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MINY3_DROME
ID   MINY3_DROME             Reviewed;         560 AA.
AC   Q9VWN5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase MINDY-3 homolog;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme MINDY-3;
DE   AltName: Full=Protein CARP homolog;
GN   Name=mindy3; ORFNames=CG7332;
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=Embryo;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND SER-219, 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: Hydrolase that can remove 'Lys-48'-linked conjugated
CC       ubiquitin from proteins. {ECO:0000250|UniProtKB:Q9H8M7}.
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:Q9H8M7};
CC   -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM188
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE014298; AAF48903.1; -; Genomic_DNA.
DR   EMBL; AY058544; AAL13773.1; -; mRNA.
DR   RefSeq; NP_001285417.1; NM_001298488.1.
DR   RefSeq; NP_573338.1; NM_133110.3.
DR   AlphaFoldDB; Q9VWN5; -.
DR   IntAct; Q9VWN5; 2.
DR   STRING; 7227.FBpp0074418; -.
DR   iPTMnet; Q9VWN5; -.
DR   PaxDb; Q9VWN5; -.
DR   PRIDE; Q9VWN5; -.
DR   DNASU; 32885; -.
DR   EnsemblMetazoa; FBtr0074647; FBpp0074418; FBgn0030973.
DR   EnsemblMetazoa; FBtr0342877; FBpp0309678; FBgn0030973.
DR   GeneID; 32885; -.
DR   KEGG; dme:Dmel_CG7332; -.
DR   UCSC; CG7332-RA; d. melanogaster.
DR   FlyBase; FBgn0030973; CG7332.
DR   VEuPathDB; VectorBase:FBgn0030973; -.
DR   eggNOG; KOG2871; Eukaryota.
DR   HOGENOM; CLU_033478_0_0_1; -.
DR   InParanoid; Q9VWN5; -.
DR   OMA; HVWDHDQ; -.
DR   OrthoDB; 1276386at2759; -.
DR   PhylomeDB; Q9VWN5; -.
DR   BioGRID-ORCS; 32885; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 32885; -.
DR   PRO; PR:Q9VWN5; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0030973; Expressed in brain and 10 other tissues.
DR   ExpressionAtlas; Q9VWN5; baseline and differential.
DR   Genevisible; Q9VWN5; DM.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IBA:GO_Central.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR025257; MINDY-3/4_CD.
DR   InterPro; IPR039785; MINY3/4.
DR   PANTHER; PTHR12473; PTHR12473; 1.
DR   Pfam; PF13898; DUF4205; 1.
DR   SMART; SM01174; DUF4205; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..560
FT                   /note="Ubiquitin carboxyl-terminal hydrolase MINDY-3
FT                   homolog"
FT                   /id="PRO_0000317565"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          44..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        139
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   ACT_SITE        403
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   MOD_RES         212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   560 AA;  61755 MW;  E843D48D983E8D47 CRC64;
     MNEKIVREQR GGEDSPSSVS AKSATAAASA STASMTFASA ALESHKTTTI TTASSSPRTS
     GASASASSSS RSASAPASSS SQQEKQPMLN ATDMRELREI KQLLWGDNVR EDVFKRWSQG
     FEFSKVEPSA LVQKQGGPCA VIAPVQAYLL KIIIMDLPGI KLSEISLDKS QNLLIQALCD
     ILKNCRAPRY RIVHLLRRRG NATEAGSTKK RSPAGEEESA LAGQAAGSSE EVEEAAEATP
     ASVSKLSQAL QLEHDMHQEL SPDEFHERLH TLHFKNIAAV ARYYMENYDQ LAHTYGVLLF
     MYSVFLTKGL ELVAADISDT SEPLIHSTYG YGGQSLINLM LTGRAVAHVW DNEQDVGGLK
     LRGICEQSDI GFITLMEEMR YCTVGSFFKN PRYPVWVMGS DTHLTVLFSN EKRLVSPETP
     SETGRRIFKS YDPEGNNFIS TTMLREVLIA LNLVSEPAYV ALMQKRLDPE NLGIILLNAF
     MDEFFPLESR STPDTFELMH YNGIPGSNEN NKVRYYCGTA ILLEGDLKSV CTSNPMVTCL
     QTKWPNIEIN WHDGHMPSLN
 
 
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