ID A0A8J2W7K8_9CRUS Unreviewed; 1411 AA.
AC A0A8J2W7K8;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 18-JUN-2025, entry version 14.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN ORFNames=DGAL_LOCUS11569 {ECO:0000313|EMBL:CAH0108200.1};
OS Daphnia galeata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=27404 {ECO:0000313|EMBL:CAH0108200.1, ECO:0000313|Proteomes:UP000789390};
RN [1] {ECO:0000313|EMBL:CAH0108200.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M5 {ECO:0000313|EMBL:CAH0108200.1};
RA Schell T.;
RL Submitted (NOV-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:CAH0108200.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAKKLH010000281; CAH0108200.1; -; Genomic_DNA.
DR OrthoDB; 6437225at2759; -.
DR Proteomes; UP000789390; 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 GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd13314; PH_Rpn13; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR FunFam; 2.40.10.10:FF:000082; Plasma kallikrein; 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 Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR040479; CLIP_SPH_mas.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
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 InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
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 Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS51917; PRU; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 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:UP000789390};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1411
FT /note="Proteasomal ubiquitin receptor ADRM1 homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035281146"
FT DOMAIN 810..1124
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 1028..1141
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 1289..1404
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 34..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..84
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..280
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..412
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..515
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..575
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..655
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..758
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1242
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1411 AA; 146968 MW; C415726C593BB0C9 CRC64;
MNWTIGLLTV ITLTLTWSQL MTISAAQQKL QQSEQSTSGV LESLTSSQAS PSDVGGTASS
TAGSSTTATA KTNPTITTTG TPTASDAKAQ QQQPSPTPGS LASSLLSGLF DTITSTSKSK
DCPGRCVHVL AALLCEKVLE NVSCSEASMR CCVENRPSPP ARSVTTTKTP IAVNASNSST
AAPSSTTTAA ATTTTTKVET TTTAVPTTTT KATTTTTPTT TTTTTTTTTT PKPTTTTTTT
TTTTTTKAPT TTTTTTKPTT TTTKAPSTTT TTAKPVSTTT RAPSTTKSSV PLDSKVEEAE
GDDEEVLKAS EVGSLRVCPG VCVATRISDY CEAVLNVDGL CKTAMKCCVT KSLFGESEPP
PELVILNEAS STVPSSTEAS TTTSTTTTTT TPRSTTTTTR PRPKPTTTAT PSAGDDKRCK
GTCVTGFFSY LCDFIDSKAV CANGGKCCIS RREGSGGLSE QKTNNVTAPV SGARPSPSSS
SKPSVVTSTT ARPTTAKPKA TTTSTTASPS TTTTAQPKRC PGVCLPGLMS AFCSKPSVVV
NNPPNLCERG SICCDSKTRD GETQSGGSSS GSSGSTNNNR PSRPPTKAPA SAMSDLLSNP
LTTLLAGPLL SSLAGAAMNQ RPSSGGDKSD ASPQRPQSIH RTPSTTTTTT STTTSAPQVV
DTRPYCPGTC MAPILSFSCF SNAEITDLFR CPSSKVVCCA QKSAIRELKP SSGVSVEAPH
SEFSRPGGSF RPPPMVRPGT AVATPPQQLP QQQQAAATSS GPRPSVARPL PNSKFVCGVK
GNHREIRDLS VIENDNATTT LSSGFRRGRV VGGNDALPGE YCWQVALINS LNQYLCGGAL
IGTQWVLTAA HCVTNIVRSG DAIYVRVGDH DLTSRYGSPG AQTLRVATTY IHHNHNSQTL
DNDIALLKLQ GQAELKPGVC IICLPSRGSI PETGRRCTVT GYGYMGETGP IPLRVREADV
PIVSEGECVR QINAVTEKIF IMPASSFCAG GEAGNDACQG DGGAFVASNE VERSKGEMSL
FSNSSSRSQS KNLVEFRAGK MTMRGNMVHP DKRKGLVYIH QSSDSLIHFC WKDRQSGNVE
DDWIIFPDDC EYVRVPQCTT GRVFLLKFKS SNKKTFFWMQ EPKTDKDETY CRKVNEYLNN
PPAPGSQSGR GGSNLGSERD LQSLLSSMSQ QQLMQLFGNV GGMSGLSSLL VPSEGAMRSS
SSSRSRSSGA TSGSASQARS AAAIPPAAAP SATAASTTPS SANVGSNLPA TPLSTGVPSL
GNLTNLQQIL SGIQVPDSAL GLSGAAAAQG QPEKPSVDLS EGLSTDVLHP ILNNADFMRQ
LRDFLPPSDQ TSEGDTASMV RDTVQSPQFA QALSVFSAAL QSGQLGPLIQ QFGLGAEAVE
AAQKGDMEAF IAALQNKDKK KEDGDDGMAL D
//
