OSBL5_HUMAN
ID OSBL5_HUMAN Reviewed; 879 AA.
AC Q9H0X9; A6NDP0; A6NJS8; B4DVB0; Q54A90; Q8N596; Q9BZB0; Q9P1Z4;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Oxysterol-binding protein-related protein 5;
DE Short=ORP-5;
DE Short=OSBP-related protein 5;
DE AltName: Full=Oxysterol-binding protein homolog 1 {ECO:0000303|PubMed:12504849};
GN Name=OSBPL5; Synonyms=KIAA1534, OBPH1 {ECO:0000303|PubMed:12504849}, ORP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IMPRINTING, AND TISSUE SPECIFICITY.
RX PubMed=12504849; DOI=10.1006/geno.2002.7006;
RA Higashimoto K., Soejima H., Yatsuki H., Joh K., Uchiyama M., Obata Y.,
RA Ono R., Wang Y., Xin Z., Zhu X., Masuko S., Ishino F., Hatada I., Jinno Y.,
RA Iwasaka T., Katsuki T., Mukai T.;
RT "Characterization and imprinting status of OBPH1/Obph1 gene: implications
RT for an extended imprinting domain in human and mouse.";
RL Genomics 80:575-584(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11735225; DOI=10.1006/geno.2001.6663;
RA Jaworski C.J., Moreira E., Li A., Lee R., Rodriguez I.R.;
RT "A family of 12 human genes containing oxysterol-binding domains.";
RL Genomics 78:185-196(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Anniss A.M., Apostolopoulos J., Sparrow R.L.;
RT "Isolation and characterization of human oxysterol-binding protein-related
RT protein-5 (ORP-5).";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Small intestine, and Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-61 (ISOFORM 1).
RX PubMed=11483621;
RA Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C., Staels B.,
RA Ikonen E., Olkkonen V.M.;
RT "The OSBP-related protein family in humans.";
RL J. Lipid Res. 42:1203-1213(2001).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-879 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [11]
RP FUNCTION.
RX PubMed=17428193; DOI=10.1042/bj20070176;
RA Suchanek M., Hynynen R., Wohlfahrt G., Lehto M., Johansson M., Saarinen H.,
RA Radzikowska A., Thiele C., Olkkonen V.M.;
RT "The mammalian oxysterol-binding protein-related proteins (ORPs) bind 25-
RT hydroxycholesterol in an evolutionarily conserved pocket.";
RL Biochem. J. 405:473-480(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP LACK OF IMPRINTING.
RX PubMed=20644730; DOI=10.1371/journal.pone.0011595;
RA Frost J.M., Udayashankar R., Moore H.D., Moore G.E.;
RT "Telomeric NAP1L4 and OSBPL5 of the KCNQ1 cluster, and the DECORIN gene are
RT not imprinted in human trophoblast stem cells.";
RL PLoS ONE 5:E11595-E11595(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21220512; DOI=10.1083/jcb.201004142;
RA Du X., Kumar J., Ferguson C., Schulz T.A., Ong Y.S., Hong W., Prinz W.A.,
RA Parton R.G., Brown A.J., Yang H.;
RT "A role for oxysterol-binding protein-related protein 5 in endosomal
RT cholesterol trafficking.";
RL J. Cell Biol. 192:121-135(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP FUNCTION.
RX PubMed=23934110; DOI=10.1038/nature12430;
RA Maeda K., Anand K., Chiapparino A., Kumar A., Poletto M., Kaksonen M.,
RA Gavin A.C.;
RT "Interactome map uncovers phosphatidylserine transport by oxysterol-binding
RT proteins.";
RL Nature 501:257-261(2013).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-389 AND
RP 478-HIS-HIS-479.
