ID A0A1D5Q562_MACMU Unreviewed; 854 AA.
AC A0A1D5Q562;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 28-JAN-2026, entry version 48.
DE RecName: Full=Oxysterol-binding protein {ECO:0000256|RuleBase:RU003845};
GN Name=OSBPL2 {ECO:0000313|VGNC:VGNC:75611};
GN Synonyms=ADRM1 {ECO:0000313|Ensembl:ENSMMUP00000043177.2,
GN ECO:0000313|VGNC:VGNC:69613};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000043177.2, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000043177.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000043177.2};
RA Graves T., Eichler E.E., Wilson R.K.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSMMUP00000043177.2}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000043177.2};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSMMUP00000043177.2}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000043177.2};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP). Interacts with the proteasomal scaffolding
CC protein PSMD1. Interacts with deubiquitinase UCHL5; this interaction
CC activates the auto-inhibited UCHL5 by deoligomerizing it. Interacts
CC with UBQLN2 and ubiquitin. {ECO:0000256|ARBA:ARBA00061738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ADRM1 family.
CC {ECO:0000256|ARBA:ARBA00009216}.
CC -!- SIMILARITY: Belongs to the OSBP family.
CC {ECO:0000256|RuleBase:RU003844}.
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DR AlphaFoldDB; A0A1D5Q562; -.
DR SMR; A0A1D5Q562; -.
DR FunCoup; A0A1D5Q562; 1475.
DR STRING; 9544.ENSMMUP00000043177; -.
DR Ensembl; ENSMMUT00000073245.2; ENSMMUP00000043177.2; ENSMMUG00000012623.4.
DR VEuPathDB; HostDB:ENSMMUG00000012623; -.
DR VGNC; VGNC:69613; ADRM1.
DR VGNC; VGNC:75611; OSBPL2.
DR eggNOG; KOG3037; Eukaryota.
DR GeneTree; ENSGT00940000158762; -.
DR InParanoid; A0A1D5Q562; -.
DR Proteomes; UP000006718; Chromosome 10.
DR Bgee; ENSMMUG00000012623; Expressed in ileum and 21 other cell types or tissues.
DR ExpressionAtlas; A0A1D5Q562; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd13314; PH_Rpn13; 1.
DR FunFam; 2.40.160.120:FF:000005; Oxysterol-binding protein; 1.
DR FunFam; 1.10.2020.20:FF:000001; Proteasomal ubiquitin receptor ADRM1; 1.
DR FunFam; 2.30.29.70:FF:000001; Proteasomal ubiquitin receptor ADRM1; 1.
DR Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 2.40.160.120; -; 1.
DR Gene3D; 3.30.70.3490; -; 1.
DR Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR InterPro; IPR032368; RPN13_DEUBAD.
DR InterPro; IPR038108; RPN13_DEUBAD_sf.
DR PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10972:SF153; OXYSTEROL-BINDING PROTEIN-RELATED PROTEIN 2; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR Pfam; PF16550; RPN13_C; 1.
DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS51917; PRU; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055,
KW ECO:0000256|RuleBase:RU003845};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW Transport {ECO:0000256|RuleBase:RU003845}.
FT DOMAIN 465..578
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 724..838
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 416..443
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 834..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 93372 MW; 6311BF2B18332605 CRC64;
MNGEEEFFDA VTGFDSDNSS GEFSEAHQKV TGMIDLDTSK NNRIGKIGER PSQENGIQKH
RTSLPAPMFS RSDFSVWTIL KKCVGLELSK ITMPIAFNEP LSFLQRITEY MEHVYLIHRA
SCQPQPLERM QSVAAFAVSA VASQWERTGK PFNPLLGETY ELIREDLGFR FISEQVSHHP
PISAFHSEGL NHDFLFHGSI YPKLKFWGKS VEAEPRGTIT LELLKHNEAY TWTNPTCCVH
NVIIGKLWIE QYGTVEILNH RTGHKCVLHF KPCGLFGKEL HKVEGHIQDK NKKKLFVIYG
KWTECLWGID PVSYESFKKQ ERRGDHLRKA KLDDSSGKAD SDVADDVPVA QETVQVIPGS
KLLWRINTRP PNSAQMYNFT SFTVSLNELE TGMEKTLPPT DCRLRPDIRG MENGNMDLAS
QEKERLEEKQ REARRERARE EAEWQTRMTT SGALFPSLVP GSRGASNKYL VEFRAGKMSL
KGTTVTPDKR KGLVYIQQTD DSLIHFCWKD RTSGNVEDDL IIFPDDCEFK RVPQCPSGRV
YVLKFKAGSK RLFFWMQEPK TDQDEEHCRK VNEYLNNPPM PGALGASGSS GHELSALGGE
GGLQSLLGNM SHSQLMQLIG PAGLGGLGGL GALTGPGLAS LLGSSGPPGS SSSSSSRSQS
AAVTPSSTTS STRATPAPSA PAAASATSPS PAPSSGNGAS TAASPTQPIQ LSDLQSILAT
MNVPAGPAGG QQVDLASVLT PEIMAPILAN ADVQERLLPY LPSGESLPQT AEEIQNTLTS
PQFQQALGMF SAALASGQLG PLMCQFGLPA EAVEAANKGD VEAFAKAMQN NAKPEQKEGD
TKDKKDEEED MSLD
//
