ID A0AAJ7N9I5_9HYME Unreviewed; 436 AA.
AC A0AAJ7N9I5;
DT 24-JUL-2024, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN Name=LOC108627517 {ECO:0000313|RefSeq:XP_017884291.1};
OS Ceratina calcarata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Ceratina; Zadontomerus.
OX NCBI_TaxID=156304 {ECO:0000313|Proteomes:UP000694925, ECO:0000313|RefSeq:XP_017884291.1};
RN [1] {ECO:0000313|RefSeq:XP_017884291.1}
RP IDENTIFICATION.
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_017884291.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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}.
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DR RefSeq; XP_017884291.1; XM_018028802.2.
DR AlphaFoldDB; A0AAJ7N9I5; -.
DR GeneID; 108627517; -.
DR KEGG; ccal:108627517; -.
DR CTD; 36545; -.
DR Proteomes; UP000694925; Unplaced.
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 Receptor {ECO:0000313|RefSeq:XP_017884291.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000694925}.
FT DOMAIN 14..127
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 251..377
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 183..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..252
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..404
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..436
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 47816 MW; 50DC6AE25BF7A2B0 CRC64;
MSGGSLFGSN ASRGTPKNLV EFKAGKMTMK GKMIYPDIRK GQLYVYQSDD SLMHFCWKDR
VSGYVEDDLI IFPDDCEFKH VPQCKTGRVY LLRFKSSNKK FFVWLQDLKT DKDEEYCRKI
NEVLNNPPTP GSQRSGCTNP EEDLHNLLSN MSQQQFMQLF SGADQVGLGN LLGTVNRLQG
VQSTRASTMT ASTRVTTNAS RPSTQVASTP ASTNDSTKST NGDSKSSSTT STTATRTPGT
STPSGNTTAG TNNKIQLSAL HNFLSRIRTP GSEYPVYQWD VVTELTHSIP SAISVTESLE
RAMSPHLPPG DRLCTTLVSP QFSRALSMFW SALQSGQAGP VISQFGLGPE AVNAAASGNI
EEFVNALESE AKSSTGQQQP EQQTQQQQQQ QPQQQQQQQQ QQGQQEEKNA KEQQAPPPAS
SSPDKKDDDD EFMALD
//
