Full text data of OSBPL8
OSBPL8
(KIAA1451, ORP8, OSBP10)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Oxysterol-binding protein-related protein 8; ORP-8; OSBP-related protein 8
Oxysterol-binding protein-related protein 8; ORP-8; OSBP-related protein 8
UniProt
Q9BZF1
ID OSBL8_HUMAN Reviewed; 889 AA.
AC Q9BZF1; A8K1T2; E9PE66; E9PE68; Q52LQ3; Q68D75; Q8WXP8; Q9P277;
read moreDT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 3.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Oxysterol-binding protein-related protein 8;
DE Short=ORP-8;
DE Short=OSBP-related protein 8;
GN Name=OSBPL8; Synonyms=KIAA1451, ORP8, OSBP10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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 [LARGE SCALE MRNA] (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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-578 (ISOFORM 2).
RX PubMed=11483621;
RA Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C.,
RA Staels B., Ikonen E., Olkkonen V.M.;
RT "The OSBP-related protein family in humans.";
RL J. Lipid Res. 42:1203-1213(2001).
RN [9]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-314;
RP SER-807; SER-808; SER-810 AND SER-814, AND MASS SPECTROMETRY.
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-328; SER-342;
RP SER-807 AND SER-808, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP STRUCTURE BY NMR OF 147-265.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the pleckstrin homology domain of oxysterol-
RT binding protein-related protein 8 (KIAA1451 protein).";
RL Submitted (JUN-2004) to the PDB data bank.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BZF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZF1-2; Sequence=VSP_009120;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9BZF1-3; Sequence=VSP_045801;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the OSBP family.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG53411.1; Type=Frameshift; Positions=30;
CC Sequence=BAA95975.3; Type=Erroneous initiation;
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DR EMBL; AF392452; AAL40665.1; -; mRNA.
DR EMBL; AB040884; BAA95975.3; ALT_INIT; mRNA.
DR EMBL; AK289997; BAF82686.1; -; mRNA.
DR EMBL; CR749542; CAH18345.1; -; mRNA.
DR EMBL; AC117491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093834; AAH93834.1; -; mRNA.
DR EMBL; BC101529; AAI01530.1; -; mRNA.
DR EMBL; BC111728; AAI11729.1; -; mRNA.
DR EMBL; AF323730; AAG53411.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001003712.1; NM_001003712.1.
DR RefSeq; NP_065892.1; NM_020841.4.
DR RefSeq; XP_005268678.1; XM_005268621.1.
DR RefSeq; XP_005268680.1; XM_005268623.1.
DR UniGene; Hs.430849; -.
DR PDB; 1V88; NMR; -; A=149-265.
DR PDBsum; 1V88; -.
DR ProteinModelPortal; Q9BZF1; -.
DR SMR; Q9BZF1; 147-265, 426-733.
DR IntAct; Q9BZF1; 6.
DR MINT; MINT-2816858; -.
DR STRING; 9606.ENSP00000261183; -.
DR PhosphoSite; Q9BZF1; -.
DR DMDM; 39932732; -.
DR PaxDb; Q9BZF1; -.
DR PRIDE; Q9BZF1; -.
DR Ensembl; ENST00000261183; ENSP00000261183; ENSG00000091039.
DR Ensembl; ENST00000393249; ENSP00000376939; ENSG00000091039.
DR Ensembl; ENST00000393250; ENSP00000376940; ENSG00000091039.
DR GeneID; 114882; -.
DR KEGG; hsa:114882; -.
DR UCSC; uc001sye.1; human.
DR CTD; 114882; -.
DR GeneCards; GC12M076745; -.
DR HGNC; HGNC:16396; OSBPL8.
DR HPA; HPA001309; -.
DR MIM; 606736; gene.
DR neXtProt; NX_Q9BZF1; -.
DR PharmGKB; PA32832; -.
DR eggNOG; NOG262374; -.
DR HOVERGEN; HBG053375; -.
DR InParanoid; Q9BZF1; -.
DR OMA; TKDLYQP; -.
DR OrthoDB; EOG7D59MQ; -.
DR PhylomeDB; Q9BZF1; -.
DR ChiTaRS; OSBPL8; human.
