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Epididymal secretory protein E1 (EPV20) (Niemann Pick type C2 protein homolog)

 NPC2_BOVIN              Reviewed;         149 AA.
P79345; Q3T091; Q58DR4;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
07-NOV-2018, entry version 128.
RecName: Full=NPC intracellular cholesterol transporter 2 {ECO:0000250|UniProtKB:P61916};
AltName: Full=EPV20 {ECO:0000303|PubMed:9030770};
AltName: Full=Epididymal secretory protein E1;
AltName: Full=Niemann Pick type C2 protein homolog;
Flags: Precursor;
Name=NPC2 {ECO:0000250|UniProtKB:P61916};
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND DISULFIDE
BONDS.
TISSUE=Mammary gland;
PubMed=9030770; DOI=10.1111/j.1432-1033.1997.0437a.x;
Larsen L.B., Ravn P., Boisen A., Berglund L., Petersen T.E.;
"Primary structure of EPV20, a secretory glycoprotein containing a
previously uncharacterized type of domain.";
Eur. J. Biochem. 243:437-441(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION.
PubMed=18823126; DOI=10.1021/bi801328u;
Xu Z., Farver W., Kodukula S., Storch J.;
"Regulation of sterol transport between membranes and NPC2.";
Biochemistry 47:11134-11143(2008).
[5]
INTERACTION WITH NPC1.
PubMed=22065762; DOI=10.1073/pnas.1110439108;
Deffieu M.S., Pfeffer S.R.;
"Niemann-Pick type C 1 function requires lumenal domain residues that
mediate cholesterol-dependent NPC2 binding.";
Proc. Natl. Acad. Sci. U.S.A. 108:18932-18936(2011).
[6]
INTERACTION WITH NPC1.
PubMed=27551080; DOI=10.1073/pnas.1611956113;
Li X., Saha P., Li J., Blobel G., Pfeffer S.R.;
"Clues to the mechanism of cholesterol transfer from the structure of
NPC1 middle lumenal domain bound to NPC2.";
Proc. Natl. Acad. Sci. U.S.A. 113:10079-10084(2016).
[7]
FUNCTION.
PubMed=29580834; DOI=10.1016/j.chemphyslip.2018.03.006;
Berzina Z., Solanko L.M., Mehadi A.S., Jensen M.L.V., Lund F.W.,
Modzel M., Szomek M., Solanko K.A., Dupont A., Nielsen G.K.,
Heegaard C.W., Ejsing C.S., Wuestner D.;
"Niemann-Pick C2 protein regulates sterol transport between plasma
membrane and late endosomes in human fibroblasts.";
Chem. Phys. Lipids 213:48-61(2018).
[8] {ECO:0000244|PDB:1NEP}
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 20-149, GLYCOSYLATION AT
ASN-58, AND DISULFIDE BONDS.
PubMed=12591954; DOI=10.1073/pnas.0437840100;
Friedland N., Liou H.L., Lobel P., Stock A.M.;
"Structure of a cholesterol-binding protein deficient in Niemann-Pick
type C2 disease.";
Proc. Natl. Acad. Sci. U.S.A. 100:2512-2517(2003).
[9] {ECO:0000244|PDB:2HKA}
X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 20-149 IN COMPLEX WITH
CHOLESTEROL SULFATE, FUNCTION, GLYCOSYLATION AT ASN-58, AND DISULFIDE
BONDS.
PubMed=17573352; DOI=10.1074/jbc.M703848200;
Xu S., Benoff B., Liou H.L., Lobel P., Stock A.M.;
"Structural basis of sterol binding by NPC2, a lysosomal protein
deficient in Niemann-Pick type C2 disease.";
J. Biol. Chem. 282:23525-23531(2007).
-!- 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:29580834).
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
(By similarity). May bind and mobilize cholesterol that is
associated with membranes (PubMed:18823126). NPC2 binds
cholesterol with a 1:1 stoichiometry (PubMed:17573352). 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 (By
similarity). {ECO:0000250|UniProtKB:P61916,
ECO:0000250|UniProtKB:Q9Z0J0, ECO:0000269|PubMed:17573352,
ECO:0000269|PubMed:18823126, ECO:0000269|PubMed:29580834}.
-!- SUBUNIT: Interacts with NPC1 (via the second lumenal domain) in a
cholestrol-dependent manner (PubMed:22065762, PubMed:27551080).
Interacts with NUS1/NgBR, the interaction stabilizes NCP2 and
regulates cholesterol trafficking. Interacts with DHDDS. Interacts
with NEDD4L (via C2 domain). Interacts with NPC1L1 (By
similarity). {ECO:0000250|UniProtKB:P61916,
ECO:0000269|PubMed:22065762, ECO:0000269|PubMed:27551080}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P61916}.
Endoplasmic reticulum {ECO:0000250|UniProtKB:P61916}. Lysosome
{ECO:0000250|UniProtKB:P61916}. Note=Interaction with cell-surface
M6PR mediates endocytosis and targeting to lysosomes.
{ECO:0000250|UniProtKB:P61916}.