RX PubMed=26206935; DOI=10.1126/science.aab1370;
RA Chung J., Torta F., Masai K., Lucast L., Czapla H., Tanner L.B.,
RA Narayanaswamy P., Wenk M.R., Nakatsu F., De Camilli P.;
RT "PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER-
RT plasma membrane contacts.";
RL Science 349:428-432(2015).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=30220461; DOI=10.1016/j.cell.2018.08.033;
RA Sandhu J., Li S., Fairall L., Pfisterer S.G., Gurnett J.E., Xiao X.,
RA Weston T.A., Vashi D., Ferrari A., Orozco J.L., Hartman C.L.,
RA Strugatsky D., Lee S.D., He C., Hong C., Jiang H., Bentolila L.A.,
RA Gatta A.T., Levine T.P., Ferng A., Lee R., Ford D.A., Young S.G.,
RA Ikonen E., Schwabe J.W.R., Tontonoz P.;
RT "Aster proteins facilitate nonvesicular plasma membrane to ER cholesterol
RT transport in mammalian cells.";
RL Cell 175:514-529(2018).
CC -!- FUNCTION: Lipid transporter involved in lipid countertransport between
CC the endoplasmic reticulum and the plasma membrane: specifically
CC exchanges phosphatidylserine with phosphatidylinositol 4-phosphate
CC (PI4P), delivering phosphatidylserine to the plasma membrane in
CC exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in
CC the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a
CC mutually exclusive manner (PubMed:23934110, PubMed:26206935). May
CC cooperate with NPC1 to mediate the exit of cholesterol from
CC endosomes/lysosomes (PubMed:21220512). Binds 25-hydroxycholesterol and
CC cholesterol (PubMed:17428193). {ECO:0000269|PubMed:17428193,
CC ECO:0000269|PubMed:21220512, ECO:0000269|PubMed:23934110,
CC ECO:0000269|PubMed:26206935}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21220512, ECO:0000269|PubMed:26206935}; Single-pass
CC membrane protein {ECO:0000269|PubMed:21220512}. Note=Localizes to
CC endoplasmic reticulum-plasma membrane contact sites (EPCS). Localizes
CC to the cortical endoplasmic reticulum at the EPCS.
CC {ECO:0000269|PubMed:26206935, ECO:0000269|PubMed:30220461}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H0X9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0X9-2; Sequence=VSP_043071;
CC Name=3;
CC IsoId=Q9H0X9-3; Sequence=VSP_057408, VSP_057409;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12504849, ECO:0000269|PubMed:21220512}.
CC -!- MISCELLANEOUS: According to a report, the gene is imprinted in
CC placenta, where it is predominantly expressed from the maternal allele
CC only. Not imprinted in other tissues (PubMed:12504849). According to
CC another report, it is not imprinted in trophoblast stem cells
CC (PubMed:20644730). {ECO:0000269|PubMed:12504849,
CC ECO:0000269|PubMed:20644730}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96058.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AB074006; BAB85686.1; -; mRNA.
DR EMBL; AF392453; AAL40666.1; -; mRNA.
DR EMBL; AF410430; AAK98617.1; -; mRNA.
DR EMBL; AL136918; CAB66852.1; -; mRNA.
DR EMBL; AK056510; BAG51735.1; -; mRNA.
DR EMBL; AK301003; BAG62622.1; -; mRNA.
DR EMBL; AC108448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC877382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF455307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF455310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471158; EAX02542.1; -; Genomic_DNA.
DR EMBL; CH471158; EAX02543.1; -; Genomic_DNA.
DR EMBL; BC032646; AAH32646.2; -; mRNA.
DR EMBL; BC039579; AAH39579.1; -; mRNA.
DR EMBL; AF331964; AAG53417.1; -; mRNA.
DR EMBL; AB040967; BAA96058.1; ALT_SEQ; mRNA.
