GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)

 SCAP_MOUSE              Reviewed;        1276 AA.
Q6GQT6; Q6A0A6; Q6NS67; Q7TNG7; Q80UI6;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 1.
13-FEB-2019, entry version 144.
RecName: Full=Sterol regulatory element-binding protein cleavage-activating protein;
Short=SCAP;
Short=SREBP cleavage-activating protein;
Name=Scap {ECO:0000312|MGI:MGI:2135958};
Synonyms=Kiaa0199 {ECO:0000312|EMBL:BAD32190.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000312|EMBL:BAD32190.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal brain {ECO:0000312|EMBL:BAD32190.1};
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
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.;
"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.";
DNA Res. 11:205-218(2004).
[2] {ECO:0000312|EMBL:BAE27338.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE27338.1};
TISSUE=Embryonic heart {ECO:0000312|EMBL:BAE27338.1}, and
Macrophage {ECO:0000312|EMBL:BAE29431.1};
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3] {ECO:0000312|EMBL:AAH72633.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH72633.1}, and
FVB/N {ECO:0000312|EMBL:AAH55472.1};
TISSUE=Brain {ECO:0000312|EMBL:AAH72633.1},
Colon {ECO:0000312|EMBL:AAH55472.1}, and
Mammary gland {ECO:0000312|EMBL:AAH51066.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4] {ECO:0000305}
FUNCTION, AND MUTAGENESIS OF ASP-443.
PubMed=9854040; DOI=10.1172/JCI5341;
Korn B.S., Shimomura I., Bashmakov Y., Hammer R.E., Horton J.D.,
Goldstein J.L., Brown M.S.;
"Blunted feedback suppression of SREBP processing by dietary
cholesterol in transgenic mice expressing sterol-resistant
SCAP(D443N).";
J. Clin. Invest. 102:2050-2060(1998).
[5] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11358865; DOI=10.1101/gad.891301;
Matsuda M., Korn B.S., Hammer R.E., Moon Y.-A., Komuro R.,
Horton J.D., Goldstein J.L., Brown M.S., Shimomura I.;
"SREBP cleavage-activating protein (SCAP) is required for increased
lipid synthesis in liver induced by cholesterol deprivation and
insulin elevation.";
Genes Dev. 15:1206-1216(2001).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821 AND SER-934, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821; SER-843 AND
SER-850, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1048, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[9]
UBIQUITINATION AT LYS-454 AND LYS-466, AND MUTAGENESIS OF LYS-454 AND
LYS-466.
PubMed=29068315; DOI=10.7554/eLife.28766;
Zhang L., Rajbhandari P., Priest C., Sandhu J., Wu X., Temel R.,
Castrillo A., de Aguiar Vallim T.Q., Sallam T., Tontonoz P.;
"Inhibition of cholesterol biosynthesis through RNF145-dependent
ubiquitination of SCAP.";
Elife 6:0-0(2017).
-!- FUNCTION: 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. {ECO:0000250|UniProtKB:P97260,
ECO:0000269|PubMed:11358865, ECO:0000269|PubMed:9854040}.
-!- SUBUNIT: 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).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P97260}. Golgi apparatus membrane
{ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P97260}. Cytoplasmic vesicle, COPII-coated
vesicle membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P97260}. Note=Moves from
the endoplasmic reticulum to the Golgi in the absence of sterols.
{ECO:0000250|UniProtKB:P97260}.
-!- DOMAIN: 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.
{ECO:0000250|UniProtKB:P97260}.
-!- PTM: Ubiquitinated at Lys-454 and Lys-466. RNF145 triggers
ubiquitination of SCAP, likely inhibiting SCAP:SREBPF2 complex
transport to the Golgi apparatus and the subsequent
processing/maturation of SREBPF2. {ECO:0000269|PubMed:29068315}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:11358865}.
-!- SIMILARITY: Belongs to the WD repeat SCAP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD32190.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AK172912; BAD32190.1; ALT_INIT; Transcribed_RNA.
EMBL; AK146658; BAE27338.1; -; mRNA.
EMBL; AK150275; BAE29431.1; -; mRNA.
EMBL; AK152478; BAE31252.1; -; mRNA.
EMBL; AK153330; BAE31909.1; -; mRNA.