-!- TISSUE SPECIFICITY: Expressed in kidney, spleen, liver and mammary
gland, but not in testis.
-!- DOMAIN: Binds cholesterol in a hydrophobic pocket; there are no
hydrogen bonds between the sterol and the protein.
{ECO:0000269|PubMed:17573352}.
-!- SIMILARITY: Belongs to the NPC2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X85799; CAA59794.1; -; mRNA.
EMBL; BT021533; AAX46380.1; -; mRNA.
EMBL; BC102504; AAI02505.1; -; mRNA.
RefSeq; NP_776343.1; NM_173918.2.
UniGene; Bt.23268; -.
PDB; 1NEP; X-ray; 1.70 A; A=20-149.
PDB; 2HKA; X-ray; 1.81 A; A/B/C=20-149.
PDBsum; 1NEP; -.
PDBsum; 2HKA; -.
ProteinModelPortal; P79345; -.
SMR; P79345; -.
STRING; 9913.ENSBTAP00000029271; -.
SwissLipids; SLP:000000474; -.
PaxDb; P79345; -.
PeptideAtlas; P79345; -.
PRIDE; P79345; -.
Ensembl; ENSBTAT00000029271; ENSBTAP00000029271; ENSBTAG00000021955.
GeneID; 280815; -.
KEGG; bta:280815; -.
CTD; 10577; -.
VGNC; VGNC:32196; NPC2.
eggNOG; KOG4063; Eukaryota.
eggNOG; ENOG4111Q8S; LUCA.
GeneTree; ENSGT00390000006223; -.
HOGENOM; HOG000007181; -.
HOVERGEN; HBG018181; -.
InParanoid; P79345; -.
KO; K13443; -.
OMA; CKSGISC; -.
OrthoDB; EOG091G0W4T; -.
TreeFam; TF317963; -.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Reactome; R-BTA-8964038; LDL clearance.
EvolutionaryTrace; P79345; -.
Proteomes; UP000009136; Chromosome 10.
Bgee; ENSBTAG00000021955; Expressed in 9 organ(s), highest expression level in lung.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
GO; GO:0017127; F:cholesterol transporter activity; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0033344; P:cholesterol efflux; ISS:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0030301; P:cholesterol transport; ISS:UniProtKB.
GO; GO:0032367; P:intracellular cholesterol transport; IDA:UniProtKB.
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.
InterPro; IPR039670; NPC2-like.
PANTHER; PTHR11306; PTHR11306; 1.
Pfam; PF02221; E1_DerP2_DerF2; 1.
SMART; SM00737; ML; 1.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cholesterol metabolism; Complete proteome;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Lipid metabolism; Lipid transport; Lysosome;
Reference proteome; Secreted; Signal; Steroid metabolism;
Sterol metabolism; Transport.
SIGNAL 1 19
CHAIN 20 149 NPC intracellular cholesterol transporter
2.
/FTId=PRO_0000019852.
MOD_RES 116 116 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z0J0}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1NEP,
ECO:0000244|PDB:2HKA,
ECO:0000269|PubMed:12591954,
ECO:0000269|PubMed:17573352}.
DISULFID 27 140 {ECO:0000244|PDB:1NEP,
ECO:0000244|PDB:2HKA,
ECO:0000269|PubMed:12591954,
ECO:0000269|PubMed:17573352,
ECO:0000269|PubMed:9030770}.
DISULFID 42 47 {ECO:0000244|PDB:1NEP,
ECO:0000244|PDB:2HKA,
ECO:0000269|PubMed:12591954,
ECO:0000269|PubMed:17573352,
ECO:0000269|PubMed:9030770}.
DISULFID 93 99 {ECO:0000244|PDB:1NEP,
ECO:0000244|PDB:2HKA,
ECO:0000269|PubMed:12591954,
ECO:0000269|PubMed:17573352,
ECO:0000269|PubMed:9030770}.
STRAND 25 27 {ECO:0000244|PDB:1NEP}.
STRAND 31 41 {ECO:0000244|PDB:1NEP}.
STRAND 43 50 {ECO:0000244|PDB:1NEP}.
STRAND 54 65 {ECO:0000244|PDB:1NEP}.
STRAND 71 78 {ECO:0000244|PDB:1NEP}.
STRAND 81 84 {ECO:0000244|PDB:1NEP}.
HELIX 92 94 {ECO:0000244|PDB:1NEP}.
STRAND 99 101 {ECO:0000244|PDB:1NEP}.
STRAND 106 114 {ECO:0000244|PDB:1NEP}.
STRAND 121 131 {ECO:0000244|PDB:1NEP}.
STRAND 137 148 {ECO:0000244|PDB:1NEP}.
SEQUENCE 149 AA; 16640 MW; 91156DC7E805B655 CRC64;
MRFLTVAFLF LALSASALAE PVKFKDCGSW VGVIKEVNVS PCPTQPCKLH RGQSYSVNVT
FTSNTQSQSS KAVVHGIVMG IPVPFPIPES DGCKSGIRCP IEKDKTYNYV NKLPVKNEYP
SIKVVVEWEL TDDKNQRFFC WQIPIEVEA


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