RBCC

Full text data of OSBPL9

OSBPL9 (ORP9, OSBP4) [Confidence: low (only semi-automatic identification from reviews)]
Oxysterol-binding protein-related protein 9; ORP-9; OSBP-related protein 9

UniProt Q96SU4
ID OSBL9_HUMAN Reviewed; 736 AA.
AC Q96SU4; B1AKJ8; B3KPQ4; D3DQ31; Q5TFC0; Q6IA67; Q86YQ3; Q8NB17;
read moreAC Q8TAS8; Q96SK4; Q9H9X2;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 2.
DT 22-JAN-2014, entry version 101.
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;
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 [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.,
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 [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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Olkkonen V.M.;
RT "OSBP-related protein 11 (ORP11) dimerizes with ORP9 and localizes at
RT the 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.,
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 [12]
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.,
RA Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
RA Brunner H.G., 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.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane. Golgi apparatus,
CC trans-Golgi network membrane. Note=Localizes at the Golgi-late
CC 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 Note=No experimental confirmation available;
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 Note=No experimental confirmation available;
CC Name=7;
CC IsoId=Q96SU4-7; Sequence=VSP_043630;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the OSBP family.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH71119.1; Type=Erroneous initiation;
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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; AL772260; CAH71118.1; -; Genomic_DNA.
DR EMBL; AL050343; CAH71118.1; JOINED; Genomic_DNA.
DR EMBL; AL831767; CAH71118.1; JOINED; Genomic_DNA.
DR EMBL; AL772260; CAH71119.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL050343; CAH71119.1; JOINED; Genomic_DNA.
DR EMBL; AL831767; CAH71119.1; JOINED; Genomic_DNA.
DR EMBL; AL831767; CAI14843.1; -; Genomic_DNA.
DR EMBL; AL050343; CAI14843.1; JOINED; Genomic_DNA.
DR EMBL; AL772260; CAI14843.1; JOINED; Genomic_DNA.
DR EMBL; AL831767; CAI14844.1; -; Genomic_DNA.
DR EMBL; AL050343; CAI14844.1; JOINED; Genomic_DNA.
DR EMBL; AL772260; CAI14844.1; JOINED; Genomic_DNA.
DR EMBL; AL050343; CAI22219.1; -; Genomic_DNA.
DR EMBL; AL772260; CAI22219.1; JOINED; Genomic_DNA.
DR EMBL; AL831767; CAI22219.1; JOINED; Genomic_DNA.
DR EMBL; AL050343; CAI22220.1; -; Genomic_DNA.
DR EMBL; AL772260; CAI22220.1; JOINED; Genomic_DNA.
DR EMBL; AL831767; CAI22220.1; JOINED; Genomic_DNA.
DR EMBL; AL050343; CAI22221.1; -; 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 RefSeq; NP_078862.4; NM_024586.5.
