OSBL6_MOUSE
ID OSBL6_MOUSE Reviewed; 959 AA.
AC Q8BXR9; Q8BYW2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Oxysterol-binding protein-related protein 6;
DE Short=ORP-6;
DE Short=OSBP-related protein 6;
GN Name=Osbpl6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Retina, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14593528; DOI=10.1007/s00441-003-0817-y;
RA Lehto M., Tienari J., Lehtonen S., Lehtonen E., Olkkonen V.M.;
RT "Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues:
RT the expression and intracellular localization of ORP3, ORP6, and ORP7.";
RL Cell Tissue Res. 315:39-57(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=26941018; DOI=10.1161/atvbaha.116.307282;
RA Ouimet M., Hennessy E.J., van Solingen C., Koelwyn G.J., Hussein M.A.,
RA Ramkhelawon B., Rayner K.J., Temel R.E., Perisic L., Hedin U.,
RA Maegdefessel L., Garabedian M.J., Holdt L.M., Teupser D., Moore K.J.;
RT "miRNA Targeting of Oxysterol-Binding Protein-Like 6 Regulates Cholesterol
RT Trafficking and Efflux.";
RL Arterioscler. Thromb. Vasc. Biol. 36:942-951(2016).
RN [5]
RP FUNCTION, SUBUNIT, INTERACTION WITH OSBPL3, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=30028970; DOI=10.1016/j.yexcr.2018.07.025;
RA Mochizuki S., Miki H., Zhou R., Kido Y., Nishimura W., Kikuchi M., Noda Y.;
RT "Oxysterol-binding protein-related protein (ORP) 6 localizes to the ER and
RT ER-plasma membrane contact sites and is involved in the turnover of PI4P in
RT cerebellar granule neurons.";
RL Exp. Cell Res. 370:601-612(2018).
CC -!- FUNCTION: Regulates cellular transport and efflux of cholesterol (By
CC similarity). Plays a role in phosphatidylinositol-4-phophate (PI4P)
CC turnover at the neuronal membrane (PubMed:30028970). Binds via its PH
CC domain PI4P, phosphatidylinositol-4,5-diphosphate,
CC phosphatidylinositol-3,4,5-triphosphate, and phosphatidic acid
CC (PubMed:30028970). Weakly binds 25-hydroxycholesterol (By similarity).
CC {ECO:0000250|UniProtKB:Q9BZF3, ECO:0000269|PubMed:30028970}.
CC -!- SUBUNIT: Homodimer (PubMed:30028970). Interacts with OSBPL3
CC (PubMed:30028970). {ECO:0000269|PubMed:30028970}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:14593528}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:14593528,
CC ECO:0000269|PubMed:30028970}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:30028970}; Peripheral
CC membrane protein {ECO:0000305}. Cell membrane
CC {ECO:0000269|PubMed:14593528}; Peripheral membrane protein
CC {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:30028970};
CC Peripheral membrane protein {ECO:0000305}. Note=Co-localizes with
CC OSBPL3 at contact sites between the plasma membrane and the endoplasmic
CC reticulum. {ECO:0000269|PubMed:30028970}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BXR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BXR9-2; Sequence=VSP_010012;
CC -!- TISSUE SPECIFICITY: Expressed in skin, respiratory epithelium, small
CC intestine epithelium, pancreas, striated muscle, brain, spinal ganglia,
CC and nervous plexus of the intestine (at protein level)
CC (PubMed:14593528, PubMed:30028970). In the brain, specifically in the
CC cerebellum, it is expressed in Purkinje and granule cells
CC (PubMed:30028970). Expressed in hepatocytes and macrophages
CC (PubMed:26941018). {ECO:0000269|PubMed:14593528,
CC ECO:0000269|PubMed:26941018, ECO:0000269|PubMed:30028970}.
CC -!- DEVELOPMENTAL STAGE: Detected in the brain at 18.5 days post coitum
CC (dpc), with expression increasing till it reaches its peak expression
CC at 28 dpc. {ECO:0000269|PubMed:30028970}.
CC -!- INDUCTION: By acetylated low-density lipoprotein and dietary intake of
CC cholesterols. {ECO:0000269|PubMed:26941018}.
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; AK037703; BAC29854.1; -; mRNA.
DR EMBL; AK044411; BAC31907.1; -; mRNA.
DR CCDS; CCDS71078.1; -. [Q8BXR9-1]
DR CCDS; CCDS71079.1; -. [Q8BXR9-2]
DR RefSeq; NP_001277662.1; NM_001290733.1. [Q8BXR9-1]
DR RefSeq; NP_001277663.1; NM_001290734.1. [Q8BXR9-2]
DR RefSeq; NP_663500.2; NM_145525.3.
DR RefSeq; XP_011238164.1; XM_011239862.2. [Q8BXR9-1]
DR AlphaFoldDB; Q8BXR9; -.
DR SMR; Q8BXR9; -.
DR BioGRID; 221173; 10.
DR IntAct; Q8BXR9; 1.