DR CCDS; CCDS31343.1; -. [Q9H0X9-2]
DR CCDS; CCDS31344.1; -. [Q9H0X9-1]
DR RefSeq; NP_001137535.1; NM_001144063.1. [Q9H0X9-2]
DR RefSeq; NP_065947.1; NM_020896.3. [Q9H0X9-1]
DR RefSeq; NP_663613.1; NM_145638.2. [Q9H0X9-2]
DR RefSeq; XP_011518175.1; XM_011519873.2. [Q9H0X9-1]
DR RefSeq; XP_016872652.1; XM_017017163.1. [Q9H0X9-1]
DR AlphaFoldDB; Q9H0X9; -.
DR SMR; Q9H0X9; -.
DR BioGRID; 125380; 62.
DR DIP; DIP-52332N; -.
DR IntAct; Q9H0X9; 23.
DR MINT; Q9H0X9; -.
DR STRING; 9606.ENSP00000263650; -.
DR SwissLipids; SLP:000000527; -.
DR TCDB; 2.D.1.1.1; the pi4p/ps counter transporter (p/p-ct) family.
DR iPTMnet; Q9H0X9; -.
DR PhosphoSitePlus; Q9H0X9; -.
DR BioMuta; OSBPL5; -.
DR DMDM; 20139173; -.
DR EPD; Q9H0X9; -.
DR jPOST; Q9H0X9; -.
DR MassIVE; Q9H0X9; -.
DR MaxQB; Q9H0X9; -.
DR PaxDb; Q9H0X9; -.
DR PeptideAtlas; Q9H0X9; -.
DR PRIDE; Q9H0X9; -.
DR ProteomicsDB; 5257; -.
DR ProteomicsDB; 80342; -. [Q9H0X9-1]
DR ProteomicsDB; 80343; -. [Q9H0X9-2]
DR Antibodypedia; 23281; 85 antibodies from 24 providers.
DR DNASU; 114879; -.
DR Ensembl; ENST00000263650.12; ENSP00000263650.7; ENSG00000021762.20. [Q9H0X9-1]
DR Ensembl; ENST00000348039.9; ENSP00000302872.8; ENSG00000021762.20. [Q9H0X9-2]
DR Ensembl; ENST00000389989.7; ENSP00000374639.3; ENSG00000021762.20. [Q9H0X9-2]
DR Ensembl; ENST00000525498.5; ENSP00000433342.1; ENSG00000021762.20. [Q9H0X9-3]
DR GeneID; 114879; -.
DR KEGG; hsa:114879; -.
DR MANE-Select; ENST00000263650.12; ENSP00000263650.7; NM_020896.4; NP_065947.1.
DR UCSC; uc001lxk.3; human. [Q9H0X9-1]
DR UCSC; uc010qxq.2; human.
DR CTD; 114879; -.
DR DisGeNET; 114879; -.
DR GeneCards; OSBPL5; -.
DR HGNC; HGNC:16392; OSBPL5.
DR HPA; ENSG00000021762; Low tissue specificity.
DR MIM; 606733; gene.
DR neXtProt; NX_Q9H0X9; -.
DR OpenTargets; ENSG00000021762; -.
DR PharmGKB; PA32829; -.
DR VEuPathDB; HostDB:ENSG00000021762; -.
DR eggNOG; KOG2210; Eukaryota.
DR GeneTree; ENSGT00940000159535; -.
DR HOGENOM; CLU_012334_2_1_1; -.
DR InParanoid; Q9H0X9; -.
DR OMA; NHHMEND; -.
DR OrthoDB; 949920at2759; -.
DR PhylomeDB; Q9H0X9; -.
DR TreeFam; TF312807; -.
DR PathwayCommons; Q9H0X9; -.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR SignaLink; Q9H0X9; -.
DR BioGRID-ORCS; 114879; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; OSBPL5; human.
DR GeneWiki; OSBPL5; -.
DR GenomeRNAi; 114879; -.
DR Pharos; Q9H0X9; Tbio.
DR PRO; PR:Q9H0X9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9H0X9; protein.
DR Bgee; ENSG00000021762; Expressed in pancreatic ductal cell and 182 other tissues.
DR ExpressionAtlas; Q9H0X9; baseline and differential.
