Full text data of OSBP2
OSBP2
(KIAA1664, ORP4, OSBPL4)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Oxysterol-binding protein 2 (Oxysterol-binding protein-related protein 4; ORP-4; OSBP-related protein 4)
Oxysterol-binding protein 2 (Oxysterol-binding protein-related protein 4; ORP-4; OSBP-related protein 4)
UniProt
Q969R2
ID OSBP2_HUMAN Reviewed; 916 AA.
AC Q969R2; B0QYG1; O60396; Q9BY96; Q9BZF0;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-FEB-2006, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Oxysterol-binding protein 2;
DE AltName: Full=Oxysterol-binding protein-related protein 4;
DE Short=ORP-4;
DE Short=OSBP-related protein 4;
GN Name=OSBP2; Synonyms=KIAA1664, ORP4, OSBPL4;
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 [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] OF
RP 2-916, AND TISSUE SPECIFICITY.
RX PubMed=11278871; DOI=10.1074/jbc.M011259200;
RA Moreira E.F., Jaworski C., Li A., Rodriguez I.R.;
RT "Molecular and biochemical characterization of a novel oxysterol-
RT binding protein (OSBP2) highly expressed in retina.";
RL J. Biol. Chem. 276:18570-18578(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT "Identification of novel transcribed sequences on human chromosome 22
RT by expressed sequence tag mapping.";
RL DNA Res. 8:1-9(2001).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
CC -!- FUNCTION: Binds 7-ketocholesterol.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed mainly in retina, testis, and fetal
CC liver.
CC -!- SIMILARITY: Belongs to the OSBP family.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK56864.1; Type=Erroneous initiation;
CC Sequence=AAK56865.1; Type=Erroneous initiation;
CC Sequence=BAB33334.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF288741; AAK56864.1; ALT_INIT; mRNA.
DR EMBL; AF288742; AAK56865.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF323731; AAG53406.1; -; mRNA.
DR EMBL; AB051451; BAB33334.2; ALT_INIT; mRNA.
DR EMBL; AC004542; AAC12953.1; -; Genomic_DNA.
DR EMBL; AL079299; CAQ07396.1; -; Genomic_DNA.
DR EMBL; AC004542; CAQ07396.1; JOINED; Genomic_DNA.
DR EMBL; AL022336; CAQ07396.1; JOINED; Genomic_DNA.
DR EMBL; AL022336; CAQ07892.1; -; Genomic_DNA.
DR EMBL; AC004542; CAQ07892.1; JOINED; Genomic_DNA.
DR EMBL; AL079299; CAQ07892.1; JOINED; Genomic_DNA.
DR EMBL; CH471095; EAW59916.1; -; Genomic_DNA.
DR PIR; T02435; T02435.
DR RefSeq; NP_001269667.1; NM_001282738.1.
DR RefSeq; NP_001269668.1; NM_001282739.1.
DR RefSeq; NP_001269669.1; NM_001282740.1.
DR RefSeq; NP_001269670.1; NM_001282741.1.
DR RefSeq; NP_001269671.1; NM_001282742.1.
DR RefSeq; NP_110385.1; NM_030758.3.
DR UniGene; Hs.517546; -.
DR ProteinModelPortal; Q969R2; -.
DR SMR; Q969R2; 187-273, 518-767.
DR IntAct; Q969R2; 2.
DR MINT; MINT-6942148; -.
DR STRING; 9606.ENSP00000332576; -.
DR PhosphoSite; Q969R2; -.
DR DMDM; 88984633; -.
DR PaxDb; Q969R2; -.
DR PRIDE; Q969R2; -.
DR Ensembl; ENST00000332585; ENSP00000332576; ENSG00000184792.
DR GeneID; 23762; -.
DR KEGG; hsa:23762; -.
DR UCSC; uc003aiy.1; human.
DR CTD; 23762; -.
DR GeneCards; GC22P031089; -.
DR H-InvDB; HIX0041322; -.
DR HGNC; HGNC:8504; OSBP2.
DR HPA; HPA021514; -.
DR MIM; 606729; gene.
DR neXtProt; NX_Q969R2; -.
DR PharmGKB; PA32823; -.
DR eggNOG; NOG281324; -.
