OSBL9_HUMAN
ID OSBL9_HUMAN Reviewed; 736 AA.
AC Q96SU4; B1AKJ8; B3KPQ4; D3DQ31; Q5TFC0; Q6IA67; Q86YQ3; Q8NB17; Q8TAS8;
AC Q96SK4; Q9H9X2;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Oxysterol-binding protein-related protein 9;
DE Short=ORP-9;
DE Short=OSBP-related protein 9;
GN Name=OSBPL9; Synonyms=ORP9, OSBP4;
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), AND TISSUE SPECIFICITY.
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 [MRNA] (ISOFORM 7).
RA Hao D.C., Hooi S.C.;
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 AND 6).
RC TISSUE=Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Lymph;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=20599956; DOI=10.1016/j.yexcr.2010.06.008;
RA Zhou Y., Li S., Mayranpaa M.I., Zhong W., Back N., Yan D., Olkkonen V.M.;
RT "OSBP-related protein 11 (ORP11) dimerizes with ORP9 and localizes at the
RT Golgi-late endosome interface.";
RL Exp. Cell Res. 316:3304-3316(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP INTERACTION WITH OSBPL10.
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-325; SER-326;
RP SER-329 AND SER-611, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP VARIANT LEU-266.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- SUBUNIT: Heterodimer with OSBPL11 (PubMed:20599956). Interacts with
CC OSBPL10 (PubMed:22906437). {ECO:0000269|PubMed:20599956,
CC ECO:0000269|PubMed:22906437}.
CC -!- INTERACTION:
CC Q96SU4; Q92685: ALG3; NbExp=2; IntAct=EBI-2511368, EBI-2848814;
CC Q96SU4; Q9BXB5: OSBPL10; NbExp=3; IntAct=EBI-2511368, EBI-2511286;
CC Q96SU4; Q9BXB4: OSBPL11; NbExp=7; IntAct=EBI-2511368, EBI-2514786;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:20599956}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:20599956}. Note=Localizes at the Golgi-
CC late endosome interface.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q96SU4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96SU4-2; Sequence=VSP_003782;
CC Name=3;
CC IsoId=Q96SU4-3; Sequence=VSP_036780, VSP_036781, VSP_003782;
CC Name=4;
CC IsoId=Q96SU4-4; Sequence=VSP_036779;
CC Name=5;
CC IsoId=Q96SU4-5; Sequence=VSP_036779, VSP_003782;
CC Name=6;
CC IsoId=Q96SU4-6; Sequence=VSP_043631, VSP_003782;
CC Name=7;
CC IsoId=Q96SU4-7; Sequence=VSP_043630;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11735225}.
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; AF392445; AAL40658.1; -; mRNA.
DR EMBL; AY178997; AAO20108.1; -; mRNA.
DR EMBL; AK022554; BAB14096.1; -; mRNA.
DR EMBL; AK027535; BAB55184.1; -; mRNA.
DR EMBL; AK027707; BAB55312.1; -; mRNA.
DR EMBL; AK056617; BAG51766.1; -; mRNA.
DR EMBL; AK091703; BAC03727.1; -; mRNA.
DR EMBL; CR457288; CAG33569.1; -; mRNA.
DR EMBL; AL050343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL772260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06810.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06813.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06816.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06819.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06817.1; -; Genomic_DNA.
DR EMBL; BC025978; AAH25978.1; -; mRNA.
