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 27-MAR-2024, entry version 179. 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; GN 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 64. 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 SwissPalm; Q9H0X9; -. DR BioMuta; OSBPL5; -. DR DMDM; 20139173; -. DR EPD; Q9H0X9; -. DR jPOST; Q9H0X9; -. DR MassIVE; Q9H0X9; -. DR MaxQB; Q9H0X9; -. DR PaxDb; 9606-ENSP00000263650; -. DR PeptideAtlas; Q9H0X9; -. DR ProteomicsDB; 5257; -. DR ProteomicsDB; 80342; -. [Q9H0X9-1] DR ProteomicsDB; 80343; -. [Q9H0X9-2] DR Pumba; Q9H0X9; -. DR Antibodypedia; 23281; 102 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 AGR; HGNC:16392; -. 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; WESAKLW; -. DR OrthoDB; 1018068at2759; -. 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; 11 hits in 1154 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 184 other cell types or tissues. DR ExpressionAtlas; Q9H0X9; baseline and differential. 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: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 CDD; cd13286; PH_OPR5_ORP8; 1. DR Gene3D; 1.10.287.2720; -; 1. DR Gene3D; 2.40.160.120; -; 1. DR Gene3D; 3.30.70.3490; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; OXYSTEROL-BINDING PROTEIN-RELATED; 1. DR PANTHER; PTHR10972:SF221; OXYSTEROL-BINDING PROTEIN-RELATED PROTEIN 5; 1. DR Pfam; PF01237; Oxysterol_BP; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS01013; OSBP; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR Genevisible; Q9H0X9; HS. 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 //