ID CALYP_DROYA Reviewed; 471 AA. AC B4P6P6; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 63. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase calypso {ECO:0000250|UniProtKB:Q7K5N4}; DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q7K5N4}; DE AltName: Full=BAP1 homolog {ECO:0000250|UniProtKB:Q7K5N4}; GN Name=caly {ECO:0000250|UniProtKB:Q7K5N4}; ORFNames=GE14091; OS Drosophila yakuba (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tai18E2 / Tucson 14021-0261.01; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC -!- FUNCTION: Polycomb group (PcG) protein. Catalytic component of the PR- CC DUB complex, a complex that specifically mediates deubiquitination of CC histone H2A monoubiquitinated at 'Lys-118' (H2AK118ub1). Does not CC deubiquitinate monoubiquitinated histone H2B. Required to maintain the CC transcriptionally repressive state of homeotic genes throughout CC development. The PR-DUB complex has weak or no activity toward 'Lys- CC 48'- and 'Lys-63'-linked polyubiquitin chains. CC {ECO:0000250|UniProtKB:Q7K5N4}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q7K5N4}; CC -!- SUBUNIT: Component of the PR-DUB complex, at least composed of calypso CC (caly) and Asx. {ECO:0000250|UniProtKB:Q7K5N4}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7K5N4}. CC Note=Localizes to PcG response elements (PREs). CC {ECO:0000250|UniProtKB:Q7K5N4}. CC -!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily. CC {ECO:0000305}. 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; CM000158; EDW91973.1; -; Genomic_DNA. DR RefSeq; XP_002092261.1; XM_002092225.2. DR AlphaFoldDB; B4P6P6; -. DR SMR; B4P6P6; -. DR MEROPS; C12.A09; -. DR EnsemblMetazoa; FBtr0260609; FBpp0259101; FBgn0231717. DR GeneID; 6531462; -. DR KEGG; dya:Dyak_GE14091; -. DR eggNOG; KOG2778; Eukaryota. DR HOGENOM; CLU_018316_2_1_1; -. DR OMA; MNHGCWE; -. DR OrthoDB; 276003at2759; -. DR PhylomeDB; B4P6P6; -. DR Proteomes; UP000002282; Chromosome 2R. DR GO; GO:0000785; C:chromatin; ISS:UniProtKB. DR GO; GO:0035517; C:PR-DUB complex; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB. DR GO; GO:0040029; P:epigenetic regulation of gene expression; ISS:UniProtKB. DR GO; GO:0031507; P:heterochromatin formation; ISS:UniProtKB. DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IEA:EnsemblMetazoa. DR GO; GO:0007385; P:specification of segmental identity, abdomen; IEA:EnsemblMetazoa. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR CDD; cd09617; Peptidase_C12_UCH37_BAP1; 1. DR Gene3D; 1.20.58.860; -; 1. DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR001578; Peptidase_C12_UCH. DR InterPro; IPR036959; Peptidase_C12_UCH_sf. DR InterPro; IPR041507; UCH_C. DR PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR10589:SF28; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE BAP1; 1. DR Pfam; PF01088; Peptidase_C12; 1. DR Pfam; PF18031; UCH_C; 1. DR PRINTS; PR00707; UBCTHYDRLASE. DR SUPFAM; SSF54001; Cysteine proteinases; 1. PE 3: Inferred from homology; KW Chromatin regulator; Hydrolase; Nucleus; Protease; Thiol protease; KW Ubl conjugation pathway. FT CHAIN 1..471 FT /note="Ubiquitin carboxyl-terminal hydrolase calypso" FT /id="PRO_0000395835" FT REGION 410..471 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 410..450 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 454..471 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 131 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 213 FT /note="Proton donor" FT /evidence="ECO:0000250" FT SITE 228 FT /note="Important for enzyme activity" FT /evidence="ECO:0000250" SQ SEQUENCE 471 AA; 51482 MW; 2E576237C4F8ABCF CRC64; MNAAGGGSGS QAAGAAGVNS SLSHNALLST ASGATTMPMA QLADGWLELE SDPGLFTLLL KDFGCHDVQV EEVYDLQKPI ESPYGFIFLF RWIEERRARR KIVETTAEIF VKDEEAISSI FFAQQVVPNS CATHALLSVL LNCNENNLQL GDTLSRLKAH TKGMSPENKG LAIGNTPELA CAHNSHAMPQ ARRRLERTGA GVSSCRFTGE AFHFVSFVPI NGQLFELDGL KPYPMNHGGW EDSEDWTDKF RRVMAERLGI ATGEQDIRFN LMAVVPDRRI AITHKLKMLR TNQAIVSGTL QKLLKADEQG ESGNGDSQRP DTPTTLLEPS AFTARDLQSL LKNLDTEIAI NEQHLADEND RRHMFKVDAS RRTHNYDKFI CTFLSMLAHQ GVLGELVSQH LLPSKKVSGQ GAANRISKQS TTASAGGSTT GATASTPKTQ QQQAAAAKNG KSPSKTPGRR RKGRNKCRKR K //