DR EvolutionaryTrace; Q9BZF1; -.
DR GeneWiki; OSBPL8; -.
DR GenomeRNAi; 114882; -.
DR NextBio; 79363; -.
DR PMAP-CutDB; Q9BZF1; -.
DR PRO; PR:Q9BZF1; -.
DR ArrayExpress; Q9BZF1; -.
DR Bgee; Q9BZF1; -.
DR CleanEx; HS_OSBPL8; -.
DR Genevestigator; Q9BZF1; -.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0045444; P:fat cell differentiation; IDA:BHF-UCL.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:BHF-UCL.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Lipid transport; Lipid-binding; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1 889 Oxysterol-binding protein-related protein
FT 8.
FT /FTId=PRO_0000100378.
FT DOMAIN 148 265 PH.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 65 65 Phosphoserine.
FT MOD_RES 68 68 Phosphoserine.
FT MOD_RES 314 314 Phosphoserine.
FT MOD_RES 328 328 Phosphoserine.
FT MOD_RES 342 342 Phosphoserine.
FT MOD_RES 807 807 Phosphoserine.
FT MOD_RES 808 808 Phosphoserine.
FT MOD_RES 810 810 Phosphoserine.
FT MOD_RES 814 814 Phosphoserine.
FT VAR_SEQ 1 42 Missing (in isoform 3).
FT /FTId=VSP_045801.
FT VAR_SEQ 15 29 Missing (in isoform 2).
FT /FTId=VSP_009120.
FT CONFLICT 347 347 M -> V (in Ref. 5; CAH18345).
FT STRAND 151 157
FT STRAND 160 163
FT STRAND 165 172
FT STRAND 175 180
FT STRAND 182 184
FT STRAND 189 192
FT TURN 203 205
FT STRAND 209 213
FT STRAND 244 246
FT HELIX 250 264
SQ SEQUENCE 889 AA; 101196 MW; 79DB8055BD15FE95 CRC64;
MEGGLADGEP DRTSLLGDSK DVLGPSTVVA NSDESQLLTP GKMSQRQGKE AYPTPTKDLH
QPSLSPASPH SQGFERGKED ISQNKDESSL SMSKSKSESK LYNGSEKDSS TSSKLTKKES
LKVQKKNYRE EKKRATKELL STITDPSVIV MADWLKIRGT LKSWTKLWCV LKPGVLLIYK
TQKNGQWVGT VLLNACEIIE RPSKKDGFCF KLFHPLEQSI WAVKGPKGEA VGSITQPLPS
SYLIIRATSE SDGRCWMDAL ELALKCSSLL KRTMIREGKE HDLSVSSDST HVTFYGLLRA
NNLHSGDNFQ LNDSEIERQH FKDQDMYSDK SDKENDQEHD ESDNEVMGKS EESDTDTSER
QDDSYIEPEP VEPLKETTYT EQSHEELGEA GEASQTETVS EENKSLIWTL LKQVRPGMDL
SKVVLPTFIL EPRSFLDKLS DYYYHADFLS EAALEENPYF RLKKVVKWYL SGFYKKPKGL
KKPYNPILGE TFRCLWIHPR TNSKTFYIAE QVSHHPPISA FYVSNRKDGF CLSGSILAKS
KFYGNSLSAI LEGEARLTFL NRGEDYVMTM PYAHCKGILY GTMTLELGGT VNITCQKTGY
SAILEFKLKP FLGSSDCVNQ ISGKLKLGKE VLATLEGHWD SEVFITDKKT DNSEVFWNPT
PDIKQWRLIR HTVKFEEQGD FESEKLWQRV TRAINAKDQT EATQEKYVLE EAQRQAARDR
KTKNEEWSCK LFELDPLTGE WHYKFADTRP WDPLNDMIQF EKDGVIQTKV KHRTPMVSVP
KMKHKPTRQQ KKVAKGYSSP EPDIQDSSGS EAQSVKPSTR RKKGIELGDI QSSIESIKQT
QEEIKRNIMA LRNHLVSSTP ATDYFLQQKD YFIIFLLILL QVIINFMFK
//
ID OSBL8_HUMAN Reviewed; 889 AA.