EMBL; BC051066; AAH51066.1; -; mRNA.
EMBL; BC055472; AAH55472.1; -; mRNA.
EMBL; BC069955; AAH69955.1; -; mRNA.
EMBL; BC070437; AAH70437.1; -; mRNA.
EMBL; BC072633; AAH72633.1; -; mRNA.
CCDS; CCDS23564.1; -.
RefSeq; NP_001001144.2; NM_001001144.3.
RefSeq; NP_001096632.1; NM_001103162.2.
RefSeq; XP_006512146.1; XM_006512083.2.
RefSeq; XP_006512147.1; XM_006512084.3.
RefSeq; XP_006512148.1; XM_006512085.3.
UniGene; Mm.288741; -.
ProteinModelPortal; Q6GQT6; -.
SMR; Q6GQT6; -.
BioGrid; 231694; 2.
DIP; DIP-61666N; -.
IntAct; Q6GQT6; 1.
STRING; 10090.ENSMUSP00000095953; -.
iPTMnet; Q6GQT6; -.
PhosphoSitePlus; Q6GQT6; -.
SwissPalm; Q6GQT6; -.
jPOST; Q6GQT6; -.
MaxQB; Q6GQT6; -.
PaxDb; Q6GQT6; -.
PeptideAtlas; Q6GQT6; -.
PRIDE; Q6GQT6; -.
Ensembl; ENSMUST00000098350; ENSMUSP00000095953; ENSMUSG00000032485.
GeneID; 235623; -.
KEGG; mmu:235623; -.
UCSC; uc009rtw.3; mouse.
CTD; 22937; -.
MGI; MGI:2135958; Scap.
eggNOG; KOG1933; Eukaryota.
eggNOG; ENOG410XR54; LUCA.
GeneTree; ENSGT00940000158130; -.
HOGENOM; HOG000230538; -.
HOVERGEN; HBG019538; -.
InParanoid; Q6GQT6; -.
OMA; PIVADKC; -.
OrthoDB; 523786at2759; -.
PhylomeDB; Q6GQT6; -.
TreeFam; TF315236; -.
Reactome; R-MMU-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
ChiTaRS; Scap; mouse.
PRO; PR:Q6GQT6; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032485; Expressed in 272 organ(s), highest expression level in primary oocyte.
ExpressionAtlas; Q6GQT6; baseline and differential.
Genevisible; Q6GQT6; MM.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0015485; F:cholesterol binding; TAS:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0044255; P:cellular lipid metabolic process; IMP:MGI.
GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI.
GO; GO:0006955; P:immune response; IMP:MGI.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IMP:MGI.
GO; GO:0042304; P:regulation of fatty acid biosynthetic process; IMP:MGI.
GO; GO:0019217; P:regulation of fatty acid metabolic process; IDA:MGI.
GO; GO:0001666; P:response to hypoxia; IMP:MGI.
GO; GO:0032868; P:response to insulin; IMP:MGI.
GO; GO:0032933; P:SREBP signaling pathway; ISO:MGI.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR030225; SCAP.
InterPro; IPR000731; SSD.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR10796:SF127; PTHR10796:SF127; 1.
Pfam; PF12349; Sterol-sensing; 1.
Pfam; PF00400; WD40; 1.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50156; SSD; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Cholesterol metabolism; Complete proteome; Cytoplasmic vesicle;
Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Isopeptide bond;
Lipid metabolism; Membrane; Methylation; Phosphoprotein;
Reference proteome; Repeat; Steroid metabolism; Sterol metabolism;
Transmembrane; Transmembrane helix; Ubl conjugation; WD repeat.
CHAIN 1 1276 Sterol regulatory element-binding protein
cleavage-activating protein.
/FTId=PRO_0000315870.
TOPO_DOM 1 18 Cytoplasmic.
{ECO:0000250|UniProtKB:P97260}.
TRANSMEM 19 39 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 40 279 Lumenal. {ECO:0000250|UniProtKB:P97260}.
TRANSMEM 280 300 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 301 312 Cytoplasmic.
{ECO:0000250|UniProtKB:P97260}.
TRANSMEM 313 333 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 334 344 Lumenal. {ECO:0000250|UniProtKB:P97260}.
TRANSMEM 345 365 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 366 401 Cytoplasmic.
{ECO:0000250|UniProtKB:P97260}.
