ID   TRBID_DROME             Reviewed;         778 AA.
AC   Q9VH90; Q8T9K1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Ubiquitin thioesterase trabid;
DE            Short=dTrbd;
DE            EC=3.4.19.12;
GN   Name=trbd; ORFNames=CG9448;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   FUNCTION, INTERACTION WITH APC, AND DISRUPTION PHENOTYPE.
RX   PubMed=18281465; DOI=10.1101/gad.463208;
RA   Tran H., Hamada F., Schwarz-Romond T., Bienz M.;
RT   "Trabid, a new positive regulator of Wnt-induced transcription with
RT   preference for binding and cleaving K63-linked ubiquitin chains.";
RL   Genes Dev. 22:528-542(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770; SER-771 AND SER-775, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Positive regulator of the Wnt signaling pathway. Specifically
CC       cleaves 'Lys-63'-linked ubiquitin chains. May act by deubiquitinating
CC       APC protein, a negative regulator of Wnt-mediated transcription (By
CC       similarity). Required for an efficient wg response, but not for other
CC       signaling responses, in the eye. {ECO:0000250,
CC       ECO:0000269|PubMed:18281465}.
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: Interacts with Apc. {ECO:0000269|PubMed:18281465}.
CC   -!- DOMAIN: The OTU domain mediates the deubiquitinating activity.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The RanBP2-type zinc fingers mediate the specific interaction
CC       with 'Lys-63'-linked ubiquitin. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Flies are viable and fertile, suggesting
CC       functional redundancy. {ECO:0000269|PubMed:18281465}.
CC   -!- SIMILARITY: Belongs to the peptidase C64 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL39403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014297; AAF54429.1; -; Genomic_DNA.
DR   EMBL; AY058438; AAL13667.1; -; mRNA.
DR   EMBL; AY069258; AAL39403.1; ALT_INIT; mRNA.
DR   RefSeq; NP_649931.1; NM_141674.3.
DR   AlphaFoldDB; Q9VH90; -.
DR   SMR; Q9VH90; -.
DR   BioGRID; 66338; 12.
DR   IntAct; Q9VH90; 16.
DR   STRING; 7227.FBpp0081569; -.
DR   MEROPS; C64.004; -.
DR   iPTMnet; Q9VH90; -.
DR   PaxDb; 7227-FBpp0081569; -.
DR   DNASU; 41179; -.
DR   EnsemblMetazoa; FBtr0082091; FBpp0081569; FBgn0037734.
DR   GeneID; 41179; -.
DR   KEGG; dme:Dmel_CG9448; -.
DR   UCSC; CG9448-RA; d. melanogaster.
DR   AGR; FB:FBgn0037734; -.
DR   CTD; 41179; -.
DR   FlyBase; FBgn0037734; trbd.
DR   VEuPathDB; VectorBase:FBgn0037734; -.
DR   eggNOG; KOG4345; Eukaryota.
DR   GeneTree; ENSGT00940000158045; -.
DR   HOGENOM; CLU_013907_0_0_1; -.
DR   InParanoid; Q9VH90; -.
DR   OMA; MCDTKDD; -.
DR   OrthoDB; 2909231at2759; -.
DR   PhylomeDB; Q9VH90; -.
DR   Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-DME-5689896; Ovarian tumor domain proteases.
DR   SignaLink; Q9VH90; -.
DR   BioGRID-ORCS; 41179; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 41179; -.
DR   PRO; PR:Q9VH90; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0037734; Expressed in antenna and 29 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0061578; F:K63-linked deubiquitinase activity; IDA:FlyBase.
DR   GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:FlyBase.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:FlyBase.
DR   GO; GO:0070536; P:protein K63-linked deubiquitination; IMP:FlyBase.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd22767; OTU_ZRANB1; 1.
DR   Gene3D; 1.25.40.560; -; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 2.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR041294; AnkUBD.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   InterPro; IPR049768; ZRANB1_OTU.
DR   PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR   PANTHER; PTHR13367:SF28; UBIQUITIN THIOESTERASE ZRANB1; 1.
DR   Pfam; PF18418; AnkUBD; 1.
DR   Pfam; PF02338; OTU; 1.
DR   Pfam; PF00641; zf-RanBP; 1.
DR   SMART; SM00547; ZnF_RBZ; 3.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 3.
DR   PROSITE; PS50199; ZF_RANBP2_2; 3.
DR   Genevisible; Q9VH90; DM.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Phosphoprotein; Protease; Reference proteome;
KW   Repeat; Thiol protease; Ubl conjugation pathway; Wnt signaling pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..778
FT                   /note="Ubiquitin thioesterase trabid"
FT                   /id="PRO_0000361559"
FT   DOMAIN          507..665
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   ZN_FING         5..36
FT                   /note="RanBP2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   ZN_FING         89..118
FT                   /note="RanBP2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   ZN_FING         232..261
FT                   /note="RanBP2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   REGION          187..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        518
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        658
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         770
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         771
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         775
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   778 AA;  88199 MW;  57AAF0A860032F07 CRC64;
     MCDTKDDAQK WKCETCTYEN YPSSLKCTMC QASKPLLNED IFRLSPAQES CTVAEEAAAV
     EVAVMSPTPS STCYSLQPQS QARQSNVADS EKWPCKVCTY LNWPRSLRCV QCCTKRGGEA
     IERGKKDMDN EADGDRAGEA LQALRISGSE ENLANKPVQL IGATASHRLS LSRGIDDATH
     LNNLANASHN QSQSQHRQPV LQQQMQLQLQ PQQQRESSSS AAVPPQQQKQ CYVSKWACNS
     CTYENWPRSI KCSMCGKTRE REISGSQNDL HASSSLNSQE ENQQQLQQPN VDTVSVNNSF
     NKKHIYQLGS SETINNCDTL QERQERRQRQ IRRQVDWQWL NACLGVVENN YSAVEAYLSC
     GGNPARSLTS TEIAALNRNS AFDVGHTLIH LAIRFHREEM LPMLLDQISG SGPGIKRVPS
     YVAPDLAADI RRHFANTLRL RKSGLPCHYV QKHATFALPA EIEELPIPIQ EQLYDELLDR
     DAQKQLETPP PALNWSLEIT ARLSSRMFVL WNRSAGDCLL DSAMQATWGV FDRDNILRRA
     LADTLHQCGH VFFTRWKEYE MLQASMLHFT LEDSQFEEDW STLLSLAGQP GSSLEQLHIF
     ALAHILRRPI IVYGVKYVKS FRGEDIGYAR FEGVYLPLFW DQNFCTKSPI ALGYTRGHFS
     ALVPMEPFTR IDGRRDDVED VTYLPLMDCE LKLLPIHFLT QSEVGNEESM MRQWLDVCVT
     DGGLLVAQQK LSKRPLLVAQ MLEEWLNHYR RIAQVITAPF IRRPQITHYS SDGDSDEE
//