DR CCDS; CCDS41332.3; -. [Q96SU4-1]
DR CCDS; CCDS41333.2; -. [Q96SU4-7]
DR CCDS; CCDS41334.1; -. [Q96SU4-5]
DR CCDS; CCDS44145.1; -. [Q96SU4-6]
DR CCDS; CCDS55598.1; -. [Q96SU4-2]
DR CCDS; CCDS558.1; -. [Q96SU4-3]
DR CCDS; CCDS81322.1; -. [Q96SU4-4]
DR RefSeq; NP_001317509.1; NM_001330580.1. [Q96SU4-4]
DR RefSeq; NP_078862.4; NM_024586.5. [Q96SU4-1]
DR RefSeq; NP_683702.1; NM_148904.3. [Q96SU4-5]
DR RefSeq; NP_683703.1; NM_148905.3. [Q96SU4-5]
DR RefSeq; NP_683704.2; NM_148906.2. [Q96SU4-7]
DR RefSeq; NP_683705.1; NM_148907.2. [Q96SU4-3]
DR RefSeq; NP_683706.3; NM_148908.3. [Q96SU4-2]
DR RefSeq; NP_683707.3; NM_148909.3. [Q96SU4-6]
DR RefSeq; XP_006710386.1; XM_006710323.2. [Q96SU4-4]
DR RefSeq; XP_006710387.1; XM_006710324.3. [Q96SU4-5]
DR RefSeq; XP_006710388.1; XM_006710325.3. [Q96SU4-5]
DR RefSeq; XP_006710389.1; XM_006710326.2. [Q96SU4-5]
DR RefSeq; XP_011538905.1; XM_011540603.2. [Q96SU4-4]
DR RefSeq; XP_011538906.1; XM_011540604.2. [Q96SU4-4]
DR RefSeq; XP_016855708.1; XM_017000219.1. [Q96SU4-5]
DR RefSeq; XP_016855709.1; XM_017000220.1. [Q96SU4-5]
DR RefSeq; XP_016855710.1; XM_017000221.1. [Q96SU4-5]
DR AlphaFoldDB; Q96SU4; -.
DR SMR; Q96SU4; -.
DR BioGRID; 125384; 75.
DR ELM; Q96SU4; -.
DR IntAct; Q96SU4; 29.
DR MINT; Q96SU4; -.
DR STRING; 9606.ENSP00000412733; -.
DR GlyGen; Q96SU4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96SU4; -.
DR PhosphoSitePlus; Q96SU4; -.
DR BioMuta; OSBPL9; -.
DR DMDM; 20139075; -.
DR EPD; Q96SU4; -.
DR jPOST; Q96SU4; -.
DR MassIVE; Q96SU4; -.
DR MaxQB; Q96SU4; -.
DR PaxDb; Q96SU4; -.
DR PeptideAtlas; Q96SU4; -.
DR PRIDE; Q96SU4; -.
DR ProteomicsDB; 78150; -. [Q96SU4-1]
DR ProteomicsDB; 78151; -. [Q96SU4-2]
DR ProteomicsDB; 78152; -. [Q96SU4-3]
DR ProteomicsDB; 78153; -. [Q96SU4-4]
DR ProteomicsDB; 78154; -. [Q96SU4-5]
DR ProteomicsDB; 78155; -. [Q96SU4-6]
DR ProteomicsDB; 78156; -. [Q96SU4-7]
DR Antibodypedia; 18985; 141 antibodies from 33 providers.
DR DNASU; 114883; -.
DR Ensembl; ENST00000361556.9; ENSP00000354970.5; ENSG00000117859.19. [Q96SU4-3]
DR Ensembl; ENST00000371714.5; ENSP00000360779.1; ENSG00000117859.19. [Q96SU4-2]
DR Ensembl; ENST00000428468.6; ENSP00000407168.1; ENSG00000117859.19. [Q96SU4-1]
DR Ensembl; ENST00000447887.5; ENSP00000412733.1; ENSG00000117859.19. [Q96SU4-6]
DR Ensembl; ENST00000453295.5; ENSP00000413263.1; ENSG00000117859.19. [Q96SU4-7]
DR Ensembl; ENST00000462759.5; ENSP00000433279.1; ENSG00000117859.19. [Q96SU4-5]
DR Ensembl; ENST00000486942.5; ENSP00000431980.1; ENSG00000117859.19. [Q96SU4-5]
DR Ensembl; ENST00000531828.5; ENSP00000433083.1; ENSG00000117859.19. [Q96SU4-4]
DR GeneID; 114883; -.
DR KEGG; hsa:114883; -.
DR MANE-Select; ENST00000428468.6; ENSP00000407168.1; NM_024586.6; NP_078862.4.
DR UCSC; uc001cst.5; human. [Q96SU4-1]
DR CTD; 114883; -.
DR DisGeNET; 114883; -.
DR GeneCards; OSBPL9; -.
DR HGNC; HGNC:16386; OSBPL9.
DR HPA; ENSG00000117859; Low tissue specificity.