TRANSMEM 402 422 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 423 423 Lumenal. {ECO:0000250|UniProtKB:P97260}.
TRANSMEM 424 444 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 445 518 Cytoplasmic.
{ECO:0000250|UniProtKB:P97260}.
TRANSMEM 519 539 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 540 707 Lumenal. {ECO:0000250|UniProtKB:P97260}.
TRANSMEM 708 728 Helical; Name=8. {ECO:0000255}.
TOPO_DOM 729 1276 Cytoplasmic.
{ECO:0000250|UniProtKB:P97260}.
DOMAIN 284 442 SSD. {ECO:0000255|PROSITE-
ProRule:PRU00199}.
REPEAT 771 811 WD 1. {ECO:0000255}.
REPEAT 949 999 WD 2. {ECO:0000255}.
REPEAT 1002 1039 WD 3. {ECO:0000255}.
REPEAT 1074 1111 WD 4. {ECO:0000255}.
REPEAT 1114 1152 WD 5. {ECO:0000255}.
REPEAT 1155 1192 WD 6. {ECO:0000255}.
REPEAT 1194 1232 WD 7. {ECO:0000255}.
REGION 447 452 ER export signal.
{ECO:0000250|UniProtKB:P97260}.
REGION 731 1276 Interaction with SREBF2.
{ECO:0000250|UniProtKB:P97260}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 837 837 Phosphoserine.
{ECO:0000250|UniProtKB:Q12770}.
MOD_RES 843 843 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 850 850 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 905 905 Phosphoserine.
{ECO:0000250|UniProtKB:Q12770}.
MOD_RES 934 934 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 1048 1048 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
CARBOHYD 263 263 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 590 590 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 641 641 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 454 454 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:29068315}.
CROSSLNK 466 466 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:29068315}.
MUTAGEN 443 443 D->N: Higher level of processed SREBF1
and SREBF2 when expressed in liver.
{ECO:0000269|PubMed:9854040}.
MUTAGEN 454 454 K->R: Loss of ubiquitination; when
associated with R-466.
{ECO:0000269|PubMed:29068315}.
MUTAGEN 466 466 K->R: Loss of ubiquitination; when
associated with R-454.
{ECO:0000269|PubMed:29068315}.
CONFLICT 247 247 Missing (in Ref. 1; BAD32190).
{ECO:0000305}.
CONFLICT 619 619 P -> L (in Ref. 3; AAH70437).
{ECO:0000305}.
SEQUENCE 1276 AA; 139611 MW; 4EE7DDCEEB6F3331 CRC64;
MTLTERLREK ISQAFYNHGL LCASYPIPII LFTGLCILAC CYPLLKLPLP GTGPVEFSTP
VKGYSPPPAD SDHKQGEPSE QPEWYVGAPV AYIQQIFVKS SVSPWHRNLL AVDVFRSPLS
RAFQLVEEIR NHVLRDSSGT KSLEEVCLQV TDLLPGLRKL RSLLPEHGCL LLSPGNFWQN
DWERFHADPD IIGTIHQHEP KTLQTSATLK DLLFGVPGKY SGVSLYTRKR MVSYTITLVF
QRYHAKFLSS LRARLMLLHP SPNCSLRAEN LVHVHFKEEI GIAELIPLVT TYIILFAYIY
FSTRKIDMVK SKWGLALAAV VTVLSSLLMS VGLCTLFGLT PTLNGGEIFP YLVVVIGLEN
VLVLTKSVVS TPVDLEVKLR IAQGLSSESW SIMKNAATEL GIILIGYFTL VPAIQEFCLF
AVVGLVSDFF LQMLFFTTVL SIDIRRMELA DLNKRLPPES CLPSAKPVGR PARYERQQAV
RPSTPHTITL QPSSFRNLRL PKRLRVIYFL ARTRLAQRLI MAGTVVWIGI LVYTDPAGLR
TYLAAQVTEQ SPLGEGSLGP MPVPSGVLPA SHPDPAFSIF PPDAPKLPEN QTLPGELPEH
AGPAEGVHDS RAPEVTWGPE DEELWRKLSF RHWPTLFNYY NITLAKRYIS LLPVIPVTLH
LNPREALEGR HPQDGRSAWA PQEPLPAGLW ESGPKGPGGT QTHGDITLYK VAALGLAAGI
VLVLLLLCLY RVLCPRNYGQ PGGGPGRRRR GELPCDDYGY APPETEIVPL VLRGHLMDIE
CLASDGMLLV SCCLAGQVCV WDAQTGDCLT RIPRPGPRRD SCGGGAFETQ ENWERLSDGG
KASPEEPGDS PPLRRRPRGP PPPSLFGDQP DLTCLIDTNF SVQLPPEPTQ PEPRHRVGCG
RSRDSGYDFS RLVQRVYQEE GLAAMRMPAL RPPSPGPPLP QASQEEGTAP EKGSPPLAWT
PSTAGSIWSL ELQGNLIVVG RSSGRLEVWD AIEGVLCCSN EEISSGITAL VFLDRRIVAA
RLNGSLDFFS LETHTSLSPL QFRGTPGRGS SPSSSVYSSS NTVTCHRTHT VPCAHQKPIT
ALRAAAGRLV TGSQDHTLRV FRLDDSCCLF TLKGHSGAIT AVYIDQTMVL ASGGQDGAIC
LWDVLTGSRV SQTFAHRGDV TSLTCTASCV ISSGLDDFIS IWDRSTGIKL YSIQQDLGCG
