OSB10_HUMAN
ID OSB10_HUMAN Reviewed; 764 AA.
AC Q9BXB5; B4E212; Q9BTU5;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Oxysterol-binding protein-related protein 10;
DE Short=ORP-10;
DE Short=OSBP-related protein 10;
GN Name=OSBPL10; Synonyms=ORP10, OSBP9;
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).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-251 (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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP FUNCTION, AND DOMAIN.
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 [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-60; SER-64; THR-196;
RP SER-201 AND SER-223, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19554302; DOI=10.1007/s00109-009-0490-z;
RA Perttila J., Merikanto K., Naukkarinen J., Surakka I., Martin N.W.,
RA Tanhuanpaa K., Grimard V., Taskinen M.R., Thiele C., Salomaa V., Jula A.,
RA Perola M., Virtanen I., Peltonen L., Olkkonen V.M.;
RT "OSBPL10, a novel candidate gene for high triglyceride trait in
RT dyslipidemic Finnish subjects, regulates cellular lipid metabolism.";
RL J. Mol. Med. 87:825-835(2009).
RN [11]
RP POLYMORPHISM.
RX PubMed=20224571; DOI=10.1038/hr.2010.28;
RA Koriyama H., Nakagami H., Katsuya T., Akasaka H., Saitoh S., Shimamoto K.,
RA Ogihara T., Kaneda Y., Morishita R., Rakugi H.;
RT "Variation in OSBPL10 is associated with dyslipidemia.";
RL Hypertens. Res. 33:511-514(2010).
RN [12]
RP POLYMORPHISM.
RX PubMed=20610895; DOI=10.5551/jat.4291;
RA Koriyama H., Nakagami H., Katsuya T., Sugimoto K., Yamashita H., Takami Y.,
RA Maeda S., Kubo M., Takahashi A., Nakamura Y., Ogihara T., Rakugi H.,
RA Kaneda Y., Morishita R.;
RT "Identification of evidence suggestive of an association with peripheral
RT arterial disease at the OSBPL10 locus by genome-wide investigation in the
RT Japanese population.";
RL J. Atheroscler. Thromb. 17:1054-1062(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND SER-223, AND
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP FUNCTION, INTERACTION WITH OSBPL9, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=22906437; DOI=10.1016/j.bbalip.2012.08.004;
RA Nissila E., Ohsaki Y., Weber-Boyvat M., Perttila J., Ikonen E.,
RA Olkkonen V.M.;
RT "ORP10, a cholesterol binding protein associated with microtubules,
RT regulates apolipoprotein B-100 secretion.";
RL Biochim. Biophys. Acta 1821:1472-1484(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-64; SER-209 AND
RP SER-223, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [17]
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH DIAPH1.
RX PubMed=23325789; DOI=10.1091/mbc.e12-08-0597;
RA Li D., Dammer E.B., Lucki N.C., Sewer M.B.;
RT "cAMP-stimulated phosphorylation of diaphanous 1 regulates protein
RT stability and interaction with binding partners in adrenocortical cells.";
RL Mol. Biol. Cell 24:848-857(2013).
RN [19]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-38, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Probable lipid transporter involved in lipid countertransport
CC between the endoplasmic reticulum and the plasma membrane. Its ability
CC to bind phosphatidylserine, suggests that it specifically exchanges
CC phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P),
CC delivering phosphatidylserine to the plasma membrane in exchange for
CC PI4P (PubMed:23934110) (Probable). Plays a role in negative regulation
CC of lipid biosynthesis (PubMed:19554302). Negatively regulates APOB
CC secretion from hepatocytes (PubMed:19554302, PubMed:22906437). Binds
CC cholesterol and acidic phospholipids (PubMed:22906437). Also binds 25-
CC hydroxycholesterol (PubMed:17428193). Binds phosphatidylserine
CC (PubMed:23934110). {ECO:0000269|PubMed:17428193,
CC ECO:0000269|PubMed:19554302, ECO:0000269|PubMed:22906437,
CC ECO:0000269|PubMed:23934110, ECO:0000305}.
