OSBL2_MOUSE
ID OSBL2_MOUSE Reviewed; 484 AA.
AC Q8BX94; Q3TCK8; Q8R0H8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Oxysterol-binding protein-related protein 2;
DE Short=ORP-2;
DE Short=OSBP-related protein 2;
GN Name=Osbpl2;
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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.
RX PubMed=25759012; DOI=10.1186/s13023-015-0238-5;
RA Thoenes M., Zimmermann U., Ebermann I., Ptok M., Lewis M.A., Thiele H.,
RA Morlot S., Hess M.M., Gal A., Eisenberger T., Bergmann C., Nuernberg G.,
RA Nuernberg P., Steel K.P., Knipper M., Bolz H.J.;
RT "OSBPL2 encodes a protein of inner and outer hair cell stereocilia and is
RT mutated in autosomal dominant hearing loss (DFNA67).";
RL Orphanet J. Rare Dis. 10:15-15(2015).
CC -!- FUNCTION: Intracellular transport protein that binds sterols and
CC phospholipids and mediates lipid transport between intracellular
CC compartments. Increases plasma membrane cholesterol levels and
CC decreases phosphatidylinositol-4,5-bisphosphate levels in the cell
CC membrane. Binds phosphoinositides, such as phosphatidylinositol-4,5-
CC bisphosphate. Exhibits strong binding to phosphatidic acid and weak
CC binding to phosphatidylinositol 3-phosphate. Binds cholesterol,
CC dehydroergosterol, 22(R)-hydroxycholesterol and 25-hydroxycholesterol
CC (in vitro). {ECO:0000250|UniProtKB:Q9H1P3}.
CC -!- SUBUNIT: Monomer. Homotetramer; phosphatidylinositol-4,5-bisphosphate
CC binding promotes formation of stable tetramers. Interacts with DIAPH1.
CC {ECO:0000250|UniProtKB:Q9H1P3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9H1P3}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q9H1P3}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9H1P3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H1P3}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H1P3}. Note=Detected on the surface of
CC cytosolic lipid droplets. Recruited to the cell membrane by
CC phosphatidylinositol-phosphate binding. {ECO:0000250|UniProtKB:Q9H1P3}.
CC -!- TISSUE SPECIFICITY: Detected in cochlea, in inner and outer hair cells
CC in the organ of Corti (at protein level).
CC {ECO:0000269|PubMed:25759012}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
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DR EMBL; AK048537; BAC33367.1; -; mRNA.
DR EMBL; AK170669; BAE41948.1; -; mRNA.
DR EMBL; BC026804; AAH26804.1; -; mRNA.
DR CCDS; CCDS17170.1; -.
DR RefSeq; NP_653083.2; NM_144500.3.
DR RefSeq; XP_017173482.1; XM_017317993.1.
DR AlphaFoldDB; Q8BX94; -.
DR SMR; Q8BX94; -.
DR STRING; 10090.ENSMUSP00000046538; -.
DR PhosphoSitePlus; Q8BX94; -.
DR EPD; Q8BX94; -.
DR MaxQB; Q8BX94; -.
DR PaxDb; Q8BX94; -.
DR PRIDE; Q8BX94; -.
DR ProteomicsDB; 294112; -.
DR Antibodypedia; 29467; 195 antibodies from 32 providers.
DR DNASU; 228983; -.
DR Ensembl; ENSMUST00000040668; ENSMUSP00000046538; ENSMUSG00000039050.
DR GeneID; 228983; -.
DR KEGG; mmu:228983; -.
DR UCSC; uc008oik.1; mouse.
DR CTD; 9885; -.
DR MGI; MGI:2442832; Osbpl2.
DR VEuPathDB; HostDB:ENSMUSG00000039050; -.
DR eggNOG; KOG2209; Eukaryota.
DR GeneTree; ENSGT00940000158762; -.
DR HOGENOM; CLU_007105_6_2_1; -.
DR InParanoid; Q8BX94; -.
DR OMA; AHSAKMY; -.
DR OrthoDB; 863978at2759; -.
DR PhylomeDB; Q8BX94; -.
DR Reactome; R-MMU-192105; Synthesis of bile acids and bile salts.
DR BioGRID-ORCS; 228983; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Osbpl2; mouse.
DR PRO; PR:Q8BX94; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BX94; protein.
DR Bgee; ENSMUSG00000039050; Expressed in urinary bladder urothelium and 244 other tissues.
DR Genevisible; Q8BX94; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; ISO:MGI.
DR GO; GO:0120020; F:cholesterol transfer activity; ISS:UniProtKB.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0030301; P:cholesterol transport; ISO:MGI.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISS:UniProtKB.
DR GO; GO:0015914; P:phospholipid transport; ISO:MGI.
DR GO; GO:0007009; P:plasma membrane organization; ISO:MGI.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR PROSITE; PS01013; OSBP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Lipid droplet; Lipid transport; Lipid-binding;
KW Membrane; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..484
FT /note="Oxysterol-binding protein-related protein 2"
FT /id="PRO_0000100370"
FT REGION 35..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q9H1P3"
FT BINDING 178..179
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q9H1P3"
FT BINDING 431..435
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q9H1P3"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1P3"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1P3"
FT CONFLICT 21
FT /note="I -> T (in Ref. 2; AAH26804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 55384 MW; E67BCF2D0C413497 CRC64;
MNGEEEFFDA VTGFDSDNSS IGEFSEANKI SGMIDLDTSK STRSGKNGEK PQQENGIQKH
RTALPAPMFT RSDFSVWSIL KKCIGLELSK ITMPIAFNEP LSFLQRITEY MEHVYLIHKA
SSQSQPLERM QSVAAFAVSA VASQWERTGK PFNPLLGETY ELIREDLGFR FISEQVSHHP
PISAFYSEGL NQDFRFHGSI YPKLKFWGKS VEAEPRGTIT LELLKHNEAY TWTNPTCCVH
NVILGQLWIE QYGIVEIVNH RTGDKCILHF KPCGLFGKEL HRVEGYIQDK NRKKLFIMYG
KWTECLWGID PASYESFKKQ EKRGDQARKA KMDDGPEKAN SDVPGDVADD VPVAQETVQV
IPGSKLLWRI NSRPPNSAQM YNFTSFTVSL NELESGMEKT LPPTDCRLRP DIRGMENGNM
DLASQEKERL EEKQREARKE RAKEDAEWRT RWFSPGNNPY TGAPDWLYAG HYFERNFSDC
PDIY
