CALYP_DROPS
ID CALYP_DROPS Reviewed; 475 AA.
AC Q291J4;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase calypso;
DE EC=3.4.19.12;
DE AltName: Full=BAP1 homolog;
GN Name=calypso; ORFNames=GA21084;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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}.
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; CM000071; EAL25118.1; -; Genomic_DNA.
DR RefSeq; XP_001360543.1; XM_001360506.3.
DR AlphaFoldDB; Q291J4; -.
DR SMR; Q291J4; -.
DR STRING; 7237.FBpp0276844; -.
DR MEROPS; C12.A09; -.
DR EnsemblMetazoa; FBtr0278406; FBpp0276844; FBgn0081072.
DR GeneID; 4803898; -.
DR KEGG; dpo:Dpse_GA21084; -.
DR eggNOG; KOG2778; Eukaryota.
DR HOGENOM; CLU_018316_2_1_1; -.
DR InParanoid; Q291J4; -.
DR OMA; IAINEQH; -.
DR PhylomeDB; Q291J4; -.
DR Proteomes; UP000001819; Chromosome 3.
DR Bgee; FBgn0081072; Expressed in female reproductive system and 2 other tissues.
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..475
FT /note="Ubiquitin carboxyl-terminal hydrolase calypso"
FT /id="PRO_0000395831"
FT REGION 411..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..475
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 227
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 475 AA; 52100 MW; 02746ECD4125FDD8 CRC64;
MNVAAGGPGT ASASTTAANS IFNNSLLASA TGATTMPMAQ LADGWLELES DPGLFTLLLE
DFGCHDVQVE EVYDLQKPIE SPYGFIFLFR WIEERRARRK IVETTAEIFV KDEEAISSIF
FAQQVVPNSC ATHALLSVLL NCNENNLQLG DTLSRLKVHT KGMSPENKGL AIGNTPELAC
AHNSHAIPQA RRRLERTGAG VASCRFTGEA FHFVSFVPIS GQLFELDGLK PYPMNHGGWE
DHEDWTDKFR RVMAERLGIA TGEQDIRFNL MAVVPDRRIA ITHKLKMLRT NQAIVSGTLQ
KLLKADEQGE SGNGDQQRPD TPTTLLEPSA FTAKDLQLLL KNLDTEIAIN EQNLADENDR
RHMFKVDASR RTHNYDKFIC TFLSMLAHQG VLGELVSQHL LPSKKVSGQS AANRISKQNS
AASSAGANAG AAAGVTPKSQ QQQQQPQTAA SKNGKSPGKT PGRRRKGRNK CRKRK