ASLGVISDNL LVTGGQGCVS FWDLNYGDLL QTVYLGKNSE AQPARQILVL DNAAIVCNFG
SELSLVYVPS VLEKLD


Related products :

Catalog number Product name Quantity
EIAAB37516 Homo sapiens,Human,KIAA0199,PSEC0227,SCAP,SCAP,SREBP cleavage-activating protein,Sterol regulatory element-binding protein cleavage-activating protein
EIAAB37518 Kiaa0199,Mouse,Mus musculus,SCAP,Scap,SREBP cleavage-activating protein,Sterol regulatory element-binding protein cleavage-activating protein
EIAAB37515 Rat,Rattus norvegicus,SCAP,Scap,SREBP cleavage-activating protein,Sterol regulatory element-binding protein cleavage-activating protein
EIAAB37519 Bos taurus,Bovine,SCAP,SCAP,SREBP cleavage-activating protein,Sterol regulatory element-binding protein cleavage-activating protein
EIAAB37517 Pig,SCAP,SCAP,SREBP cleavage-activating protein,Sterol regulatory element-binding protein cleavage-activating protein,Sus scrofa
H3302 Sterol regulatory element-binding protein cleavage-activating protein (SCAP), Rat, ELISA Kit 96T
H3301 Sterol regulatory element-binding protein cleavage-activating protein (SCAP), Pig, ELISA Kit 96T
CSB-EL020758RA Rat Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit 96T
CSB-EL020758RA Rat Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit SpeciesRat 96T
CSB-EL020758PI Pig Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit SpeciesPig 96T
H3300 Sterol regulatory element-binding protein cleavage-activating protein (SCAP), Mouse, ELISA Kit 96T
H3299 Sterol regulatory element-binding protein cleavage-activating protein (SCAP), Human, ELISA Kit 96T
CSB-EL020758HU Human Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit 96T
CSB-EL020758BO Bovine Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit 96T
H3298 Sterol regulatory element-binding protein cleavage-activating protein (SCAP), Bovine, ELISA Kit 96T
CSB-EL020758MO Mouse Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit 96T
SCAP_RAT ELISA Kit FOR Sterol regulatory element-binding protein cleavage-activating protein; organism: Rat; gene name: Scap 96T
CSB-EL020758BO Bovine Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit SpeciesBovine 96T
CSB-EL020758MO Mouse Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit SpeciesMouse 96T
CSB-EL020758HU Human Sterol regulatory element-binding protein cleavage-activating protein(SCAP) ELISA kit SpeciesHuman 96T
SCAP_MOUSE ELISA Kit FOR Sterol regulatory element-binding protein cleavage-activating protein; organism: Mouse; gene name: Scap 96T
SCAP_PIG Pig ELISA Kit FOR Sterol regulatory element-binding protein cleavage-activating protein 96T
EIAAB39839 ADD1,Adipocyte determination- and differentiation-dependent factor 1,Rat,Rattus norvegicus,Srebf1,Srebp1,SREBP-1,Sterol regulatory element-binding protein 1,Sterol regulatory element-binding transcrip
EIAAB39841 Mouse,Mus musculus,Srebf2,Srebp2,SREBP-2,Sterol regulatory element-binding protein 2,Sterol regulatory element-binding transcription factor 2
EIAAB39837 Mouse,Mus musculus,Srebf1,Srebp1,SREBP-1,Sterol regulatory element-binding protein 1,Sterol regulatory element-binding transcription factor 1

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP731: Sterol regulatory element binding protein related
WP1493: Carbon assimilation C4 pathway
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP1909: Signal regulatory protein (SIRP) family interactions
WP2292: Chemokine signaling pathway
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1502: Mitochondrial biogenesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation

Related Genes :
[SCAP] Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)
[SCAP KIAA0199 PSEC0227] Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)
[Scap Kiaa0199] Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)
[scp1 SPBC3B9.15c] Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)
[Scap] Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)
[SREBF2 SREBP2] Sterol regulatory element-binding protein 2 (SREBP-2) (Sterol regulatory element-binding transcription factor 2) [Cleaved into: Processed sterol regulatory element-binding protein 2]
[Srebf1 Srebp1] Sterol regulatory element-binding protein 1 (SREBP-1) (Sterol regulatory element-binding transcription factor 1) [Cleaved into: Processed sterol regulatory element-binding protein 1]
[SCAP] Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)
[SCAP] Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)
[sre1 SPBC19C2.09] Sterol regulatory element-binding protein 1 [Cleaved into: Processed sterol regulatory element-binding protein 1]
[MBTPS2 S2P] Membrane-bound transcription factor site-2 protease (EC 3.4.24.85) (Endopeptidase S2P) (Sterol regulatory element-binding proteins intramembrane protease) (SREBPs intramembrane protease)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[ATF2 CREB2 CREBP1] Cyclic AMP-dependent transcription factor ATF-2 (cAMP-dependent transcription factor ATF-2) (EC 2.3.1.48) (Activating transcription factor 2) (Cyclic AMP-responsive element-binding protein 2) (CREB-2) (cAMP-responsive element-binding protein 2) (HB16) (Histone acetyltransferase ATF2) (cAMP response element-binding protein CRE-BP1)
[dsc1 SPBC947.10] DSC E3 ubiquitin ligase complex subunit 1 (EC 2.3.2.27) (Defective for SREBP cleavage protein 1) (RING-type E3 ubiquitin transferase DSC1)
[dsc2 ucp14 SPAC1486.02c] DSC E3 ubiquitin ligase complex subunit 2 (EC 2.3.2.27) (Defective for SREBP cleavage protein 2) (RING-type E3 ubiquitin transferase DSC2) (UBA domain-containing protein 14)
[PPBP CTAP3 CXCL7 SCYB7 TGB1 THBGB1] Platelet basic protein (PBP) (C-X-C motif chemokine 7) (Leukocyte-derived growth factor) (LDGF) (Macrophage-derived growth factor) (MDGF) (Small-inducible cytokine B7) [Cleaved into: Connective tissue-activating peptide III (CTAP-III) (LA-PF4) (Low-affinity platelet factor IV); TC-2; Connective tissue-activating peptide III(1-81) (CTAP-III(1-81)); Beta-thromboglobulin (Beta-TG); Neutrophil-activating peptide 2(74) (NAP-2(74)); Neutrophil-activating peptide 2(73) (NAP-2(73)); Neutrophil-activating peptide 2 (NAP-2); TC-1; Neutrophil-activating peptide 2(1-66) (NAP-2(1-66)); Neutrophil-activating peptide 2(1-63) (NAP-2(1-63))]
[HABP2 HGFAL PHBP] Hyaluronan-binding protein 2 (EC 3.4.21.-) (Factor VII-activating protease) (Factor seven-activating protease) (FSAP) (Hepatocyte growth factor activator-like protein) (Plasma hyaluronan-binding protein) [Cleaved into: Hyaluronan-binding protein 2 50 kDa heavy chain; Hyaluronan-binding protein 2 50 kDa heavy chain alternate form; Hyaluronan-binding protein 2 27 kDa light chain; Hyaluronan-binding protein 2 27 kDa light chain alternate form]