DR STRING; 10090.ENSMUSP00000077123; -.
DR iPTMnet; Q8BXR9; -.
DR PhosphoSitePlus; Q8BXR9; -.
DR MaxQB; Q8BXR9; -.
DR PaxDb; Q8BXR9; -.
DR PeptideAtlas; Q8BXR9; -.
DR PRIDE; Q8BXR9; -.
DR ProteomicsDB; 294113; -. [Q8BXR9-1]
DR ProteomicsDB; 294114; -. [Q8BXR9-2]
DR Antibodypedia; 33930; 134 antibodies from 23 providers.
DR DNASU; 99031; -.
DR Ensembl; ENSMUST00000111929; ENSMUSP00000107560; ENSMUSG00000042359. [Q8BXR9-1]
DR Ensembl; ENSMUST00000111930; ENSMUSP00000107561; ENSMUSG00000042359. [Q8BXR9-2]
DR GeneID; 99031; -.
DR KEGG; mmu:99031; -.
DR UCSC; uc008kfb.2; mouse. [Q8BXR9-1]
DR UCSC; uc008kfc.2; mouse. [Q8BXR9-2]
DR CTD; 114880; -.
DR MGI; MGI:2139014; Osbpl6.
DR VEuPathDB; HostDB:ENSMUSG00000042359; -.
DR eggNOG; KOG1737; Eukaryota.
DR GeneTree; ENSGT00940000156791; -.
DR HOGENOM; CLU_007105_4_1_1; -.
DR InParanoid; Q8BXR9; -.
DR OrthoDB; 542090at2759; -.
DR Reactome; R-MMU-192105; Synthesis of bile acids and bile salts.
DR BioGRID-ORCS; 99031; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Osbpl6; mouse.
DR PRO; PR:Q8BXR9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BXR9; protein.
DR Bgee; ENSMUSG00000042359; Expressed in nasal cavity and 232 other tissues.
DR ExpressionAtlas; Q8BXR9; baseline and differential.
DR Genevisible; Q8BXR9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; 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:0032374; P:regulation of cholesterol transport; ISO:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041680; PH_8.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF15409; PH_8; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW Endoplasmic reticulum; Endosome; Lipid transport; Lipid-binding; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BZF3"
FT CHAIN 2..959
FT /note="Oxysterol-binding protein-related protein 6"
FT /id="PRO_0000100376"
FT DOMAIN 86..181
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZF3"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZF3"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZF3"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZF3"
FT VAR_SEQ 299..329
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010012"
FT CONFLICT 796
FT /note="W -> L (in Ref. 1; BAC29854)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 959 AA; 108920 MW; 5D50B27C0065C361 CRC64;
MSSDEKGISP AHKTSTPTHR SASSSTSSQR ESRQSIHVLE RTASSSTEPS VSRQLLEPEP
IPLSKEADSW EIIEGLKIGQ TNVQKPDRHE GFMLKKRKWP LKGWHKRFFV LDNGMLKYSK
APLDIQKGKV HGSIDVGLSV MSIKKKARRI DLDTEEHIYH LKVKSQDWFD AWVSKLRHHR
LYRQNEIVRS PRDASFHIFP ATSTAESSPA ANVSVVDGKM QPNSFPWQSP LPCSNSLPAT
CTTGQSKVAA WLQDSEEMDR CAEDLAHCQS NLVELSKLLQ NLEILQRTQS APNFTDMQAN
CVDISKKDKR VTRRWRTKSV SKDTKIQLQE GPPAKGQFNT TRRRQRLAAA VATTVPFSAT
MSPVRLHSSN PNLCADIEFQ TPPSHLTDPL ESSTDYTKLQ EEFCLIAQKV HSLLKSAFNS
IAIEKEKLKQ VVSEQDHNKG HSTQMARLRQ SLSQALNQNA ELRSRLNRIH SESTICDHVV
SVNIIPSPDE PGEQIHVSLP LSQQVANESR LSMSESVSEF FDAQEVLLSA SSSENEASDD
ESYISDVSDN ISEDNTSVAD NISRQILNGE LTGGAFRNGR RTCLPAPCPD TSNINLWNIL
RNNIGKDLSK VSMPVELNEP LNTLQHLCEE MEYSELLDKA SETDDPYERM VLVAAFAVSG
YCSTYFRAGS KPFNPVLGET YECIREDKGF RFFSEQVSHH PPISACHCES KNFVFWQDIR
WKNKFWGKSM EILPVGTLNV TLPKYGDYYV WNKVTTCIHN ILSGRRWIEH YGEVTLRNTK
SSVCICKLTF VKVNYWNSNV NEVQGVVIDQ EGKVVHRLFG KWHEGLYCGV APSAKCIWRP
GSLPTNYELY YGFTRFAVEL NELDPVLKDL LPPTDARFRP DQRFLEEGNL EAAAAEKQRV
EELQRSRRRY MEENNLEHIP KFFKKVIDAN QREAWVSNDT YWELRKDPGF SKVDSPVLW