DR HOGENOM; HOG000231233; -.
DR HOVERGEN; HBG053374; -.
DR OMA; KIPSESG; -.
DR GeneWiki; OSBP2; -.
DR GenomeRNAi; 23762; -.
DR NextBio; 46715; -.
DR PRO; PR:Q969R2; -.
DR ArrayExpress; Q969R2; -.
DR Bgee; Q969R2; -.
DR CleanEx; HS_OSBP2; -.
DR Genevestigator; Q969R2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
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 Complete proteome; Lipid transport; Lipid-binding; Membrane;
KW Polymorphism; Reference proteome; Transport.
FT CHAIN 1 916 Oxysterol-binding protein 2.
FT /FTId=PRO_0000100366.
FT DOMAIN 182 274 PH.
FT VARIANT 760 760 M -> V (in dbSNP:rs34240867).
FT /FTId=VAR_053546.
FT CONFLICT 34 34 T -> A (in Ref. 3; BAB33334).
SQ SEQUENCE 916 AA; 101266 MW; 3EAC49EB56516F18 CRC64;
MGKAAAPSRG GGCGGRSRGL SSLFTVVPCL SCHTAAPGMS ASTSGSGPEP KPQPQPVPEP
ERGPLSEQVS EAVSEAVPRS EPVSETTSEP EPGAGQPSEL LQGSRPGSES SSGVGAGPFT
KAASEPLSRA VGSATFLRPE SGSLPALKPL PLLRPGQAKT PLGVPMSGTG TTSSAPLALL
PLDSFEGWLL KWTNYLKGYQ RRWFVLGNGL LSYYRNQGEM AHTCRGTINL STAHIDTEDS
CGILLTSGAR SYHLKASSEV DRQQWITALE LAKAKAVRVM NTHSDDSGDD DEATTPADKS
ELHHTLKNLS LKLDDLSTCN DLIAKHGAAL QRSLTELDGL KIPSESGEKL KVVNERATLF
RITSNAMINA CRDFLELAEI HSRKWQRALQ YEQEQRVHLE ETIEQLAKQH NSLERAFHSA
PGRPANPSKS FIEGSLLTPK GEDSEEDEDT EYFDAMEDST SFITVITEAK EDSRKAEGST
GTSSVDWSSA DNVLDGASLV PKGSSKVKRR VRIPNKPNYS LNLWSIMKNC IGRELSRIPM
PVNFNEPLSM LQRLTEDLEY HHLLDKAVHC TSSVEQMCLV AAFSVSSYST TVHRIAKPFN
PMLGETFELD RLDDMGLRSL CEQVSHHPPS AAHYVFSKHG WSLWQEITIS SKFRGKYISI
MPLGAIHLEF QASGNHYVWR KSTSTVHNII VGKLWIDQSG DIEIVNHKTN DRCQLKFLPY
SYFSKEAARK VTGVVSDSQG KAHYVLSGSW DEQMECSKVM HSSPSSPSSD GKQKTVYQTL
SAKLLWKKYP LPENAENMYY FSELALTLNE HEEGVAPTDS RLRPDQRLME KGRWDEANTE
KQRLEEKQRL SRRRRLEACG PGSSCSSEEE KEADAYTPLW FEKRLDPLTG EMACVYKGGY
WEAKEKQDWH MCPNIF
//
ID OSBP2_HUMAN Reviewed; 916 AA.
AC Q969R2; B0QYG1; O60396; Q9BY96; Q9BZF0;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-FEB-2006, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Oxysterol-binding protein 2;
DE AltName: Full=Oxysterol-binding protein-related protein 4;
DE Short=ORP-4;
DE Short=OSBP-related protein 4;
GN Name=OSBP2; Synonyms=KIAA1664, ORP4, OSBPL4;
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 [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] OF
RP 2-916, AND TISSUE SPECIFICITY.
RX PubMed=11278871; DOI=10.1074/jbc.M011259200;
RA Moreira E.F., Jaworski C., Li A., Rodriguez I.R.;
RT "Molecular and biochemical characterization of a novel oxysterol-
RT binding protein (OSBP2) highly expressed in retina.";
RL J. Biol. Chem. 276:18570-18578(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT "Identification of novel transcribed sequences on human chromosome 22
RT by expressed sequence tag mapping.";
RL DNA Res. 8:1-9(2001).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
CC -!- FUNCTION: Binds 7-ketocholesterol.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed mainly in retina, testis, and fetal
CC liver.