AC Q9BZF1; A8K1T2; E9PE66; E9PE68; Q52LQ3; Q68D75; Q8WXP8; Q9P277;
read moreDT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 3.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Oxysterol-binding protein-related protein 8;
DE Short=ORP-8;
DE Short=OSBP-related protein 8;
GN Name=OSBPL8; Synonyms=KIAA1451, ORP8, OSBP10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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 [LARGE SCALE MRNA] (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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-578 (ISOFORM 2).
RX PubMed=11483621;
RA Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C.,
RA Staels B., Ikonen E., Olkkonen V.M.;
RT "The OSBP-related protein family in humans.";
RL J. Lipid Res. 42:1203-1213(2001).
RN [9]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-314;
RP SER-807; SER-808; SER-810 AND SER-814, AND MASS SPECTROMETRY.
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-328; SER-342;
RP SER-807 AND SER-808, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP STRUCTURE BY NMR OF 147-265.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the pleckstrin homology domain of oxysterol-
RT binding protein-related protein 8 (KIAA1451 protein).";
RL Submitted (JUN-2004) to the PDB data bank.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BZF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZF1-2; Sequence=VSP_009120;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9BZF1-3; Sequence=VSP_045801;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the OSBP family.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG53411.1; Type=Frameshift; Positions=30;
CC Sequence=BAA95975.3; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AF392452; AAL40665.1; -; mRNA.
DR EMBL; AB040884; BAA95975.3; ALT_INIT; mRNA.
DR EMBL; AK289997; BAF82686.1; -; mRNA.
DR EMBL; CR749542; CAH18345.1; -; mRNA.
DR EMBL; AC117491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093834; AAH93834.1; -; mRNA.
DR EMBL; BC101529; AAI01530.1; -; mRNA.
DR EMBL; BC111728; AAI11729.1; -; mRNA.
DR EMBL; AF323730; AAG53411.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001003712.1; NM_001003712.1.
DR RefSeq; NP_065892.1; NM_020841.4.
DR RefSeq; XP_005268678.1; XM_005268621.1.
DR RefSeq; XP_005268680.1; XM_005268623.1.
DR UniGene; Hs.430849; -.
DR PDB; 1V88; NMR; -; A=149-265.
DR PDBsum; 1V88; -.
DR ProteinModelPortal; Q9BZF1; -.
DR SMR; Q9BZF1; 147-265, 426-733.
DR IntAct; Q9BZF1; 6.
DR MINT; MINT-2816858; -.
DR STRING; 9606.ENSP00000261183; -.
DR PhosphoSite; Q9BZF1; -.
DR DMDM; 39932732; -.
DR PaxDb; Q9BZF1; -.
DR PRIDE; Q9BZF1; -.
DR Ensembl; ENST00000261183; ENSP00000261183; ENSG00000091039.
DR Ensembl; ENST00000393249; ENSP00000376939; ENSG00000091039.
DR Ensembl; ENST00000393250; ENSP00000376940; ENSG00000091039.
DR GeneID; 114882; -.
DR KEGG; hsa:114882; -.
DR UCSC; uc001sye.1; human.
DR CTD; 114882; -.
DR GeneCards; GC12M076745; -.
DR HGNC; HGNC:16396; OSBPL8.
DR HPA; HPA001309; -.
DR MIM; 606736; gene.
DR neXtProt; NX_Q9BZF1; -.
DR PharmGKB; PA32832; -.
DR eggNOG; NOG262374; -.
DR HOVERGEN; HBG053375; -.
DR InParanoid; Q9BZF1; -.
DR OMA; TKDLYQP; -.
DR OrthoDB; EOG7D59MQ; -.
DR PhylomeDB; Q9BZF1; -.
DR ChiTaRS; OSBPL8; human.
DR EvolutionaryTrace; Q9BZF1; -.
DR GeneWiki; OSBPL8; -.
DR GenomeRNAi; 114882; -.
DR NextBio; 79363; -.
DR PMAP-CutDB; Q9BZF1; -.
DR PRO; PR:Q9BZF1; -.
DR ArrayExpress; Q9BZF1; -.
DR Bgee; Q9BZF1; -.
DR CleanEx; HS_OSBPL8; -.
