EVI5_DROME
ID EVI5_DROME Reviewed; 807 AA.
AC Q9VYY9; C9QP48; E1JJH7; F0JAJ2; Q8IR89; Q8MT90; Q95S00;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ecotropic viral integration site 5 ortholog;
GN Name=Evi5; ORFNames=CG11727;
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM B).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 375-807 (ISOFORM D).
RA Carlson J., Booth B., Frise E., Park S., Sandler J., Wan K., Yu C.,
RA Celniker S.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-64, 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).
RN [7]
RP FUNCTION, INTERACTION WITH RAB11, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-160.
RX PubMed=22778279; DOI=10.1083/jcb.201112114;
RA Laflamme C., Assaker G., Ramel D., Dorn J.F., She D., Maddox P.S.,
RA Emery G.;
RT "Evi5 promotes collective cell migration through its Rab-GAP activity.";
RL J. Cell Biol. 198:57-67(2012).
CC -!- FUNCTION: Functions as a GTPase-activating protein (GAP). During border
CC cell migration in the ovary, acts as a GAP for Rab11 and is necessary
CC for the maintenance of active receptor tyrosine kinases at the leading
CC edge. {ECO:0000269|PubMed:22778279}.
CC -!- SUBUNIT: Interacts with Rab11. {ECO:0000269|PubMed:22778279}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22778279}. Endosome
CC {ECO:0000269|PubMed:22778279}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A;
CC IsoId=Q9VYY9-1; Sequence=Displayed;
CC Name=C; Synonyms=E;
CC IsoId=Q9VYY9-3; Sequence=VSP_047764, VSP_037210;
CC Name=D;
CC IsoId=Q9VYY9-4; Sequence=VSP_047764;
CC Name=B;
CC IsoId=Q9VYY9-2; Sequence=VSP_037210;
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DR EMBL; AE014298; AAN09633.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF48044.3; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95256.1; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95257.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95293.1; -; Genomic_DNA.
DR EMBL; AY061021; AAL28569.1; -; mRNA.
DR EMBL; AY118309; AAM48338.1; -; mRNA.
DR EMBL; BT099930; ACX36506.1; -; mRNA.
DR EMBL; BT099932; ACX36508.1; -; mRNA.
DR EMBL; BT126034; ADY17733.1; -; mRNA.
DR RefSeq; NP_001162721.1; NM_001169250.2. [Q9VYY9-3]
DR RefSeq; NP_001162722.1; NM_001169251.4. [Q9VYY9-4]
DR RefSeq; NP_001259450.1; NM_001272521.1. [Q9VYY9-3]
DR RefSeq; NP_572716.3; NM_132488.5. [Q9VYY9-2]
DR RefSeq; NP_727526.2; NM_167285.4. [Q9VYY9-1]
DR AlphaFoldDB; Q9VYY9; -.
DR SMR; Q9VYY9; -.
DR BioGRID; 58499; 4.
DR IntAct; Q9VYY9; 3.
DR STRING; 7227.FBpp0073392; -.
DR iPTMnet; Q9VYY9; -.
DR PaxDb; Q9VYY9; -.
DR PRIDE; Q9VYY9; -.
DR DNASU; 32088; -.
DR EnsemblMetazoa; FBtr0073546; FBpp0073391; FBgn0262740. [Q9VYY9-2]
DR EnsemblMetazoa; FBtr0073547; FBpp0073392; FBgn0262740. [Q9VYY9-1]
DR EnsemblMetazoa; FBtr0300732; FBpp0289956; FBgn0262740. [Q9VYY9-3]
DR EnsemblMetazoa; FBtr0300733; FBpp0289957; FBgn0262740. [Q9VYY9-4]
DR EnsemblMetazoa; FBtr0332620; FBpp0304866; FBgn0262740. [Q9VYY9-3]
DR GeneID; 32088; -.
DR KEGG; dme:Dmel_CG11727; -.