CC -!- SIMILARITY: Belongs to the OSBP family.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK56864.1; Type=Erroneous initiation;
CC Sequence=AAK56865.1; Type=Erroneous initiation;
CC Sequence=BAB33334.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF288741; AAK56864.1; ALT_INIT; mRNA.
DR EMBL; AF288742; AAK56865.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF323731; AAG53406.1; -; mRNA.
DR EMBL; AB051451; BAB33334.2; ALT_INIT; mRNA.
DR EMBL; AC004542; AAC12953.1; -; Genomic_DNA.
DR EMBL; AL079299; CAQ07396.1; -; Genomic_DNA.
DR EMBL; AC004542; CAQ07396.1; JOINED; Genomic_DNA.
DR EMBL; AL022336; CAQ07396.1; JOINED; Genomic_DNA.
DR EMBL; AL022336; CAQ07892.1; -; Genomic_DNA.
DR EMBL; AC004542; CAQ07892.1; JOINED; Genomic_DNA.
DR EMBL; AL079299; CAQ07892.1; JOINED; Genomic_DNA.
DR EMBL; CH471095; EAW59916.1; -; Genomic_DNA.
DR PIR; T02435; T02435.
DR RefSeq; NP_001269667.1; NM_001282738.1.
DR RefSeq; NP_001269668.1; NM_001282739.1.
DR RefSeq; NP_001269669.1; NM_001282740.1.
DR RefSeq; NP_001269670.1; NM_001282741.1.
DR RefSeq; NP_001269671.1; NM_001282742.1.
DR RefSeq; NP_110385.1; NM_030758.3.
DR UniGene; Hs.517546; -.
DR ProteinModelPortal; Q969R2; -.
DR SMR; Q969R2; 187-273, 518-767.
DR IntAct; Q969R2; 2.
DR MINT; MINT-6942148; -.
DR STRING; 9606.ENSP00000332576; -.
DR PhosphoSite; Q969R2; -.
DR DMDM; 88984633; -.
DR PaxDb; Q969R2; -.
DR PRIDE; Q969R2; -.
DR Ensembl; ENST00000332585; ENSP00000332576; ENSG00000184792.
DR GeneID; 23762; -.
DR KEGG; hsa:23762; -.
DR UCSC; uc003aiy.1; human.
DR CTD; 23762; -.
DR GeneCards; GC22P031089; -.
DR H-InvDB; HIX0041322; -.
DR HGNC; HGNC:8504; OSBP2.
DR HPA; HPA021514; -.
DR MIM; 606729; gene.
DR neXtProt; NX_Q969R2; -.
DR PharmGKB; PA32823; -.
DR eggNOG; NOG281324; -.
DR HOGENOM; HOG000231233; -.
DR HOVERGEN; HBG053374; -.
DR OMA; KIPSESG; -.
DR GeneWiki; OSBP2; -.
DR GenomeRNAi; 23762; -.
DR NextBio; 46715; -.
DR PRO; PR:Q969R2; -.
DR ArrayExpress; Q969R2; -.
DR Bgee; Q969R2; -.
DR CleanEx; HS_OSBP2; -.
DR Genevestigator; Q969R2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
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 Complete proteome; Lipid transport; Lipid-binding; Membrane;
KW Polymorphism; Reference proteome; Transport.
FT CHAIN 1 916 Oxysterol-binding protein 2.
FT /FTId=PRO_0000100366.
FT DOMAIN 182 274 PH.
FT VARIANT 760 760 M -> V (in dbSNP:rs34240867).
FT /FTId=VAR_053546.
FT CONFLICT 34 34 T -> A (in Ref. 3; BAB33334).