CC -!- SUBUNIT: Interacts with OSBPL9 (PubMed:22906437). Interacts with DIAPH1
CC (PubMed:23325789). {ECO:0000269|PubMed:22906437,
CC ECO:0000269|PubMed:23325789}.
CC -!- INTERACTION:
CC Q9BXB5; Q96SU4: OSBPL9; NbExp=3; IntAct=EBI-2511286, EBI-2511368;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19554302, ECO:0000269|PubMed:22906437}.
CC Note=Associates with microtubules. {ECO:0000269|PubMed:19554302,
CC ECO:0000269|PubMed:22906437}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BXB5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXB5-2; Sequence=VSP_042930;
CC -!- DOMAIN: The C-terminal region binds cholesterol, 25-hydroxysterol and
CC acidic phospholipids and is required for localization to microtubules.
CC {ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:22906437}.
CC -!- DOMAIN: The PH domain selectively interacts with phosphatidylinositol-
CC 4-phosphate. {ECO:0000269|PubMed:22906437}.
CC -!- POLYMORPHISM: Polymorphisms are associated with dyslipidemia. Variant
CC Asn-254 is associated with LDL-cholesterol levels in Japanese
CC population (PubMed:20224571). Association with peripheral arterial
CC disease has also been observed (PubMed:20610895).
CC {ECO:0000269|PubMed:20224571, ECO:0000269|PubMed:20610895}.
CC -!- SIMILARITY: Belongs to the OSBP family. {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; AF392451; AAL40664.1; -; mRNA.
DR EMBL; AK304067; BAG64974.1; -; mRNA.
DR EMBL; AC092024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC094019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003168; AAH03168.2; -; mRNA.
DR EMBL; AF346291; AAK31140.1; -; mRNA.
DR CCDS; CCDS2651.1; -. [Q9BXB5-1]
DR CCDS; CCDS54559.1; -. [Q9BXB5-2]
DR RefSeq; NP_001167531.1; NM_001174060.1. [Q9BXB5-2]
DR RefSeq; NP_060254.2; NM_017784.4. [Q9BXB5-1]
DR AlphaFoldDB; Q9BXB5; -.
DR SMR; Q9BXB5; -.
DR BioGRID; 125385; 47.
DR IntAct; Q9BXB5; 23.
DR STRING; 9606.ENSP00000379804; -.
DR SwissLipids; SLP:000000528; -.
DR GlyGen; Q9BXB5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BXB5; -.
DR PhosphoSitePlus; Q9BXB5; -.
DR BioMuta; OSBPL10; -.
DR DMDM; 20139128; -.
DR CPTAC; CPTAC-1625; -.
DR EPD; Q9BXB5; -.
DR jPOST; Q9BXB5; -.
DR MassIVE; Q9BXB5; -.
DR MaxQB; Q9BXB5; -.
DR PaxDb; Q9BXB5; -.
DR PeptideAtlas; Q9BXB5; -.
DR PRIDE; Q9BXB5; -.
DR ProteomicsDB; 79399; -. [Q9BXB5-1]
DR ProteomicsDB; 79400; -. [Q9BXB5-2]
DR Antibodypedia; 1161; 171 antibodies from 30 providers.
DR DNASU; 114884; -.
DR Ensembl; ENST00000396556.7; ENSP00000379804.2; ENSG00000144645.15. [Q9BXB5-1]
DR Ensembl; ENST00000438237.6; ENSP00000406124.2; ENSG00000144645.15. [Q9BXB5-2]
DR GeneID; 114884; -.
DR KEGG; hsa:114884; -.
DR MANE-Select; ENST00000396556.7; ENSP00000379804.2; NM_017784.5; NP_060254.2.
DR UCSC; uc011axf.3; human. [Q9BXB5-1]
DR CTD; 114884; -.
DR DisGeNET; 114884; -.
DR GeneCards; OSBPL10; -.
DR HGNC; HGNC:16395; OSBPL10.
