ID   CALYP_DROSE             Reviewed;         471 AA.
AC   B4HST0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase calypso;
DE            EC=3.4.19.12;
DE   AltName: Full=BAP1 homolog;
GN   Name=calypso; ORFNames=GM20083;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
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 (By similarity).
CC       {ECO:0000250}.
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;
CC   -!- SUBUNIT: Component of the PR-DUB complex, at least composed of calypso
CC       and Asx. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to PcG
CC       response elements (PREs). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH480816; EDW48094.1; -; Genomic_DNA.
DR   RefSeq; XP_002034081.1; XM_002034045.1.
DR   AlphaFoldDB; B4HST0; -.
DR   SMR; B4HST0; -.
DR   STRING; 7238.B4HST0; -.
DR   MEROPS; C12.A09; -.
DR   EnsemblMetazoa; FBtr0203068; FBpp0201560; FBgn0174966.
DR   GeneID; 6609392; -.
DR   KEGG; dse:6609392; -.
DR   HOGENOM; CLU_018316_2_1_1; -.
DR   OMA; IAINEQH; -.
DR   PhylomeDB; B4HST0; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
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:0031507; P:heterochromatin assembly; ISS:UniProtKB.
DR   GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
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   Gene3D; 3.40.532.10; -; 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; PTHR10589; 2.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   Pfam; PF18031; UCH_C; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Hydrolase; Nucleus; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..471
FT                   /note="Ubiquitin carboxyl-terminal hydrolase calypso"
FT                   /id="PRO_0000395832"
FT   REGION          307..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..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;  51551 MW;  89CE740831A27182 CRC64;
     MNAAGGGSGA QAAGVAAGNI SLSHNALLST ASGATTMPMA QLADGWLELE SDPGLFTLLL
     KDFGCHDVQV EEVYDLQKPI ESPYGFIFLF RWIEERRARR KIVETTAEIF VKDEEAISSI
     FFAQQVVPNS CATHALLSVL LNCNENNLQL GDTLSRLKTH TKGMSPENKG LAIGNTPELA
     CAHNSHAMPQ ARRRLERTGA GVSSCRFTGE AFHFVSFVPI NGQLFELDGL KPYPMNHGGW
     EDSEDWTDKF RRVMAERLGI ATGEQDIRFN LMAVVPDRRI AITHKLKMLR TNQAIVSGTL
     QKLLKADEQG ESGNGDSQRP DTPTTLLEPS AFTARDLQSL LKNLDTEIAI NEQHLTDEND
     RRHMFKVDAS RRTHNYDKFI CTFLSMLAHQ GVLGELVSQH LLPSKKVSGQ GAANRISKQS
     NTASAGGSTT GASASTPKTQ QQQAAAAKNG KSPSKTPGRR RKGRNKCRKR K