SQ SEQUENCE 916 AA; 101266 MW; 3EAC49EB56516F18 CRC64;
MGKAAAPSRG GGCGGRSRGL SSLFTVVPCL SCHTAAPGMS ASTSGSGPEP KPQPQPVPEP
ERGPLSEQVS EAVSEAVPRS EPVSETTSEP EPGAGQPSEL LQGSRPGSES SSGVGAGPFT
KAASEPLSRA VGSATFLRPE SGSLPALKPL PLLRPGQAKT PLGVPMSGTG TTSSAPLALL
PLDSFEGWLL KWTNYLKGYQ RRWFVLGNGL LSYYRNQGEM AHTCRGTINL STAHIDTEDS
CGILLTSGAR SYHLKASSEV DRQQWITALE LAKAKAVRVM NTHSDDSGDD DEATTPADKS
ELHHTLKNLS LKLDDLSTCN DLIAKHGAAL QRSLTELDGL KIPSESGEKL KVVNERATLF
RITSNAMINA CRDFLELAEI HSRKWQRALQ YEQEQRVHLE ETIEQLAKQH NSLERAFHSA
PGRPANPSKS FIEGSLLTPK GEDSEEDEDT EYFDAMEDST SFITVITEAK EDSRKAEGST
GTSSVDWSSA DNVLDGASLV PKGSSKVKRR VRIPNKPNYS LNLWSIMKNC IGRELSRIPM
PVNFNEPLSM LQRLTEDLEY HHLLDKAVHC TSSVEQMCLV AAFSVSSYST TVHRIAKPFN
PMLGETFELD RLDDMGLRSL CEQVSHHPPS AAHYVFSKHG WSLWQEITIS SKFRGKYISI
MPLGAIHLEF QASGNHYVWR KSTSTVHNII VGKLWIDQSG DIEIVNHKTN DRCQLKFLPY
SYFSKEAARK VTGVVSDSQG KAHYVLSGSW DEQMECSKVM HSSPSSPSSD GKQKTVYQTL
SAKLLWKKYP LPENAENMYY FSELALTLNE HEEGVAPTDS RLRPDQRLME KGRWDEANTE
KQRLEEKQRL SRRRRLEACG PGSSCSSEEE KEADAYTPLW FEKRLDPLTG EMACVYKGGY
WEAKEKQDWH MCPNIF
//
MIM
606729
*RECORD*
*FIELD* NO
606729
*FIELD* TI
*606729 OXYSTEROL-BINDING PROTEIN 2; OSBP2
;;OSBP-RELATED PROTEIN 4; ORP4;;
KIAA1664
read more*FIELD* TX
DESCRIPTION
Oxysterols accumulate in tissues and exert pharmacologic effects on
cellular sterol biosynthesis and uptake. They are oxidized byproducts of
cholesterol that cause cytotoxic effects on a variety of cells.
Oxysterol-binding proteins such as OSBP1 (167040) and OSBP2 may mediate
oxysterol cytotoxicity in tissues.
CLONING
By database searching for sequences similar to OSBP1, followed by
probing a retina library and 5-prime and 3-prime RACE, Moreira et al.
(2001) obtained a cDNA encoding OSPBP2. Sequence analysis predicted that
the 878-amino acid protein, which is 63% identical to OSBP1, contains an
N-terminal pleckstrin homology domain, an oxysterol-binding domain, and
a conserved C terminus.
By Northern blot analysis, Moreira et al. (2001) detected expression of
a predominant 2.7-kb OSBP2 transcript mainly in retina, pineal gland,
and fetal liver, and a 4.2-kb transcript that was most abundant in
testis and cerebellum. In contrast, OSBP1 was more widely expressed.
RT-PCR analysis detected expression of an OSBP2 splice variant that
lacks exon 12, resulting in a protein with an aberrant C terminus after
the first 692 amino acids, only in retina. In monkey retina, significant
expression of OSBP2 was found in neural macula and peripheral neural
retina, with little or no expression in macular or peripheral pigment
epithelium choroids. OSBP1, on the other hand, was expressed
equivalently in all but the peripheral pigment epithelium choroid.
Western blot analysis showed expression of a 90-kD OSBP2 protein
associated with retinal membranes. Immunocytochemical analysis
demonstrated expression of OSBP2 in monkey retinal ganglion cells
distinct from those expressing OSBP1, and in retinal pigment epithelium,
where the low density lipoprotein receptor (606945) is expressed.
