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Oxysterol-binding protein-related protein 2 (ORP-2) (OSBP-related protein 2)

 OSBL2_HUMAN             Reviewed;         480 AA.
Q9H1P3; A8K736; Q6IBT0; Q9BZB1; Q9Y4B8;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 141.
RecName: Full=Oxysterol-binding protein-related protein 2;
Short=ORP-2;
Short=OSBP-related protein 2;
Name=OSBPL2; Synonyms=KIAA0772, ORP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
PubMed=11279184; DOI=10.1074/jbc.M101204200;
Xu Y., Liu Y., Ridgway N.D., McMaster C.R.;
"Novel members of the human oxysterol-binding protein family bind
phospholipids and regulate vesicle transport.";
J. Biol. Chem. 276:18407-18414(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=11735225; DOI=10.1006/geno.2001.6663;
Jaworski C.J., Moreira E., Li A., Lee R., Rodriguez I.R.;
"A family of 12 human genes containing oxysterol-binding domains.";
Genomics 78:185-196(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XI.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:277-286(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Rectum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-116 (ISOFORM 1).
PubMed=11483621;
Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C.,
Staels B., Ikonen E., Olkkonen V.M.;
"The OSBP-related protein family in humans.";
J. Lipid Res. 42:1203-1213(2001).
[10]
FUNCTION, AND MUTAGENESIS OF MET-93; PHE-103; LYS-150; PHE-152 AND
ILE-249.
PubMed=17428193; DOI=10.1042/BJ20070176;
Suchanek M., Hynynen R., Wohlfahrt G., Lehto M., Johansson M.,
Saarinen H., Radzikowska A., Thiele C., Olkkonen V.M.;
"The mammalian oxysterol-binding protein-related proteins (ORPs) bind
25-hydroxycholesterol in an evolutionarily conserved pocket.";
Biochem. J. 405:473-480(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
INTERACTION WITH DIAPH1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23325789; DOI=10.1091/mbc.E12-08-0597;
Li D., Dammer E.B., Lucki N.C., Sewer M.B.;
"cAMP-stimulated phosphorylation of diaphanous 1 regulates protein
stability and interaction with binding partners in adrenocortical
cells.";
Mol. Biol. Cell 24:848-857(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-20, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
INVOLVEMENT IN DFNA67.
PubMed=25077649; DOI=10.1038/gim.2014.90;
Xing G., Yao J., Wu B., Liu T., Wei Q., Liu C., Lu Y., Chen Z.,
Zheng H., Yang X., Cao X.;
"Identification of OSBPL2 as a novel candidate gene for progressive
nonsyndromic hearing loss by whole-exome sequencing.";
Genet. Med. 17:210-218(2015).
[16]
INVOLVEMENT IN DFNA67.
PubMed=25759012; DOI=10.1186/s13023-015-0238-5;
Thoenes M., Zimmermann U., Ebermann I., Ptok M., Lewis M.A.,
Thiele H., Morlot S., Hess M.M., Gal A., Eisenberger T., Bergmann C.,
Nuernberg G., Nuernberg P., Steel K.P., Knipper M., Bolz H.J.;
"OSBPL2 encodes a protein of inner and outer hair cell stereocilia and
is mutated in autosomal dominant hearing loss (DFNA67).";
Orphanet J. Rare Dis. 10:15-15(2015).
-!- FUNCTION: Binds phospholipids; exhibits strong binding to
phosphatidic acid and weak binding to phosphatidylinositol 3-
phosphate (PubMed:11279184). Binds 25-hydroxycholesterol
(PubMed:17428193). {ECO:0000269|PubMed:11279184,
ECO:0000269|PubMed:17428193}.
-!- SUBUNIT: Interacts with DIAPH1. {ECO:0000269|PubMed:23325789}.
-!- INTERACTION:
Q9P0L0:VAPA; NbExp=3; IntAct=EBI-2828285, EBI-1059156;
Q53XM7:VAPB; NbExp=3; IntAct=EBI-2828285, EBI-10178947;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H1P3-1; Sequence=Displayed;
Name=2;
IsoId=Q9H1P3-2; Sequence=VSP_003781;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- DISEASE: Deafness, autosomal dominant, 67 (DFNA67) [MIM:616340]: A
form of non-syndromic sensorineural hearing loss. Sensorineural
deafness results from damage to the neural receptors of the inner
ear, the nerve pathways to the brain, or the area of the brain
that receives sound information. {ECO:0000269|PubMed:25077649,
ECO:0000269|PubMed:25759012}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA34492.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AY028168; AAK18044.1; -; mRNA.
EMBL; AF392447; AAL40660.1; -; mRNA.
EMBL; AB018315; BAA34492.2; ALT_INIT; mRNA.
EMBL; AK291851; BAF84540.1; -; mRNA.
EMBL; CR456722; CAG33003.1; -; mRNA.
EMBL; AL354836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW75377.1; -; Genomic_DNA.
EMBL; CH471077; EAW75379.1; -; Genomic_DNA.
EMBL; BC000296; AAH00296.1; -; mRNA.
EMBL; BC004455; AAH04455.1; -; mRNA.
EMBL; AF331963; AAG53416.1; -; mRNA.
CCDS; CCDS13494.1; -. [Q9H1P3-2]
CCDS; CCDS13495.1; -. [Q9H1P3-1]
RefSeq; NP_055650.1; NM_014835.3. [Q9H1P3-2]
RefSeq; NP_653081.1; NM_144498.2. [Q9H1P3-1]
RefSeq; XP_016883654.1; XM_017028165.1. [Q9H1P3-1]
UniGene; Hs.473254; -.