[CASP3 CPP32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CREB3 LZIP] Cyclic AMP-responsive element-binding protein 3 (CREB-3) (cAMP-responsive element-binding protein 3) (Leucine zipper protein) (Luman) (Transcription factor LZIP-alpha) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3 (N-terminal Luman) (Transcriptionally active form)]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Kmt2a All1 Hrx Mll Mll1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (IRP) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[RNF139 TRC8] E3 ubiquitin-protein ligase RNF139 (EC 2.3.2.27) (RING finger protein 139) (RING-type E3 ubiquitin transferase RNF139) (Translocation in renal carcinoma on chromosome 8 protein)
[CREB3L3 CREBH HYST1481] Cyclic AMP-responsive element-binding protein 3-like protein 3 (cAMP-responsive element-binding protein 3-like protein 3) (Transcription factor CREB-H) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 3]
[Creb3l1 Oasis] Cyclic AMP-responsive element-binding protein 3-like protein 1 (cAMP-responsive element-binding protein 3-like protein 1) (Old astrocyte specifically-induced substance) (OASIS) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 1 (Oasis N-terminal fragment) (OA-N)]
[PPAF1 PPAF-I] Phenoloxidase-activating factor 1 (EC 3.4.21.-) (Prophenoloxidase-activating factor I) (Serine protease PPAF-1) [Cleaved into: Phenoloxidase-activating factor 1 light chain; Phenoloxidase-activating factor 1 heavy chain]
[PPAF2 PPAF-II] Phenoloxidase-activating factor 2 (45 KDa PPAF) (Hd-45) (Prophenoloxidase-activating factor II) (Serine protease-like PPAF-2) [Cleaved into: Phenoloxidase-activating factor 2 light chain; Phenoloxidase-activating factor 2 heavy chain]
[UBA3 UBE1C] NEDD8-activating enzyme E1 catalytic subunit (EC 6.2.1.-) (NEDD8-activating enzyme E1C) (Ubiquitin-activating enzyme E1C) (Ubiquitin-like modifier-activating enzyme 3) (Ubiquitin-activating enzyme 3)
[CPSF6 CFIM68] Cleavage and polyadenylation specificity factor subunit 6 (Cleavage and polyadenylation specificity factor 68 kDa subunit) (CPSF 68 kDa subunit) (Cleavage factor Im complex 68 kDa subunit) (CFIm68) (Pre-mRNA cleavage factor Im 68 kDa subunit) (Protein HPBRII-4/7)
[ATG7 APG7L] Ubiquitin-like modifier-activating enzyme ATG7 (ATG12-activating enzyme E1 ATG7) (Autophagy-related protein 7) (APG7-like) (hAGP7) (Ubiquitin-activating enzyme E1-like protein)

Bibliography :
[30604228] Aspirin attenuates podocyte injury in diabetic rats through overriding cyclooxygenase-2-mediated dysregulation of LDL receptor pathway.
[30562550] Increased hepatic INSIG-SCAP-SREBP expression is associated with cholesterol metabolism disorder in assisted reproductive technology-conceived aged mice.
[30462530] SCAP knockdown in vascular smooth muscle cells alleviates atherosclerosis plaque formation via up-regulating autophagy in ApoE mice.
[30423569] Mammalian Target of Rapamycin Complex 1 Activation Disrupts the Low-Density Lipoprotein Receptor Pathway: A Novel Mechanism for Extracellular Matrix Accumulation in Human Peritoneal Mesothelial Cells.
[30394316] SREBP-2 aggravates breast cancer associated osteolysis by promoting osteoclastogenesis and breast cancer metastasis.
[29804513] Isoxanthohumol stimulates ubiquitin-proteasome-dependent degradation of precursor forms of sterol regulatory element-binding proteins.
[29788888] SCAP/SREBPs are Central Players in Lipid Metabolism and Novel Metabolic Targets in Cancer Therapy.
[29784041] Lipid metabolism reprogramming and its potential targets in cancer.
[29596892] Dysfunction of cholesterol sensor SCAP promotes inflammation activation in THP-1 macrophages.
[29356579] Insulin Treatment Cannot Promote Lipogenesis in Rat Fetal Lung in Gestational Diabetes Mellitus Because of Failure to Redress the Imbalance Among SREBP-1, SCAP, and INSIG-1.
?>