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Database: UniProt
Entry: A0AAD5LSK2_PARTN
LinkDB: A0AAD5LSK2_PARTN
Original site: A0AAD5LSK2_PARTN 
ID   A0AAD5LSK2_PARTN        Unreviewed;       395 AA.
AC   A0AAD5LSK2;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 8.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN   ORFNames=KIN20_000481 {ECO:0000313|EMBL:KAJ1345855.1};
OS   Parelaphostrongylus tenuis (Meningeal worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Parelaphostrongylus.
OX   NCBI_TaxID=148309 {ECO:0000313|EMBL:KAJ1345855.1, ECO:0000313|Proteomes:UP001196413};
RN   [1] {ECO:0000313|EMBL:KAJ1345855.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MNPRO001-30 {ECO:0000313|EMBL:KAJ1345855.1};
RC   TISSUE=Meninges {ECO:0000313|EMBL:KAJ1345855.1};
RA   Garwood T.J., Larsen P.A., Fountain-Jones N.M., Garbe J.R.,
RA   Macchietto M.G., Kania S.A., Gerhold R.W., Richards J.E., Wolf T.M.;
RT   "Parelaphostrongylus tenuis whole genome reference sequence.";
RL   Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May function as a proteasomal ubiquitin receptor. May promote
CC       the deubiquitinating activity associated with the 26S proteasome.
CC       {ECO:0000256|ARBA:ARBA00054744}.
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   -!- 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:KAJ1345855.1}.
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DR   EMBL; JAHQIW010000077; KAJ1345855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAD5LSK2; -.
DR   Proteomes; UP001196413; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:TreeGrafter.
DR   GO; GO:0061133; F:endopeptidase activator activity; IEA:TreeGrafter.
DR   GO; GO:0070628; F:proteasome binding; IEA:TreeGrafter.
DR   CDD; cd13314; PH_Rpn13; 1.
DR   FunFam; 2.30.29.70:FF:000001; Proteasomal ubiquitin receptor ADRM1; 1.
DR   Gene3D; 1.10.2020.20; -; 1.
DR   Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR   InterPro; IPR044867; DEUBAD_dom.
DR   InterPro; IPR006773; Rpn13/ADRM1.
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; PTHR12225; ADHESION REGULATING MOLECULE 1 110 KDA CELL MEMBRANE GLYCOPROTEIN; 1.
DR   PANTHER; PTHR12225:SF0; PROTEASOMAL UBIQUITIN RECEPTOR ADRM1; 1.
DR   Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR   Pfam; PF16550; RPN13_C; 1.
DR   PROSITE; PS51916; DEUBAD; 1.
DR   PROSITE; PS51917; PRU; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP001196413}.
FT   DOMAIN          15..134
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          242..353
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          129..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..368
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   395 AA;  42060 MW;  6FD1BA72270F8A2D CRC64;
     MSAMFSTTRS SQGGSSSGNL VEFKAGRSFL QQGTGANKKK VVADKTKGLV FIKQSNDQLM
     HFCWKNRETG AVVDDLIIFP GDTEFKEVKG CPDGKVYMLK FKTSDERRLF WIQDGNADVD
     RDLCKKVNDT LNKPPTTRAS ARGGSSERTT GGLSTANLAG LGGNEELGAL GGLDQQQLMQ
     LLQFMNQGNS DSPALVPQVP SGASSERTAS GNTPKVSASE LTQLQTLLGG LRAPGAESSQ
     GSADRQVTVE LSDVIAGGQV VEAAMSNADR LLEHMPVEDK TSADTKKALE DTVRSPHYRQ
     AANSFGHALS TGQMAPVLER FGISEGAVQA AATGNLLEFA RKLTESERGL EAAQAASVPA
     ATTNAETTVE VENEDSLKEP EPKRGRTDED EMDLD
//
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