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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.
12-SEP-2018, entry version 137.
RecName: Full=NPC intracellular cholesterol transporter 2 {ECO:0000312|MGI:MGI:1915213};
AltName: Full=Epididymal secretory protein E1;
Short=mE1 {ECO:0000303|PubMed:10863096};
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], SUBCELLULAR LOCATION, GLYCOSYLATION, AND
TISSUE SPECIFICITY.
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]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-51; PHE-85;
ASP-91; LYS-94; VAL-115 AND TYR-119.
PubMed=12591949; DOI=10.1073/pnas.0530027100;
Ko D.C., Binkley J., Sidow A., Scott M.P.;
"The integrity of a cholesterol-binding pocket in Niemann-Pick C2
protein is necessary to control lysosome cholesterol levels.";
Proc. Natl. Acad. Sci. U.S.A. 100:2518-2525(2003).
[5]
FUNCTION.
PubMed=17018531; DOI=10.1074/jbc.M608743200;
Liou H.L., Dixit S.S., Xu S., Tint G.S., Stock A.M., Lobel P.;
"NPC2, the protein deficient in Niemann-Pick C2 disease, consists of
multiple glycoforms that bind a variety of sterols.";
J. Biol. Chem. 281:36710-36723(2006).
[6]
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).
[7]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASP-91 AND VAL-115.
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).
[8]
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).
[9]
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).
[10]
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).
[11]
FUNCTION, AND MUTAGENESIS OF GLN-48; HIS-50; LYS-51; ASN-58; ILE-81;
VAL-83; ASP-91; LYS-94; ASP-104; GLU-127; ASP-132 AND LYS-134.
PubMed=26296895; DOI=10.1074/jbc.M115.667469;
McCauliff L.A., Xu Z., Li R., Kodukula S., Ko D.C., Scott M.P.,
Kahn P.C., Storch J.;
"Multiple Surface Regions on the Niemann-Pick C2 Protein Facilitate
Intracellular Cholesterol Transport.";
J. Biol. Chem. 290:27321-27331(2015).
-!- FUNCTION: Intracellular cholesterol transporter which acts in
concert with NPC1 and plays an important role in the egress of
cholesterol from the lysosomal compartment (PubMed:12591949,
PubMed:17018531, PubMed:21315718, PubMed:26296895). Unesterified
cholesterol that has been released from LDLs in the lumen of the
late endosomes/lysosomes is transferred by NPC2 to the
cholesterol-binding pocket in the N-terminal domain of NPC1. May
bind and mobilize cholesterol that is associated with membranes.
NPC2 binds cholesterol with a 1:1 stoichiometry. Can bind a
variety of sterols, including lathosterol, desmosterol and the
plant sterols stigmasterol and beta-sitosterol (By similarity).
The secreted form of NCP2 regulates biliary cholesterol secretion
via stimulation of ABCG5/ABCG8-mediated cholesterol transport
(PubMed:21315718). {ECO:0000250|UniProtKB:P61916,
ECO:0000269|PubMed:12591949, ECO:0000269|PubMed:17018531,
ECO:0000269|PubMed:21315718, ECO:0000269|PubMed:26296895}.
-!- SUBUNIT: Interacts with NPC1 (via the second lumenal domain) in a
cholestrol-dependent manner. Interacts with NUS1/NgBR, the
interaction stabilizes NCP2 and regulates cholesterol trafficking.
Interacts with DHDDS. Interacts with NEDD4L (via C2 domain).
Interacts with NPC1L1. {ECO:0000250|UniProtKB:P61916}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10863096,
ECO:0000269|PubMed:12591949, ECO:0000269|PubMed:21315718}.
Endoplasmic reticulum {ECO:0000250|UniProtKB:P61916}. Lysosome
{ECO:0000250|UniProtKB:P61916}. Note=Interaction with cell-surface
M6PR mediates endocytosis and targeting to lysosomes.
{ECO:0000305|PubMed:12591949}.
-!- TISSUE SPECIFICITY: Detected in liver and bile (PubMed:21315718).
Detected in epididymis (at protein level). Detected in caput
epididymis, corpus epididymis, cauda epididymis and ovary
(PubMed:10863096). {ECO:0000269|PubMed:10863096,
ECO:0000269|PubMed:21315718}.
-!- DOMAIN: Binds cholesterol in a hydrophobic pocket; there are no
hydrogen bonds between the sterol and the protein.
{ECO:0000250|UniProtKB:P79345}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:10863096}.
-!- SIMILARITY: Belongs to the NPC2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) 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; Expressed in 305 organ(s), highest expression level in right lung.
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;
Lipid transport; Lysosome; Reference proteome; Secreted; Signal;
Steroid metabolism; Sterol metabolism; Transport.
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|UniProtKB:P61916}.
DISULFID 42 47 {ECO:0000250|UniProtKB:P61916}.
DISULFID 93 99 {ECO:0000250|UniProtKB:P61916}.
MUTAGEN 48 48 Q->A: Strongly decreased cholesterol
export. {ECO:0000269|PubMed:26296895}.
MUTAGEN 50 50 H->A: Strongly decreased cholesterol
export. {ECO:0000269|PubMed:26296895}.
MUTAGEN 51 51 K->A: Decreased cholesterol binding.
Strongly decreased cholesterol transport
activity. {ECO:0000269|PubMed:12591949,
ECO:0000269|PubMed:26296895}.
MUTAGEN 58 58 N->A: Decreased cholesterol binding.
Strongly decreased cholesterol transport
activity. {ECO:0000269|PubMed:26296895}.
MUTAGEN 81 81 I->D: No effect on cholesterol binding.
Strongly decreased cholesterol transport
activity. {ECO:0000269|PubMed:26296895}.
MUTAGEN 83 83 V->A: No effect on cholesterol binding.
Strongly decreased cholesterol transport
activity. {ECO:0000269|PubMed:26296895}.
MUTAGEN 85 85 F->A: Loss of cholesterol binding.
Abolishes cholesterol transport activity.
{ECO:0000269|PubMed:12591949}.
MUTAGEN 91 91 D->A: Decreased cholesterol binding.
Nearly abolishes cholesterol transport
activity. {ECO:0000269|PubMed:12591949,
ECO:0000269|PubMed:26296895}.
MUTAGEN 91 91 D->A: No significant effect on biliary
cholesterol secretion.
{ECO:0000269|PubMed:21315718}.
MUTAGEN 94 94 K->A: Decreased cholesterol binding.
Nearly abolishes cholesterol transport
activity. {ECO:0000269|PubMed:12591949,
ECO:0000269|PubMed:26296895}.
MUTAGEN 104 104 D->A: Decreased cholesterol binding.
Strongly decreased cholesterol transport
activity. {ECO:0000269|PubMed:26296895}.
MUTAGEN 115 115 V->F: Loss of cholesterol binding.
Abolishes cholesterol transport activity.
Abolishes stimulation of biliary
cholesterol secretion.
{ECO:0000269|PubMed:12591949,
ECO:0000269|PubMed:21315718}.
MUTAGEN 119 119 Y->A: Loss of cholesterol binding.
Abolishes cholesterol transport activity.
{ECO:0000269|PubMed:12591949}.
MUTAGEN 127 127 E->A: Strongly decreased cholesterol
export. {ECO:0000269|PubMed:26296895}.
MUTAGEN 132 132 D->A: No effect on cholesterol binding.
Strongly decreased cholesterol transport
activity. {ECO:0000269|PubMed:26296895}.
MUTAGEN 134 134 K->A: No effect on cholesterol binding.
Strongly decreased cholesterol transport
activity. {ECO:0000269|PubMed:26296895}.
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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