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Epididymal secretory protein E1 (mE1) (Niemann Pick type C2 protein homolog)

 NPC2_MOUSE              Reviewed;         149 AA.
Q9Z0J0; Q3UB23;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
23-MAY-2018, entry version 136.
RecName: Full=NPC intracellular cholesterol transporter 2 {ECO:0000312|MGI:MGI:1915213};
AltName: Full=Epididymal secretory protein E1;
Short=mE1;
AltName: Full=Niemann Pick type C2 protein homolog;
Flags: Precursor;
Name=Npc2 {ECO:0000312|MGI:MGI:1915213};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo;
PubMed=10863096; DOI=10.1016/S0378-1119(00)00189-X;
Nakamura Y., Takayama N., Minamitani T., Ikuta T., Ariga H.,
Matsumoto K.;
"Primary structure, genomic organization and expression of the major
secretory protein of murine epididymis, ME1.";
Gene 251:55-62(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=BALB/cJ, C57BL/6J, and NOD;
TISSUE=Bone marrow, Small intestine, Spleen, Tongue, and
Visual cortex;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
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).
[5]
FUNCTION.
PubMed=21315718; DOI=10.1053/j.gastro.2011.01.050;
Yamanashi Y., Takada T., Yoshikado T., Shoda J., Suzuki H.;
"NPC2 regulates biliary cholesterol secretion via stimulation of
ABCG5/G8-mediated cholesterol transport.";
Gastroenterology 140:1664-1674(2011).
[6]
REVIEW ON FUNCTION.
PubMed=19232397; DOI=10.1016/j.bbalip.2009.02.001;
Storch J., Xu Z.;
"Niemann-Pick C2 (NPC2) and intracellular cholesterol trafficking.";
Biochim. Biophys. Acta 1791:671-678(2009).
[7]
REVIEW ON FUNCTION.
PubMed=21412152; DOI=10.1097/MOL.0b013e3283453e69;
Vance J.E., Peake K.B.;
"Function of the Niemann-Pick type C proteins and their bypass by
cyclodextrin.";
Curr. Opin. Lipidol. 22:204-209(2011).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Intracellular cholesterol transporter which acts in
concert with NPC1 and plays an important role in the egress of
cholesterol from the endosomal/lysosomal compartment. Both NPC1
and NPC2 function as the cellular 'tag team duo' (TTD) to catalyze
the mobilization of cholesterol within the multivesicular
environment of the late endosome (LE) to effect egress through the
limiting bilayer of the LE. NPC2 binds unesterified cholesterol
that has been released from LDLs in the lumen of the late
endosomes/lysosomes and transfers it to the cholesterol-binding
pocket of the N-terminal domain of NPC1. Cholesterol binds to NPC1
with the hydroxyl group buried in the binding pocket and is
exported from the limiting membrane of late endosomes/ lysosomes
to the ER and plasma membrane by an unknown mechanism. The
secreted form of NCP2 regulates biliary cholesterol secretion via
stimulation of ABCG5/ABCG8-mediated cholesterol transport.
{ECO:0000269|PubMed:21315718}.
-!- SUBUNIT: Interacts with NUS1/NgBR, the interaction stabilizes NCP2
and regulates cholesterol trafficking. Interacts with DHDDS (By
similarity). Interacts with NEDD4L (via C2 domain) (By
similarity). Interacts with NPC1L1 (By similarity). Interacts with
NPC1 (via the second lumenal domain) in a cholestrol-dependent
manner (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted. Endoplasmic reticulum
{ECO:0000250}. Lysosome {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in epididymis.
-!- PTM: N-glycosylated.
-!- SIMILARITY: Belongs to the NPC2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB021289; BAA35183.1; -; mRNA.
EMBL; AK008603; BAB25771.1; -; mRNA.
EMBL; AK009127; BAB26090.1; -; mRNA.
EMBL; AK151067; BAE30083.1; -; mRNA.
EMBL; AK151133; BAE30141.1; -; mRNA.
EMBL; AK153020; BAE31654.1; -; mRNA.