DR HPA; ENSG00000144645; Low tissue specificity.
DR MIM; 606738; gene.
DR neXtProt; NX_Q9BXB5; -.
DR OpenTargets; ENSG00000144645; -.
DR PharmGKB; PA32824; -.
DR VEuPathDB; HostDB:ENSG00000144645; -.
DR eggNOG; KOG2210; Eukaryota.
DR GeneTree; ENSGT00940000157880; -.
DR HOGENOM; CLU_012334_3_1_1; -.
DR InParanoid; Q9BXB5; -.
DR OMA; MHQVGQH; -.
DR OrthoDB; 949920at2759; -.
DR PhylomeDB; Q9BXB5; -.
DR TreeFam; TF312807; -.
DR PathwayCommons; Q9BXB5; -.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR SignaLink; Q9BXB5; -.
DR BioGRID-ORCS; 114884; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; OSBPL10; human.
DR GenomeRNAi; 114884; -.
DR Pharos; Q9BXB5; Tbio.
DR PRO; PR:Q9BXB5; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BXB5; protein.
DR Bgee; ENSG00000144645; Expressed in secondary oocyte and 186 other tissues.
DR ExpressionAtlas; Q9BXB5; baseline and differential.
DR Genevisible; Q9BXB5; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
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:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome.
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; IPR041680; PH_8.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF15409; PH_8; 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; Cytoplasm; Cytoskeleton;
KW Lipid biosynthesis; Lipid metabolism; Lipid transport; Lipid-binding;
KW Methylation; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..764
FT /note="Oxysterol-binding protein-related protein 10"
FT /id="PRO_0000100380"
FT DOMAIN 74..171
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 713..740
FT /evidence="ECO:0000255"
FT COMPBIAS 9..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 413..418
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 413..418
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 477..480
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 480
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 535..536
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 561
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 721
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 725
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 729
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 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:S4R1M9"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 38
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 180..243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042930"
FT VARIANT 254
FT /note="N -> D (in dbSNP:rs2290532)"
FT /id="VAR_022100"
SQ SEQUENCE 764 AA; 83970 MW; 62B1DF599C7C15FC CRC64;
MERAVQGTDG GGGSNSSSRS SSRATSAGSS PSCSLAGRGV SSRSAAAGLG GGGSRSSPGS
VAASPSGGGG RRREPALEGV LSKYTNLLQG WQNRYFVLDF EAGILQYFVN EQSKHQKPRG
VLSLSGAIVS LSDEAPHMLV VYSANGEMFK LRAADAKEKQ FWVTQLRACA KYHMEMNSKS
APSSRSRSLT LLPHGTPNSA SPCSQRHLSV GAPGVVTITH HKSPAAARRA KSQYSGQLHE
VREMMNQVEG QQKNLVHAIE SLPGSGPLTA LDQDLLLLKA TSAATLSCLG ECLNLLQQSV
HQAGQPSQKP GASENILGWH GSKSHSTEQL KNGTLGSLPS ASANITWAIL PNSAEDEQTS
QPEPEPNSGS ELVLSEDEKS DNEDKEETEL GVMEDQRSII LHLISQLKLG MDLTKVVLPT
FILEKRSLLE MYADFMAHPD LLLAITAGAT PEERVICFVE YYLTAFHEGR KGALAKKPYN
PIIGETFHCS WEVPKDRVKP KRTASRSPAS CHEHPMADDP SKSYKLRFVA EQVSHHPPIS
CFYCECEEKR LCVNTHVWTK SKFMGMSVGV SMIGEGVLRL LEHGEEYVFT LPSAYARSIL
TIPWVELGGK VSINCAKTGY SATVIFHTKP FYGGKVHRVT AEVKHNPTNT IVCKAHGEWN
GTLEFTYNNG ETKVIDTTTL PVYPKKIRPL EKQGPMESRN LWREVTRYLR LGDIDAATEQ
KRHLEEKQRV EERKRENLRT PWKPKYFIQE GDGWVYFNPL WKAH