DR Genevisible; Q9H0X9; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
DR GO; GO:0008142; F:oxysterol binding; NAS:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0140343; F:phosphatidylserine transfer activity; IDA:GO_Central.
DR GO; GO:0005548; F:phospholipid transporter activity; TAS:Reactome.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0008203; P:cholesterol metabolic process; NAS:UniProtKB.
DR GO; GO:0030301; P:cholesterol transport; NAS:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; NAS:UniProtKB.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0015914; P:phospholipid transport; IDA:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Endoplasmic reticulum; Lipid transport;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..879
FT /note="Oxysterol-binding protein-related protein 5"
FT /id="PRO_0000100373"
FT TRANSMEM 860..878
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 126..243
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 93..123
FT /evidence="ECO:0000255"
FT COMPBIAS 299..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 384..389
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 384..389
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 446..449
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 449
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 478..479
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 504
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 670
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 674
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT BINDING 678
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:Q02201"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ER64"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057408"
FT VAR_SEQ 134..201
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043071"
FT VAR_SEQ 161..201
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057409"
FT VARIANT 90
FT /note="T -> I (in dbSNP:rs6578323)"
FT /id="VAR_060079"
FT VARIANT 774
FT /note="A -> T (in dbSNP:rs2277301)"
FT /id="VAR_020414"
FT MUTAGEN 389
FT /note="L->D: Impaired lipid countertransport between the
FT endoplasmic reticulum and the plasma membrane."
FT /evidence="ECO:0000269|PubMed:26206935"
FT MUTAGEN 478..479
FT /note="HH->AA: Impaired lipid countertransport between the
FT endoplasmic reticulum and the plasma membrane."
FT /evidence="ECO:0000269|PubMed:26206935"
SQ SEQUENCE 879 AA; 98616 MW; 7EF06544347CC60A CRC64;
MKEEAFLRRR FSLCPPSSTP QKVDPRKLTR NLLLSGDNEL YPLSPGKDME PNGPSLPRDE
GPPTPSSATK VPPAEYRLCN GSDKECVSPT ARVTKKETLK AQKENYRQEK KRATRQLLSA
LTDPSVVIMA DSLKIRGTLK SWTKLWCVLK PGVLLIYKTP KVGQWVGTVL LHCCELIERP
SKKDGFCFKL FHPLDQSVWA VKGPKGESVG SITQPLPSSY LIFRAASESD GRCWLDALEL
ALRCSSLLRL GTCKPGRDGE PGTSPDASPS SLCGLPASAT VHPDQDLFPL NGSSLENDAF
SDKSERENPE ESDTETQDHS RKTESGSDQS ETPGAPVRRG TTYVEQVQEE LGELGEASQV
ETVSEENKSL MWTLLKQLRP GMDLSRVVLP TFVLEPRSFL NKLSDYYYHA DLLSRAAVEE
DAYSRMKLVL RWYLSGFYKK PKGIKKPYNP ILGETFRCCW FHPQTDSRTF YIAEQVSHHP
PVSAFHVSNR KDGFCISGSI TAKSRFYGNS LSALLDGKAT LTFLNRAEDY TLTMPYAHCK
GILYGTMTLE LGGKVTIECA KNNFQAQLEF KLKPFFGGST SINQISGKIT SGEEVLASLS
GHWDRDVFIK EEGSGSSALF WTPSGEVRRQ RLRQHTVPLE EQTELESERL WQHVTRAISK
GDQHRATQEK FALEEAQRQR ARERQESLMP WKPQLFHLDP ITQEWHYRYE DHSPWDPLKD
IAQFEQDGIL RTLQQEAVAR QTTFLGSPGP RHERSGPDQR LRKASDQPSG HSQATESSGS
TPESCPELSD EEQDGDFVPG GESPCPRCRK EARRLQALHE AILSIREAQQ ELHRHLSAML
SSTARAAQAP TPGLLQSPRS WFLLCVFLAC QLFINHILK