ProteinModelPortal; Q9H1P3; -.
SMR; Q9H1P3; -.
BioGrid; 115216; 12.
ELM; Q9H1P3; -.
IntAct; Q9H1P3; 10.
STRING; 9606.ENSP00000316649; -.
SwissLipids; SLP:000001533; -.
iPTMnet; Q9H1P3; -.
PhosphoSitePlus; Q9H1P3; -.
DMDM; 20139174; -.
EPD; Q9H1P3; -.
MaxQB; Q9H1P3; -.
PaxDb; Q9H1P3; -.
PeptideAtlas; Q9H1P3; -.
PRIDE; Q9H1P3; -.
ProteomicsDB; 80434; -.
ProteomicsDB; 80435; -. [Q9H1P3-2]
DNASU; 9885; -.
Ensembl; ENST00000313733; ENSP00000316649; ENSG00000130703. [Q9H1P3-1]
Ensembl; ENST00000358053; ENSP00000350755; ENSG00000130703. [Q9H1P3-2]
Ensembl; ENST00000643412; ENSP00000494549; ENSG00000130703. [Q9H1P3-1]
Ensembl; ENST00000643981; ENSP00000495379; ENSG00000130703. [Q9H1P3-1]
GeneID; 9885; -.
KEGG; hsa:9885; -.
UCSC; uc002yck.3; human. [Q9H1P3-1]
CTD; 9885; -.
DisGeNET; 9885; -.
EuPathDB; HostDB:ENSG00000130703.15; -.
GeneCards; OSBPL2; -.
HGNC; HGNC:15761; OSBPL2.
HPA; HPA041127; -.
HPA; HPA042659; -.
MalaCards; OSBPL2; -.
MIM; 606731; gene.
MIM; 616340; phenotype.
neXtProt; NX_Q9H1P3; -.
OpenTargets; ENSG00000130703; -.
PharmGKB; PA32827; -.
eggNOG; KOG1737; Eukaryota.
eggNOG; ENOG410XP9E; LUCA.
GeneTree; ENSGT00760000119155; -.
HOGENOM; HOG000231233; -.
HOVERGEN; HBG053374; -.
InParanoid; Q9H1P3; -.
KO; K20174; -.
OMA; FRIICEQ; -.
OrthoDB; EOG091G07RK; -.
PhylomeDB; Q9H1P3; -.
Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
ChiTaRS; OSBPL2; human.
GeneWiki; OSBPL2; -.
GenomeRNAi; 9885; -.
PRO; PR:Q9H1P3; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000130703; Expressed in 226 organ(s), highest expression level in skin of abdomen.
CleanEx; HS_OSBPL2; -.
ExpressionAtlas; Q9H1P3; baseline and differential.
Genevisible; Q9H1P3; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
GO; GO:0015248; F:sterol transporter activity; TAS:Reactome.
GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
InterPro; IPR037239; OSBP_sf.
InterPro; IPR000648; Oxysterol-bd.
InterPro; IPR018494; Oxysterol-bd_CS.
PANTHER; PTHR10972; PTHR10972; 1.
Pfam; PF01237; Oxysterol_BP; 1.
SUPFAM; SSF144000; SSF144000; 2.
PROSITE; PS01013; OSBP; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Deafness; Lipid transport;
Lipid-binding; Non-syndromic deafness; Phosphoprotein;
Reference proteome; Transport.
CHAIN 1 480 Oxysterol-binding protein-related protein
2.
/FTId=PRO_0000100369.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 13 24 Missing (in isoform 2).
{ECO:0000303|PubMed:11279184,
ECO:0000303|PubMed:11735225,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9872452}.
/FTId=VSP_003781.
MUTAGEN 93 93 M->K: Does not significantly impair 25-
hydroxycholesterol binding.
{ECO:0000269|PubMed:17428193}.
MUTAGEN 103 103 F->W: Does not significantly impair 25-
hydroxycholesterol binding.
{ECO:0000269|PubMed:17428193}.
MUTAGEN 150 150 K->A: Reduces 25-hydroxycholesterol
binding. {ECO:0000269|PubMed:17428193}.
MUTAGEN 152 152 F->D: Does not significantly impair 25-
hydroxycholesterol binding.
{ECO:0000269|PubMed:17428193}.
MUTAGEN 249 249 I->W: Reduces 25-hydroxycholesterol
binding. {ECO:0000269|PubMed:17428193}.
SEQUENCE 480 AA; 55201 MW; A93D1B389D0A2740 CRC64;
MNGEEEFFDA VTGFDSDNSS GEFSEANQKV TGMIDLDTSK NNRIGKTGER PSQENGIQKH
RTSLPAPMFS RSDFSVWTIL KKCVGLELSK ITMPIAFNEP LSFLQRITEY MEHVYLIHRA
SCQPQPLERM QSVAAFAVSA VASQWERTGK PFNPLLGETY ELIREDLGFR FISEQVSHHP
PISAFHSEGL NHDFLFHGSI YPKLKFWGKS VEAEPRGTIT LELLKHNEAY TWTNPTCCVH
NVIIGKLWIE QYGTVEILNH RTGHKCVLHF KPCGLFGKEL HKVEGHIQDK NKKKLFMIYG
KWTECLWGID PVSYESFKKQ ERRGDHLRKA KLDEDSGKAD SDVADDVPVA QETVQVIPGS
KLLWRINTRP PNSAQMYNFT SFTVSLNELE TGMEKTLPPT DCRLRPDIRG MENGNMDLAS
QEKERLEEKQ REARRERAKE EAEWQTRWFY PGNNPYTGTP DWLYAGDYFE RNFSDCPDIY


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