DR Genevestigator; Q9BZF1; -.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0045444; P:fat cell differentiation; IDA:BHF-UCL.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:BHF-UCL.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Lipid transport; Lipid-binding; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1 889 Oxysterol-binding protein-related protein
FT 8.
FT /FTId=PRO_0000100378.
FT DOMAIN 148 265 PH.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 65 65 Phosphoserine.
FT MOD_RES 68 68 Phosphoserine.
FT MOD_RES 314 314 Phosphoserine.
FT MOD_RES 328 328 Phosphoserine.
FT MOD_RES 342 342 Phosphoserine.
FT MOD_RES 807 807 Phosphoserine.
FT MOD_RES 808 808 Phosphoserine.
FT MOD_RES 810 810 Phosphoserine.
FT MOD_RES 814 814 Phosphoserine.
FT VAR_SEQ 1 42 Missing (in isoform 3).
FT /FTId=VSP_045801.
FT VAR_SEQ 15 29 Missing (in isoform 2).
FT /FTId=VSP_009120.
FT CONFLICT 347 347 M -> V (in Ref. 5; CAH18345).
FT STRAND 151 157
FT STRAND 160 163
FT STRAND 165 172
FT STRAND 175 180
FT STRAND 182 184
FT STRAND 189 192
FT TURN 203 205
FT STRAND 209 213
FT STRAND 244 246
FT HELIX 250 264
SQ SEQUENCE 889 AA; 101196 MW; 79DB8055BD15FE95 CRC64;
MEGGLADGEP DRTSLLGDSK DVLGPSTVVA NSDESQLLTP GKMSQRQGKE AYPTPTKDLH
QPSLSPASPH SQGFERGKED ISQNKDESSL SMSKSKSESK LYNGSEKDSS TSSKLTKKES
LKVQKKNYRE EKKRATKELL STITDPSVIV MADWLKIRGT LKSWTKLWCV LKPGVLLIYK
TQKNGQWVGT VLLNACEIIE RPSKKDGFCF KLFHPLEQSI WAVKGPKGEA VGSITQPLPS
SYLIIRATSE SDGRCWMDAL ELALKCSSLL KRTMIREGKE HDLSVSSDST HVTFYGLLRA
NNLHSGDNFQ LNDSEIERQH FKDQDMYSDK SDKENDQEHD ESDNEVMGKS EESDTDTSER
QDDSYIEPEP VEPLKETTYT EQSHEELGEA GEASQTETVS EENKSLIWTL LKQVRPGMDL
SKVVLPTFIL EPRSFLDKLS DYYYHADFLS EAALEENPYF RLKKVVKWYL SGFYKKPKGL
KKPYNPILGE TFRCLWIHPR TNSKTFYIAE QVSHHPPISA FYVSNRKDGF CLSGSILAKS
KFYGNSLSAI LEGEARLTFL NRGEDYVMTM PYAHCKGILY GTMTLELGGT VNITCQKTGY
SAILEFKLKP FLGSSDCVNQ ISGKLKLGKE VLATLEGHWD SEVFITDKKT DNSEVFWNPT
PDIKQWRLIR HTVKFEEQGD FESEKLWQRV TRAINAKDQT EATQEKYVLE EAQRQAARDR
KTKNEEWSCK LFELDPLTGE WHYKFADTRP WDPLNDMIQF EKDGVIQTKV KHRTPMVSVP
KMKHKPTRQQ KKVAKGYSSP EPDIQDSSGS EAQSVKPSTR RKKGIELGDI QSSIESIKQT
QEEIKRNIMA LRNHLVSSTP ATDYFLQQKD YFIIFLLILL QVIINFMFK
//
MIM
606736
*RECORD*
*FIELD* NO
606736
*FIELD* TI
*606736 OXYSTEROL-BINDING PROTEIN-LIKE PROTEIN 8; OSBPL8
;;OSBP-RELATED PROTEIN 8; ORP8;;
read moreKIAA1451
*FIELD* TX
DESCRIPTION
OSBPL8 is a member of the OSBP family of intracellular lipid receptors.
For background information on OSBPs, see OSBP2 (606729).