DR UCSC; CG11727-RA; d. melanogaster. [Q9VYY9-1]
DR UCSC; CG11727-RB; d. melanogaster.
DR CTD; 7813; -.
DR FlyBase; FBgn0262740; Evi5.
DR VEuPathDB; VectorBase:FBgn0262740; -.
DR eggNOG; KOG4436; Eukaryota.
DR GeneTree; ENSGT00940000169844; -.
DR InParanoid; Q9VYY9; -.
DR OMA; GHIVADW; -.
DR PhylomeDB; Q9VYY9; -.
DR SignaLink; Q9VYY9; -.
DR BioGRID-ORCS; 32088; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32088; -.
DR PRO; PR:Q9VYY9; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0262740; Expressed in spermathecum and 32 other tissues.
DR Genevisible; Q9VYY9; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:FlyBase.
DR GO; GO:0032880; P:regulation of protein localization; IDA:UniProtKB.
DR InterPro; IPR031214; Evi5.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR PANTHER; PTHR22957:SF254; PTHR22957:SF254; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Endosome; GTPase activation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..807
FT /note="Ecotropic viral integration site 5 ortholog"
FT /id="PRO_0000372854"
FT DOMAIN 116..300
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..463
FT /evidence="ECO:0000255"
FT COILED 494..583
FT /evidence="ECO:0000255"
FT COILED 627..772
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 463..468
FT /note="Missing (in isoform C and isoform D)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047764"
FT VAR_SEQ 763..807
FT /note="LTALKSRGKFPGAKLRSSSIQSIESTEIDFNDLNMVRRGSTELST -> YPT
FT PITSPDTEPWKWIS (in isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.4"
FT /id="VSP_037210"
FT MUTAGEN 160
FT /note="R->A: Does not affect subcellular location or
FT interaction with Rab11. Fails to inactivate Rab11."
FT /evidence="ECO:0000269|PubMed:22778279"
FT CONFLICT 507
FT /note="A -> D (in Ref. 4; ADY17733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 807 AA; 92782 MW; 521E528AA8206748 CRC64;
MTLTTTTTAS SAESQAKMDV KGGALPGEEN LPTSEMDLLA KLEAANKLIE SDAKSLNSLH
STHSRKNSDT SQISLTSSGN SVAEEDIWTT WATILNDWEG ALKRKNPCVS ELVRRGIPHH
FRAIVWQQLS GASDGDKKQY AEYIKATSAC EKVIRRDIAR TYPEVEFFKE KDGPGQEALF
NVIKAYSLHD REVGYCQGSG FIVGLLLMQM PEEEAFAVLV QIMQQHRMRH MFKPSMSELG
LCMYQLENLV QEQIPDMHIH FQQQGFQTTM YASSWFLTLY TTTLNVNLSC RIMDVFLSEG
MEFIFKVALA LLLTGKDTLL CLDMEAMLKF FQKELPGRVE ADVEGFFNLA YSIKLNTKRM
KKMEKEYQDL KKKEQEEMAE LRRLRRENCL LKQRNELLEA ESAELADRLV RGQVSRAEEE
ETSYAIQTEL MQLRRSYLEV SHQLENANEE VRGLSLRLQE NNVSIDSNNS RQSSIDELCM
KEEALKQRDE MVSCLLEELV KVRQGLAESE DQIRNLKAKV EELEEDKKTL RETTPDNSVA
HLQDELIASK LREAEASLSL KDLKQRVQEL SSQWQRQLAE NQRSESERTT NAVDSTPKKL
LTNFFDSSKS SEHTQKLEEE LMTTRIREME TLTELKELRL KVMELETQVQ VSTNQLRRQD
EEHKKLKEEL EMAVTREKDM SNKAREQQHR YSDLESRMKD ELMNVKIKFT EQSQTVAELK
QEISRLETKN SEMLAEGELR ANLDDSDKVR DLQDRLADMK AELTALKSRG KFPGAKLRSS
SIQSIESTEI DFNDLNMVRR GSTELST
