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Database: UniProt
Entry: A0A164K8Q9_9CRUS
LinkDB: A0A164K8Q9_9CRUS
Original site: A0A164K8Q9_9CRUS 
ID   A0A164K8Q9_9CRUS        Unreviewed;      1146 AA.
AC   A0A164K8Q9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   18-JUN-2025, entry version 27.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN   ORFNames=APZ42_034297 {ECO:0000313|EMBL:KZS03055.1};
OS   Daphnia magna.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS03055.1, ECO:0000313|Proteomes:UP000076858};
RN   [1] {ECO:0000313|EMBL:KZS03055.1, ECO:0000313|Proteomes:UP000076858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinb3 {ECO:0000313|EMBL:KZS03055.1,
RC   ECO:0000313|Proteomes:UP000076858};
RC   TISSUE=Complete organism {ECO:0000313|EMBL:KZS03055.1};
RA   Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT   "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL   Submitted (MAR-2016) 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:KZS03055.1}.
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DR   EMBL; LRGB01003372; KZS03055.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A164K8Q9; -.
DR   STRING; 35525.A0A164K8Q9; -.
DR   OrthoDB; 6437225at2759; -.
DR   Proteomes; UP000076858; 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; 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; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR   InterPro; IPR040479; CLIP_SPH_mas.
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; PF18398; CLIP_SPH_mas; 5.
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|EMBL:KZS03055.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076858}.
FT   DOMAIN          761..874
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          1022..1137
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          929..983
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..75
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..167
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..498
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..563
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..622
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..979
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1146 AA;  119023 MW;  378E6B97331EF8E2 CRC64;
     MAEKSEWGKG IGDRDLFGWN AIHGQKQPSM SGAESLTSPS PSDVGGTSSN TAGSSTTATA
     KANPTTSTTT GMPTTNNAKA QQPSPTPGSL ASSLLSGLFD TITSTSKSKD CPGRCVHVLA
     ALLCEKVLEN VTCSEGSMRC CVENRPSPPA RSVTTKTPAV STSSVVSSSS EATTTQKVVT
     TTAPTTTTTK ATTAIPTTTT ASTTTTKPTT QSTTTAKATT TTAPTTTTTK TTTTTTKPTT
     TTTKAPTTTT KAPTTTTTTV KPSSTTTTVA TTTKAAVTVD SKVEDAEGGD DDEVLKASEV
     GSLRICPGVC VATRISDYCE AVLNVDGLCK TAMKCCVTKS LFGESEPPPE LVILNEASST
     GASTTEASTT TSRTTTTVRT TSTTTRPRPK TTTTAVPAAD DDKRCKGTCV TGFFSYLCDF
     IDAKAVCANG GKCCISRREG GGGASEQKTN NVTAPASGSR PSAGSSKPSV VTSTTARPTT
     AKPKATTTSA PSTTTASVPK RCPGVCLPGL MSAFCSKPSV VVNNPPNLCD RGSICCDSKT
     RDSPQSGGSG SNSGSSGSTN NRPSRPPTKA PASAMSDLLS NPLTTLLAGP LLSSLAGAAM
     NQRPSSSGDK SDVSPQRPQS IGTRPPPTTT TTTTTTTSAP QVVDTRPYCP GTCMAPILSF
     SCFSNAEITD LFRCPSSKVV CCAQKSAIRE LKPSSPATVE VPQSEFSRLG TNREEASLEY
     GDTAMICSFI FDEIVSASRL ETLVFYREEK MSLFSNSSSR SQSKNLVEFR AGKMTMRGNM
     VHPDKRKGLV YIHQSSDSLI HFCWKDRQSG NVEDDWIIFP DDCEYVRVPQ CTTGRVFLLK
     FKSSNKKTFF WMQEPKTDKD ETYCRKVNEY LNNPPTPGSQ GGRGGSNLGS ERDLQSLLSS
     MSQQQLMQLF GNVGGMSGLS SLLVPSDSAV RSSSSSRSRS SGATSGSASQ ARSAAAIPPA
     TATGATAAAT TPSSANAGSN LPATPLSTGV PSLGNLTNLQ QILSGIQVPD SALGLSGTAA
     AQGQPEKPSV DLSEGLSTDV LHPILNNADF MRQLRDFLPP SDQASEGDTA SMVRDTVQSP
     QFAQALSVFS AALQSGQLGP LIQQFGLGSE AVEAAQKGDM EAFIAALQSQ DKDKKKDDGD
     DGMALD
//
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