CALYP_AEDAE
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 03-AUG-2022, entry version 85.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase calypso;
DE EC=3.4.19.12;
DE AltName: Full=BAP1 homolog;
GN Name=calypso; 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) (By
CC similarity). {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. {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; CH477201; EAT48182.1; -; Genomic_DNA.
DR RefSeq; XP_001651006.1; XM_001650956.1.
DR AlphaFoldDB; Q17N72; -.
DR SMR; Q17N72; -.
DR STRING; 7159.AAEL000787-PA; -.
DR MEROPS; C12.A09; -.
DR PRIDE; Q17N72; -.
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; IAINEQH; -.
DR OrthoDB; 1363547at2759; -.
DR PhylomeDB; Q17N72; -.
DR Proteomes; UP000008820; 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: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..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