DR RefSeq; NP_683702.1; NM_148904.3.
DR RefSeq; NP_683703.1; NM_148905.3.
DR RefSeq; NP_683704.2; NM_148906.2.
DR RefSeq; NP_683705.1; NM_148907.2.
DR RefSeq; NP_683706.3; NM_148908.3.
DR RefSeq; NP_683707.3; NM_148909.3.
DR UniGene; Hs.21938; -.
DR UniGene; Hs.738830; -.
DR ProteinModelPortal; Q96SU4; -.
DR SMR; Q96SU4; 7-96, 369-731.
DR IntAct; Q96SU4; 14.
DR STRING; 9606.ENSP00000337265; -.
DR PhosphoSite; Q96SU4; -.
DR DMDM; 20139075; -.
DR PaxDb; Q96SU4; -.
DR PRIDE; Q96SU4; -.
DR Ensembl; ENST00000361556; ENSP00000354970; ENSG00000117859.
DR Ensembl; ENST00000371714; ENSP00000360779; ENSG00000117859.
DR Ensembl; ENST00000428468; ENSP00000407168; ENSG00000117859.
DR Ensembl; ENST00000435686; ENSP00000402646; ENSG00000117859.
DR Ensembl; ENST00000447887; ENSP00000412733; ENSG00000117859.
DR Ensembl; ENST00000453295; ENSP00000413263; ENSG00000117859.
DR Ensembl; ENST00000462759; ENSP00000433279; ENSG00000117859.
DR Ensembl; ENST00000486942; ENSP00000431980; ENSG00000117859.
DR Ensembl; ENST00000531828; ENSP00000433083; ENSG00000117859.
DR GeneID; 114883; -.
DR KEGG; hsa:114883; -.
DR UCSC; uc001cst.4; human.
DR CTD; 114883; -.
DR GeneCards; GC01P052042; -.
DR HGNC; HGNC:16386; OSBPL9.
DR HPA; HPA027378; -.
DR HPA; HPA027397; -.
DR MIM; 606737; gene.
DR neXtProt; NX_Q96SU4; -.
DR PharmGKB; PA32833; -.
DR eggNOG; NOG262374; -.
DR HOGENOM; HOG000233872; -.
DR HOVERGEN; HBG053376; -.
DR OrthoDB; EOG7PK8ZG; -.
DR ChiTaRS; OSBPL9; human.
DR GeneWiki; OSBPL9; -.
DR GenomeRNAi; 114883; -.
DR NextBio; 79369; -.
DR PRO; PR:Q96SU4; -.
DR ArrayExpress; Q96SU4; -.
DR Bgee; Q96SU4; -.
DR CleanEx; HS_OSBPL9; -.
DR Genevestigator; Q96SU4; -.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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 Acetylation; Alternative splicing; Complete proteome; Endosome;
KW Golgi apparatus; Lipid transport; Lipid-binding; Membrane;
KW Polymorphism; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 736 Oxysterol-binding protein-related protein
FT 9.
FT /FTId=PRO_0000100379.
FT DOMAIN 2 99 PH.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 165 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_036779.
FT VAR_SEQ 1 97 Missing (in isoform 3).
FT /FTId=VSP_036780.
FT VAR_SEQ 38 54 Missing (in isoform 7).
FT /FTId=VSP_043630.
FT VAR_SEQ 98 106 ILRHTLQLQ -> MAFLLATCG (in isoform 3).
FT /FTId=VSP_036781.
FT VAR_SEQ 106 106 Q -> QISTTLAFFQSSGISPVLEFSKII (in isoform
FT 6).
FT /FTId=VSP_043631.
FT VAR_SEQ 182 194 Missing (in isoform 2, isoform 3, isoform
FT 5 and isoform 6).
FT /FTId=VSP_003782.
FT VARIANT 266 266 P -> L.
FT /FTId=VAR_069380.
FT CONFLICT 295 295 F -> L (in Ref. 3; BAC03727).
FT CONFLICT 735 735 K -> R (in Ref. 3; BAB55312).
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
//