CLONING
By screening for cDNAs with the potential to encode large proteins
expressed in brain, Nagase et al. (2000) identified a cDNA encoding
OSBPL8, which they called KIAA1451. The deduced 488-amino acid protein
was predicted to be 33% identical to mouse Osbp. RT-PCR analysis
detected wide expression that was strongest in testis, ovary, liver,
kidney, and brain. Within brain, expression was particularly strong in
caudate nucleus.
Lehto et al. (2001) used RT-PCR analysis with specific primers and
5-prime RACE to isolate a full-length cDNA encoding OSBPL8, which they
called ORP8. Sequence analysis predicted that the 847-amino acid protein
contains a C-terminal sterol-binding (SB) domain of approximately 400
residues that includes the OSBP motif (EQVSHHPP). It has a pleckstrin
homology (PH) domain in its N terminus. OSBPL8 is 78% and 88% identical
to OSBPL5 (606733) in the SB and PH domains, respectively.
Jaworski et al. (2001) cloned multiple OSBPs, including 2 variants of
OSBPL8 that encode proteins of 847 and 889 amino acids. RT-PCR analysis
detected ubiquitous expression that was strongest in brain, testis, and
fetal brain.
GENE STRUCTURE
By sequence analysis, Lehto et al. (2001) determined that the OSBPL8
gene contains 23 exons. Jaworski et al. (2001) also found that it
contains 23 exons.
MAPPING
By radiation hybrid analysis, Nagase et al. (2000) mapped the OSBPL8
gene to chromosome 12. By sequence analysis, Lehto et al. (2001) also
mapped the gene to chromosome 12. Jaworski et al. (2001) localized the
gene to 12p.
*FIELD* RF
1. 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.
2. 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.
3. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 143-150, 2000.
*FIELD* CD
Paul J. Converse: 2/28/2002
*FIELD* ED
mgross: 02/28/2002
*RECORD*
*FIELD* NO
606736
*FIELD* TI
*606736 OXYSTEROL-BINDING PROTEIN-LIKE PROTEIN 8; OSBPL8
;;OSBP-RELATED PROTEIN 8; ORP8;;
read moreKIAA1451
*FIELD* TX
DESCRIPTION
OSBPL8 is a member of the OSBP family of intracellular lipid receptors.
For background information on OSBPs, see OSBP2 (606729).
CLONING
By screening for cDNAs with the potential to encode large proteins
expressed in brain, Nagase et al. (2000) identified a cDNA encoding
OSBPL8, which they called KIAA1451. The deduced 488-amino acid protein
was predicted to be 33% identical to mouse Osbp. RT-PCR analysis
detected wide expression that was strongest in testis, ovary, liver,
kidney, and brain. Within brain, expression was particularly strong in
caudate nucleus.
Lehto et al. (2001) used RT-PCR analysis with specific primers and
5-prime RACE to isolate a full-length cDNA encoding OSBPL8, which they
called ORP8. Sequence analysis predicted that the 847-amino acid protein
contains a C-terminal sterol-binding (SB) domain of approximately 400
residues that includes the OSBP motif (EQVSHHPP). It has a pleckstrin
homology (PH) domain in its N terminus. OSBPL8 is 78% and 88% identical
to OSBPL5 (606733) in the SB and PH domains, respectively.
Jaworski et al. (2001) cloned multiple OSBPs, including 2 variants of
OSBPL8 that encode proteins of 847 and 889 amino acids. RT-PCR analysis
detected ubiquitous expression that was strongest in brain, testis, and
fetal brain.
GENE STRUCTURE
By sequence analysis, Lehto et al. (2001) determined that the OSBPL8
gene contains 23 exons. Jaworski et al. (2001) also found that it
contains 23 exons.
MAPPING
By radiation hybrid analysis, Nagase et al. (2000) mapped the OSBPL8
gene to chromosome 12. By sequence analysis, Lehto et al. (2001) also
mapped the gene to chromosome 12. Jaworski et al. (2001) localized the
gene to 12p.
*FIELD* RF
1. Jaworski, C. J.; Moreira, E.; Li, A.; Lee, R.; Rodriguez, I. R.
: A family of 12 human genes containing oxysterol-binding domains. Genomics 78:
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*FIELD* CD
Paul J. Converse: 2/28/2002
*FIELD* ED
mgross: 02/28/2002