TRBID_DROME
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 03-AUG-2022, entry version 157.
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; Q9VH90; -.
DR PRIDE; Q9VH90; -.
DR DNASU; 41179; -.
DR EnsemblMetazoa; FBtr0082091; FBpp0081569; FBgn0037734.
DR GeneID; 41179; -.
DR KEGG; dme:Dmel_CG9448; -.
DR UCSC; CG9448-RA; d. melanogaster.
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; RWREYEA; -.
DR OrthoDB; 728724at2759; -.
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 tissues.
DR Genevisible; Q9VH90; DM.
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:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IMP:FlyBase.
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:0071947; P:protein deubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0035523; P:protein K29-linked deubiquitination; IBA:GO_Central.
DR GO; GO:1990168; P:protein K33-linked deubiquitination; IBA:GO_Central.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IMP:FlyBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR041294; AnkUBD.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
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; SSF90209; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 3.
DR PROSITE; PS50199; ZF_RANBP2_2; 3.
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
