ID A9PF88_POPTR Unreviewed; 375 AA.
AC A9PF88;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Ubiquitin receptor RAD23 {ECO:0000256|RuleBase:RU367049};
DE AltName: Full=DNA repair protein RAD23 {ECO:0000256|RuleBase:RU367049};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694 {ECO:0000313|EMBL:ABK95041.1};
RN [1] {ECO:0000313|EMBL:ABK95041.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Young and mature leaves {ECO:0000313|EMBL:ABK95041.1};
RX PubMed=18230180; DOI=10.1186/1471-2164-9-57;
RA Ralph S.G., Chun H.J., Cooper D., Kirkpatrick R., Kolosova N., Gunter L.,
RA Tuskan G.A., Douglas C.J., Holt R.A., Jones S.J., Marra M.A., Bohlmann J.;
RT "Analysis of 4,664 high-quality sequence-finished poplar full-length cDNA
RT clones and their utility for the discovery of genes responding to insect
RT feeding.";
RL BMC Genomics 9:57-57(2008).
CC -!- FUNCTION: Multiubiquitin chain receptor involved in modulation of
CC proteasomal degradation. Involved in nucleotide excision repair.
CC {ECO:0000256|RuleBase:RU367049}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367049}.
CC Cytoplasm {ECO:0000256|RuleBase:RU367049}.
CC -!- SIMILARITY: Belongs to the RAD23 family.
CC {ECO:0000256|RuleBase:RU367049}.
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DR EMBL; EF147005; ABK95041.1; -; mRNA.
DR RefSeq; XP_006368664.1; XM_006368602.1.
DR AlphaFoldDB; A9PF88; -.
DR GeneID; 7476798; -.
DR KEGG; pop:7476798; -.
DR eggNOG; KOG0011; Eukaryota.
DR OrthoDB; 158575at2759; -.
DR ExpressionAtlas; A9PF88; differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043130; F:ubiquitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd14379; UBA1_Rad23_plant; 1.
DR CDD; cd01805; Ubl_Rad23; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 1.10.10.540; XPC-binding domain; 1.
DR InterPro; IPR004806; Rad23.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR015360; XPC-bd.
DR InterPro; IPR036353; XPC-bd_sf.
DR NCBIfam; TIGR00601; rad23; 1.
DR PANTHER; PTHR10621; UV EXCISION REPAIR PROTEIN RAD23; 1.
DR PANTHER; PTHR10621:SF0; UV EXCISION REPAIR PROTEIN RAD23; 1.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF09280; XPC-binding; 1.
DR PRINTS; PR01839; RAD23PROTEIN.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; UBA-like; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF101238; XPC-binding domain; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|RuleBase:RU367049};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367049};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367049};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367049};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..79
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 145..188
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 329..369
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 80..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 39861 MW; 6B8E45485052AB91 CRC64;
MKLTVKTLKG SHFEIKVQPT DTVMGVKKNI EDVQGKDNYP CGQQLLIHNG KVLKDETTLV
DNKVTEDGFL VVMLSKSKTA AAGTSSTQPV STPPTTTPTS NSTPDAPAPD AQAPASKSAS
ASDTATANAQ SDTYGQAASN LVAGSSLEQT IQQIMDVGGG NWDKETVTRA LRAAYNNPER
AVDYLYSGIP ETAEVAVPVA RFPADQGIET GAAPAAPALA PGGPNSSPLN MFPETLSGGG
GDAGLVLGSL DFLRNNQQFQ ALRSMVQANP QILQPMLQEL GKQNPQLLRM IQEHNAEFLQ
LINEPLDGSE GDIFDQPDQD MPHAINVTPA EQEAIERLVA MGFDRALVIE AFLACDRNEE
LAANYLLENG ADFED
//