Moreira et al. (2001) concluded that OSBPs and their oxysterol ligands,
which accumulate gradually with age, may play an important role in the
pathogenesis of age-related ocular diseases, such as macular
degeneration.
GENE FUNCTION
Using binding analysis, Moreira et al. (2001) showed that OSBP2
interacts preferentially with 7-ketocholesterol.
GENE STRUCTURE
By genomic sequence analysis, Moreira et al. (2001) determined that the
OSBP2 gene contains 14 exons, like OSBP1, and spans 217 kb.
MAPPING
By sequence analysis, Moreira et al. (2001) mapped the OSBP2 gene to
chromosome 22q12.
*FIELD* RF
1. Moreira, E. F.; Jaworski, C.; Li, A.; Rodriguez, I. R.: Molecular
and biochemical characterization of a novel oxysterol-binding protein
(OSBP2) highly expressed in retina. J. Biol. Chem. 276: 18570-18578,
2001.
*FIELD* CD
Paul J. Converse: 2/28/2002
*FIELD* ED
ckniffin: 06/05/2002
mgross: 2/28/2002
*RECORD*
*FIELD* NO
606729
*FIELD* TI
*606729 OXYSTEROL-BINDING PROTEIN 2; OSBP2
;;OSBP-RELATED PROTEIN 4; ORP4;;
KIAA1664
read more*FIELD* TX
DESCRIPTION
Oxysterols accumulate in tissues and exert pharmacologic effects on
cellular sterol biosynthesis and uptake. They are oxidized byproducts of
cholesterol that cause cytotoxic effects on a variety of cells.
Oxysterol-binding proteins such as OSBP1 (167040) and OSBP2 may mediate
oxysterol cytotoxicity in tissues.
CLONING
By database searching for sequences similar to OSBP1, followed by
probing a retina library and 5-prime and 3-prime RACE, Moreira et al.
(2001) obtained a cDNA encoding OSPBP2. Sequence analysis predicted that
the 878-amino acid protein, which is 63% identical to OSBP1, contains an
N-terminal pleckstrin homology domain, an oxysterol-binding domain, and
a conserved C terminus.
By Northern blot analysis, Moreira et al. (2001) detected expression of
a predominant 2.7-kb OSBP2 transcript mainly in retina, pineal gland,
and fetal liver, and a 4.2-kb transcript that was most abundant in
testis and cerebellum. In contrast, OSBP1 was more widely expressed.
RT-PCR analysis detected expression of an OSBP2 splice variant that
lacks exon 12, resulting in a protein with an aberrant C terminus after
the first 692 amino acids, only in retina. In monkey retina, significant
expression of OSBP2 was found in neural macula and peripheral neural
retina, with little or no expression in macular or peripheral pigment
epithelium choroids. OSBP1, on the other hand, was expressed
equivalently in all but the peripheral pigment epithelium choroid.
Western blot analysis showed expression of a 90-kD OSBP2 protein
associated with retinal membranes. Immunocytochemical analysis
demonstrated expression of OSBP2 in monkey retinal ganglion cells
distinct from those expressing OSBP1, and in retinal pigment epithelium,
where the low density lipoprotein receptor (606945) is expressed.
Moreira et al. (2001) concluded that OSBPs and their oxysterol ligands,
which accumulate gradually with age, may play an important role in the
pathogenesis of age-related ocular diseases, such as macular
degeneration.
GENE FUNCTION
Using binding analysis, Moreira et al. (2001) showed that OSBP2
interacts preferentially with 7-ketocholesterol.
GENE STRUCTURE
By genomic sequence analysis, Moreira et al. (2001) determined that the
OSBP2 gene contains 14 exons, like OSBP1, and spans 217 kb.
MAPPING
By sequence analysis, Moreira et al. (2001) mapped the OSBP2 gene to
chromosome 22q12.
*FIELD* RF
1. Moreira, E. F.; Jaworski, C.; Li, A.; Rodriguez, I. R.: Molecular
and biochemical characterization of a novel oxysterol-binding protein
(OSBP2) highly expressed in retina. J. Biol. Chem. 276: 18570-18578,
2001.
*FIELD* CD
Paul J. Converse: 2/28/2002
*FIELD* ED
ckniffin: 06/05/2002
mgross: 2/28/2002