ID   CALYP_AEDAE             Reviewed;         478 AA.
AC   Q17N72;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=AAEL000787;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(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.
CC       {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}.
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DR   EMBL; CH477201; EAT48182.1; -; Genomic_DNA.
DR   RefSeq; XP_001651006.1; XM_001650956.1.
DR   AlphaFoldDB; Q17N72; -.
DR   SMR; Q17N72; -.
DR   STRING; 7159.Q17N72; -.
DR   MEROPS; C12.A09; -.
DR   PaxDb; 7159-AAEL000787-PA; -.
DR   GeneID; 5566609; -.
DR   KEGG; aag:5566609; -.
DR   VEuPathDB; VectorBase:AAEL000787; -.
DR   eggNOG; KOG2778; Eukaryota.
DR   HOGENOM; CLU_018316_2_1_1; -.
DR   InParanoid; Q17N72; -.
DR   OMA; MNHGCWE; -.
DR   OrthoDB; 276003at2759; -.
DR   PhylomeDB; Q17N72; -.
DR   Proteomes; UP000008820; Unassembled WGS sequence.
DR   Proteomes; UP000682892; 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:0040029; P:epigenetic regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0031507; P:heterochromatin formation; ISS:UniProtKB.
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; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..478
FT                   /note="Ubiquitin carboxyl-terminal hydrolase calypso"
FT                   /id="PRO_0000395824"
FT   REGION          432..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..478
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        97
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        176
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            191
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  54158 MW;  80C8628EC07A5556 CRC64;
     MPVDINRLTD GWLELESDPG LFTLLLEDFG VKGVQVEEIY DLQKNIEGPV YGFIFLFRWI
     EERRARRKIV ETTEIYVKDE EAVNNIFFAQ QVVPNSCATH ALLSVLLNCS DIDLGNTLSR
     LKVHTKGMCP ENKGWAIGNT PELACAHNSH AMPQARRRMD RNSGVSTGRF TGEAFHFVSF
     VPINGHLFEL DGLKPFPMDH GPWGEKEAWT DKFRRVMSDR LGISTGEQDI RFNLMAVVPD
     RRIAITHKLK MLRTNQTIVS AALEKLLKSK RTESRSLETV DKIKKEEESP VKLSSEYSQL
     LEMNEKDDSS VPMSKELESL VSLNSSSDSV EIIGETEIKK ENPPPSPPPS FIGAGTFSPK
     DLLSLLKNLE SEINITEQHL CDENEKRAMF KVDDCRRTHN YDEFICTFLS MLAHQGELGD
     LVSQHLITNR KPNMGSVQNS GSRGVVRNYN KKTTTNGSSP KTPSSKRRRG RTKYRKRK
//