DR MIM; 606737; gene.
DR neXtProt; NX_Q96SU4; -.
DR OpenTargets; ENSG00000117859; -.
DR PharmGKB; PA32833; -.
DR VEuPathDB; HostDB:ENSG00000117859; -.
DR eggNOG; KOG2210; Eukaryota.
DR GeneTree; ENSGT00940000154690; -.
DR HOGENOM; CLU_012334_3_0_1; -.
DR InParanoid; Q96SU4; -.
DR OMA; WPGSDEK; -.
DR OrthoDB; 949920at2759; -.
DR PhylomeDB; Q96SU4; -.
DR TreeFam; TF312807; -.
DR PathwayCommons; Q96SU4; -.
DR Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
DR SignaLink; Q96SU4; -.
DR BioGRID-ORCS; 114883; 27 hits in 1084 CRISPR screens.
DR ChiTaRS; OSBPL9; human.
DR GeneWiki; OSBPL9; -.
DR GenomeRNAi; 114883; -.
DR Pharos; Q96SU4; Tbio.
DR PRO; PR:Q96SU4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96SU4; protein.
DR Bgee; ENSG00000117859; Expressed in calcaneal tendon and 206 other tissues.
DR ExpressionAtlas; Q96SU4; baseline and differential.
DR Genevisible; Q96SU4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0006699; P:bile acid biosynthetic process; 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; 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 Acetylation; Alternative splicing; Endosome; Golgi apparatus;
KW Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..736
FT /note="Oxysterol-binding protein-related protein 9"
FT /id="PRO_0000100379"
FT DOMAIN 2..99
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 231..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..165
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_036779"
FT VAR_SEQ 1..97
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036780"
FT VAR_SEQ 38..54
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_043630"
FT VAR_SEQ 98..106
FT /note="ILRHTLQLQ -> MAFLLATCG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036781"
FT VAR_SEQ 106
FT /note="Q -> QISTTLAFFQSSGISPVLEFSKII (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043631"
FT VAR_SEQ 182..194
FT /note="Missing (in isoform 2, isoform 3, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_003782"
FT VARIANT 266
FT /note="P -> L (in dbSNP:rs140080386)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069380"
FT CONFLICT 295
FT /note="F -> L (in Ref. 3; BAC03727)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="K -> R (in Ref. 3; BAB55312)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 736 AA; 83185 MW; A689D5D68E95EC6C CRC64;
MASIMEGPLS KWTNVMKGWQ YRWFVLDYNA GLLSYYTSKD KMMRGSRRGC VRLRGAVIGI
DDEDDSTFTI TVDQKTFHFQ ARDADEREKW IHALEETILR HTLQLQGLDS GFVPSVQDFD
KKLTEADAYL QILIEQLKLF DDKLQNCKED EQRKKIETLK ETTNSMVESI KHCIVLLQIA
KDQSNAEKHA DGMISTINPV DAIYQPSPLE PVISTMPSQT VLPPEPVQLC KSEQRPSSLP
VGPVLATLGH HQTPTPNSTG SGHSPPSSSL TSPSHVNLSP NTVPEFSYSS SEDEFYDADE
FHQSGSSPKR LIDSSGSASV LTHSSSGNSL KRPDTTESLN SSLSNGTSDA DLFDSHDDRD
DDAEAGSVEE HKSVIMHLLS QVRLGMDLTK VVLPTFILER RSLLEMYADF FAHPDLFVSI
SDQKDPKDRM VQVVKWYLSA FHAGRKGSVA KKPYNPILGE IFQCHWTLPN DTEENTELVS
EGPVPWVSKN SVTFVAEQVS HHPPISAFYA ECFNKKIQFN AHIWTKSKFL GMSIGVHNIG
QGCVSCLDYD EHYILTFPNG YGRSILTVPW VELGGECNIN CSKTGYSANI IFHTKPFYGG
KKHRITAEIF SPNDKKSFCS IEGEWNGVMY AKYATGENTV FVDTKKLPII KKKVRKLEDQ
NEYESRSLWK DVTFNLKIRD IDAATEAKHR LEERQRAEAR ERKEKEIQWE TRLFHEDGEC
WVYDEPLLKR LGAAKH
