAH69955.1.
BC070437 mRNA. Translation: AAH70437.1.
BC072633 mRNA. Translation: AAH72633.1.
CCDSiCCDS23564.1.
RefSeqiNP_001001144.2. NM_001001144.3.
NP_001096632.1. NM_001103162.2.
XP_006512146.1. XM_006512083.2.
XP_006512147.1. XM_006512084.2.
XP_006512148.1. XM_006512085.2.
UniGeneiMm.288741.

Genome annotation databases

EnsembliENSMUST00000098350; ENSMUSP00000095953; ENSMUSG00000032485.
GeneIDi235623.
KEGGimmu:235623.
UCSCiuc009rtw.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK172912 Transcribed RNA. Translation: BAD32190.1. Different initiation.
AK146658 mRNA. Translation: BAE27338.1.
AK150275 mRNA. Translation: BAE29431.1.
AK152478 mRNA. Translation: BAE31252.1.
AK153330 mRNA. Translation: BAE31909.1.
BC051066 mRNA. Translation: AAH51066.1.
BC055472 mRNA. Translation: AAH55472.1.
BC069955 mRNA. Translation: AAH69955.1.
BC070437 mRNA. Translation: AAH70437.1.
BC072633 mRNA. Translation: AAH72633.1.
CCDSiCCDS23564.1.
RefSeqiNP_001001144.2. NM_001001144.3.
NP_001096632.1. NM_001103162.2.
XP_006512146.1. XM_006512083.2.
XP_006512147.1. XM_006512084.2.
XP_006512148.1. XM_006512085.2.
UniGeneiMm.288741.

3D structure databases

ProteinModelPortaliQ6GQT6.
SMRiQ6GQT6. Positions 965-1268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231694. 2 interactions.
DIPiDIP-61666N.
STRINGi10090.ENSMUSP00000095953.

PTM databases

iPTMnetiQ6GQT6.
PhosphoSiteiQ6GQT6.

Proteomic databases

EPDiQ6GQT6.
MaxQBiQ6GQT6.
PaxDbiQ6GQT6.
PRIDEiQ6GQT6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098350; ENSMUSP00000095953; ENSMUSG00000032485.
GeneIDi235623.
KEGGimmu:235623.
UCSCiuc009rtw.3. mouse.

Organism-specific databases

CTDi22937.
MGIiMGI:2135958. Scap.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1933. Eukaryota.
ENOG410XR54. LUCA.
GeneTreeiENSGT00840000129955.
HOGENOMiHOG000230538.
HOVERGENiHBG019538.
InParanoidiQ6GQT6.
OMAiNSEAQPA.
OrthoDBiEOG7992PX.
PhylomeDBiQ6GQT6.
TreeFamiTF315236.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiScap. mouse.
PROiQ6GQT6.
SOURCEiSearch...

Gene expression databases

BgeeiQ6GQT6.
CleanExiMM_SCAP.
ExpressionAtlasiQ6GQT6. baseline and differential.
GenevisibleiQ6GQT6. MM.

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

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brainImported.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported.
    Tissue: Embryonic heartImported and MacrophageImported.
  3. "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].
    Strain: C57BL/6JImported and FVB/NImported.
    Tissue: BrainImported, ColonImported and Mammary glandImported.
  4. "Blunted feedback suppression of SREBP processing by dietary cholesterol in transgenic mice expressing sterol-resistant SCAP(D443N)."
    Korn B.S., Shimomura I., Bashmakov Y., Hammer R.E., Horton J.D., Goldstein J.L., Brown M.S.
    J. Clin. Invest. 102:2050-2060(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-443.
  5. "SREBP cleavage-activating protein (SCAP) is required for increased lipid synthesis in liver induced by cholesterol deprivation and insulin elevation."
    Matsuda M., Korn B.S., Hammer R.E., Moon Y.-A., Komuro R., Horton J.D., Goldstein J.L., Brown M.S., Shimomura I.
    Genes Dev. 15:1206-1216(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821 AND SER-934, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821; SER-843 AND SER-850, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiSCAP_MOUSE
AccessioniPrimary (citable) accession number: Q6GQT6
Secondary accession number(s): Q6A0A6
, Q6NS67, Q7TNG7, Q80UI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2004
Last modified: June 8, 2016
This is version 122 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.