ID A0A811XUV5_NYCPR Unreviewed; 853 AA.
AC A0A811XUV5;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 08-OCT-2025, entry version 15.
DE RecName: Full=Oxysterol-binding protein {ECO:0000256|RuleBase:RU003845};
GN ORFNames=NYPRO_LOCUS1953 {ECO:0000313|EMBL:CAD7669159.1};
OS Nyctereutes procyonoides (Raccoon dog) (Canis procyonoides).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Nyctereutes.
OX NCBI_TaxID=34880 {ECO:0000313|EMBL:CAD7669159.1, ECO:0000313|Proteomes:UP000645828};
RN [1] {ECO:0000313|EMBL:CAD7669159.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TBG_1078 {ECO:0000313|EMBL:CAD7669159.1};
RG Molecular Ecology Group;
RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAD7669159.1}.
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DR EMBL; CAJHUB010000653; CAD7669159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A811XUV5; -.
DR Proteomes; UP000645828; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0015485; F:cholesterol binding; IEA:TreeGrafter.
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 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:UP000645828};
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..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..695
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 853 AA; 92977 MW; 4A09198E66710D40 CRC64;
MNGEEEFFDA VTGFDSENSS GEFSEADPRV AGVMRVDTGR SNGIGKVGER PPRENGIQKH
RTSLPAPMFT RSDFSVWSIL KKCIGLELSK ITMPIAFNEP LSFLQRITEY MEHVYLIHRA
SCQPQALERM QCVAAFAVSA VASQWERTGK PFNPLLGETY ELIREDLGFR FISEQVSHHP
PISAFYSEGL NQDFLFHGSI YPKLKFWGKS VEAEPRGTIT LELLKHNEAY TWTNPTCCVH
NVIIGKLWIE QYGTVEILNH RTGDKCVLHF KPCGLFGKEL HKVEGHIQDK NKKKLFMIYG
KWTECLWGID PAAYESYKKR ERRGDPLSKA QPDDSSQKAD GDVLDAVPEA QETVHVIPGS
KLLWRVNTRP PNSAQMYNFT SFTVSLNELQ SGMEKTLAPT DCRLRPDIRG MENGDMDLAS
QEKERLEEKQ REARRERATQ EAEWQTRMTT SGALFPSLVP GSRGSSNKYL VEFRAGKMSL
KGTTVTPDKR KGLVYIQQTD DSLIHFCWKD RTSGNVEDDL IIFPDDCEFK RVPQCPSGRV
YVLKFKAGSK RLFFWMQEPK TDQDEEHCRK VNEYLNNPPM PGALGTSGSG GHELSALGGE
GGLQSLLGNM SHSQLMQLIG PAGLGGLGGL GALTGPGLAS LLGSGGPPAS SSSSSSRSQS
AAVTPSSTTS STRATPAPSA PAAASVTSPS PAPSSGNGTS TAASPTQPIQ LSDLQSILAT
MNVPAGPGGG QQVDLASVLT PEIMAPILAN ADVQERLLPY LPSGESLPQT AEEIQNTLTS
PQFQQALGMF SAALASGQLG PLMCQFGLPA EAVEAANKGD VEAFAKAMQN SARSEQEGDG
KDKKDEEEDM SLD
//
