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Database: UniProt
Entry: H2MPX4_ORYLA
LinkDB: H2MPX4_ORYLA
Original site: H2MPX4_ORYLA 
ID   H2MPX4_ORYLA            Unreviewed;       337 AA.
AC   H2MPX4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=UV excision repair protein RAD23 {ECO:0000256|RuleBase:RU367049};
GN   Name=rad23aa {ECO:0000313|Ensembl:ENSORLP00000020787.2};
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000020787.2, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000020787.2, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000020787.2,
RC   ECO:0000313|Proteomes:UP000001038};
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA   Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA   Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA   Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA   Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA   Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome evolution.";
RL   Nature 447:714-719(2007).
RN   [2] {ECO:0000313|Ensembl:ENSORLP00000020787.2}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000020787.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00009878, ECO:0000256|RuleBase:RU367049}.
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DR   AlphaFoldDB; H2MPX4; -.
DR   Ensembl; ENSORLT00000020788.2; ENSORLP00000020787.2; ENSORLG00000016606.2.
DR   eggNOG; KOG0011; Eukaryota.
DR   GeneTree; ENSGT00390000012078; -.
DR   HOGENOM; CLU_040364_0_1_1; -.
DR   TreeFam; TF101216; -.
DR   Proteomes; UP000001038; Chromosome 8.
DR   Bgee; ENSORLG00000016606; Expressed in gastrula and 14 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
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; cd14377; UBA1_Rad23; 1.
DR   CDD; cd14427; UBA2_HR23A; 1.
DR   CDD; cd17126; Ubl_HR23A; 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; IPR041811; RAD23A/B_UBA1.
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; 2.
DR   PANTHER; PTHR10621; UV EXCISION REPAIR PROTEIN RAD23; 1.
DR   PANTHER; PTHR10621:SF29; UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG A; 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   3: Inferred from homology;
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   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          3..78
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          142..182
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          292..332
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          83..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..113
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   337 AA;  36895 MW;  72118C1601A000FF CRC64;
     AAMQITLKTL QQQTIQIEID PEQTVKALKE KIEAERGKDN FPVSGQKLIY AGKILQDDTP
     IKDYKIDEKN FVVVMVSKVR LHGPPPAQDS GSTSTAAPPS NPPAAPTPAA VPIPPEEAKQ
     EQSAEATEPQ QPLVEKGDEM GKEYEAMLTE IMSMGYERER VVAALRASFN NPHRAVEYLL
     TGIPSSPVQE SNPPVQPPTS GSTDNPLAFL RTQPQFLHMR QAIQQNPALL PTLLQQLGRE
     NPQLLQQISQ HQELFIQMLN EPVGEGGDPP EVGEMGAAGE EGAPVNYIQV TPQEKEAIER
     LKALGFPEAL VIQAYFACEK NENLAANFLL NQGLEDD
//
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