EMBL; AK153203; BAE31803.1; -; mRNA.
EMBL; AK158624; BAE34585.1; -; mRNA.
EMBL; AK165263; BAE38111.1; -; mRNA.
EMBL; AK167869; BAE39885.1; -; mRNA.
EMBL; AK170327; BAE41721.1; -; mRNA.
EMBL; BC003471; AAH03471.1; -; mRNA.
EMBL; BC007190; AAH07190.1; -; mRNA.
CCDS; CCDS26050.1; -.
RefSeq; NP_075898.1; NM_023409.4.
UniGene; Mm.282556; -.
ProteinModelPortal; Q9Z0J0; -.
SMR; Q9Z0J0; -.
IntAct; Q9Z0J0; 1.
MINT; Q9Z0J0; -.
STRING; 10090.ENSMUSP00000021668; -.
SwissLipids; SLP:000000473; -.
iPTMnet; Q9Z0J0; -.
PhosphoSitePlus; Q9Z0J0; -.
SwissPalm; Q9Z0J0; -.
EPD; Q9Z0J0; -.
MaxQB; Q9Z0J0; -.
PaxDb; Q9Z0J0; -.
PeptideAtlas; Q9Z0J0; -.
PRIDE; Q9Z0J0; -.
Ensembl; ENSMUST00000021668; ENSMUSP00000021668; ENSMUSG00000021242.
GeneID; 67963; -.
KEGG; mmu:67963; -.
UCSC; uc007oft.1; mouse.
CTD; 10577; -.
MGI; MGI:1915213; Npc2.
eggNOG; KOG4063; Eukaryota.
eggNOG; ENOG4111Q8S; LUCA.
GeneTree; ENSGT00390000006223; -.
HOGENOM; HOG000007181; -.
HOVERGEN; HBG018181; -.
InParanoid; Q9Z0J0; -.
KO; K13443; -.
OMA; CKSGISC; -.
OrthoDB; EOG091G0W4T; -.
PhylomeDB; Q9Z0J0; -.
TreeFam; TF317963; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-8964038; LDL clearance.
ChiTaRS; Npc2; mouse.
PRO; PR:Q9Z0J0; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000021242; -.
CleanEx; MM_NPC2; -.
Genevisible; Q9Z0J0; MM.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005764; C:lysosome; ISS:HGNC.
GO; GO:0015485; F:cholesterol binding; IMP:UniProtKB.
GO; GO:0017127; F:cholesterol transporter activity; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0033344; P:cholesterol efflux; IMP:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; ISS:HGNC.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0030301; P:cholesterol transport; IMP:UniProtKB.
GO; GO:0032367; P:intracellular cholesterol transport; IMP:HGNC.
GO; GO:0032366; P:intracellular sterol transport; ISS:HGNC.
GO; GO:0009615; P:response to virus; IEA:Ensembl.
CDD; cd00916; Npc2_like; 1.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR003172; ML_dom.
InterPro; IPR033916; ML_Npc2-like.
Pfam; PF02221; E1_DerP2_DerF2; 1.
SMART; SM00737; ML; 1.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
Acetylation; Cholesterol metabolism; Complete proteome;
Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lipid metabolism;
Lysosome; Reference proteome; Secreted; Signal; Steroid metabolism;
Sterol metabolism.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 149 NPC intracellular cholesterol transporter
2.
/FTId=PRO_0000019856.
MOD_RES 116 116 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 27 140 {ECO:0000250}.
DISULFID 42 47 {ECO:0000250}.
DISULFID 93 99 {ECO:0000250}.
SEQUENCE 149 AA; 16442 MW; 6BDE56CF69791805 CRC64;
MRFLAATILL LALVAASQAE PLHFKDCGSK VGVIKEVNVS PCPTDPCQLH KGQSYSVNIT
FTSGTQSQNS TALVHGILEG IRVPFPIPEP DGCKSGINCP IQKDKVYSYL NKLPVKNEYP
SIKLVVEWKL EDDKKNNLFC WEIPVQITS


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