MIM 606737
*RECORD*
*FIELD* NO
606737
*FIELD* TI
*606737 OXYSTEROL-BINDING PROTEIN-LIKE PROTEIN 9; OSBPL9
;;OSBP-RELATED PROTEIN 9; ORP9
read more*FIELD* TX

DESCRIPTION

OSBPL9 is a member of the OSBP family of intracellular lipid receptors.
For background information on OSBPs, see OSBP2 (606729).

CLONING

Lehto et al. (2001) used database searching to identify a cDNA encoding
OSBPL9, which they called ORP9. Sequence analysis predicted that the
558-amino acid protein contains a C-terminal sterol-binding (SB) domain
of approximately 400 residues that includes the OSBP motif (EQVSHHPP).
OSBPL9 appears to be in a distinct OSBP subfamily and shares relatively
little homology in the SB domain with other OSBPs. Gene expression
database analysis indicated highest expression in brain and spleen,
followed by heart, skeletal muscle, placenta, and testis.

Jaworski et al. (2001) cloned multiple OSBPs, including OSBPL9, which
encodes a 737-amino acid protein that has an N-terminal pleckstrin
homology (PH) domain. RT-PCR analysis detected ubiquitous expression
that was highest in retinal pigment epithelium and choroid.

Using the vesicle membrane-associated protein VAPA (605703) as bait in a
yeast 2-hybrid screen of a human B cell cDNA library, and by PCR of a
human kidney cDNA library, Wyles and Ridgway (2004) cloned 2 splice
variants of OSBPL9, which they designated ORP9L and ORP9S. Full-length
ORP9L contains 723 amino acids and has a calculated molecular mass of 81
kD, whereas ORP9S contains 558 amino acids and has a calculated
molecular mass of 63 kD. ORP9S lacks the N-terminal PH domain of ORP9L;
however, both proteins contain a VAP-binding motif and C-terminal OSBP
homology domain. Northern blot analysis detected a major 3-kb transcript
highly expressed in heart, skeletal muscle, kidney, and liver, with
weaker expression in brain, spleen, placenta, and lung. PCR analysis
with variant-specific primers revealed variable and uncoordinated
expression of both ORP9S and ORP9L in most tissues, with coexpression in
lung, liver, and placenta. Confocal and immunofluorescence microscopy
revealed ORP9L concentrated in the perinuclear Golgi apparatus, with
some diffuse cytoplasmic staining. Western blot analysis detected ORP9L
at an apparent molecular mass of 95 kD in brain, heart, kidney, and
liver, and detected ORP9S at an apparent mass of 70-to-75 kD only in
liver.

GENE FUNCTION

Using yeast 2-hybrid and protein pull-down assays, Wyles and Ridgway
(2004) showed that VAPA interacted with both ORP9L and ORP9S. Mutation
analysis revealed that the interactions required a conserved N-terminal
motif in VAPA and the VAP-binding regions of ORP9S and ORP9S.
Coimmunoprecipitation analysis revealed that antibody directed against
ORP9 pulled down VAPB (605704) in addition to VAPA. Overexpressed ORP9L
colocalized with Vapa in Chinese hamster ovary cells and caused dramatic
reorganization and/or vacuolation of the endoplasmic reticulum (ER) and
ER-Golgi intermediate compartment; these effects required the
interaction of ORP9L with VAPA via its VAP-binding domain.
Overexpression of ORP9S showed much weaker disruption of these
compartments.

Using knockdown and overexpression studies, Ngo and Ridgway (2009)
showed that ORP9L partitioned between the trans-Golgi/trans-Golgi
network (TGN) and the ER, and it location dependent on its PH domain and
VAP-binding domain. The PH domain of ORP9L predominantly bound
phosphatidylinositol 4-phosphate (PtdIns(4)P) in lipid overlay assays,
and ORP9L mediated PtdIns(4)P-dependent cholesterol transport between
liposomes in vitro. Depletion of ORP9L via RNA interference caused Golgi
fragmentation, inhibition of vesicle transport from the ER, and
accumulation of cholesterol in endosomes/lysosomes. ORP9S, lacking the
PH domain, behaved as a dominant-negative variant, and its
overexpression caused complete cessation of protein transport and
inhibition of cell growth. Ngo and Ridgway (2009) concluded that ORP9
maintains the integrity of the early secretory pathway by mediating
transport of sterols between the ER and trans-Golgi/TGN.

GENE STRUCTURE

By sequence analysis, Lehto et al. (2001) determined that the OSBPL9
gene contains 19 exons. Jaworski et al. (2001) found that it contains at
least 22 exons.

Wyles and Ridgway (2004) determined that the OSBPL9 gene contains 24
exons, including an alternative exon located between exon 4 and exon 5,
which they termed 'exon 5-prime.' The ORP9S transcript results from
splicing of 'exon 5-prime' to exon 6 and is predicted to result in
translation initiation exon 8.

MAPPING

By sequence analysis, Lehto et al. (2001) mapped the OSBPL9 gene to
chromosome 1. Jaworski et al. (2001) refined the localization to
chromosome 1p34.2-p32.2.

*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. Ngo, M.; Ridgway, N. D.: Oxysterol binding protein-related protein
9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure
and function. Molec. Biol. Cell 20: 1388-1399, 2009.

4. Wyles, J. P.; Ridgway, N. D.: VAMP-associated protein-A regulates
partitioning of oxysterol-binding protein-related protein-9 between
the endoplasmic reticulum and Golgi apparatus. Exp. Cell Res. 297:
533-547, 2004.

*FIELD* CN
Patricia A. Hartz - updated: 8/20/2010

*FIELD* CD
Paul J. Converse: 2/28/2002

*FIELD* ED
wwang: 09/16/2010
terry: 8/20/2010
mgross: 2/28/2002

RBCC Red Blood Cell Collection

Full text data of OSBPL9