RME6_DROME
ID RME6_DROME Reviewed; 1712 AA.
AC Q9VZ08; B4YWV1; Q95RG2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Receptor-mediated endocytosis protein 6 homolog;
GN ORFNames=CG1657;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 345-555.
RC STRAIN=Co, Ga, Ken48, KK, KM, La79, MD, ML, MW6, NK, NM, Nr, OK17, ZH1, and
RC ZS5;
RX PubMed=18535209; DOI=10.1126/science.1158078;
RA Emerson J.J., Cardoso-Moreira M., Borevitz J.O., Long M.;
RT "Natural selection shapes genome-wide patterns of copy-number polymorphism
RT in Drosophila melanogaster.";
RL Science 320:1629-1631(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645; SER-646; SER-834;
RP SER-890; SER-893 AND SER-1154, AND 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: Acts both as a GTPase-activating protein (GAP) and a guanine
CC nucleotide exchange factor (GEF), and participates in endocytosis.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GAPVD1 family. {ECO:0000305}.
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DR EMBL; AE014298; AAF48024.2; -; Genomic_DNA.
DR EMBL; AY061391; AAL28939.1; -; mRNA.
DR EMBL; EU706774; ACF28014.1; -; Genomic_DNA.
DR EMBL; EU706775; ACF28015.1; -; Genomic_DNA.
DR EMBL; EU706776; ACF28016.1; -; Genomic_DNA.
DR EMBL; EU706777; ACF28017.1; -; Genomic_DNA.
DR EMBL; EU706778; ACF28018.1; -; Genomic_DNA.
DR EMBL; EU706779; ACF28019.1; -; Genomic_DNA.
DR EMBL; EU706780; ACF28020.1; -; Genomic_DNA.
DR EMBL; EU706781; ACF28021.1; -; Genomic_DNA.
DR EMBL; EU706782; ACF28022.1; -; Genomic_DNA.
DR EMBL; EU706783; ACF28023.1; -; Genomic_DNA.
DR EMBL; EU706784; ACF28024.1; -; Genomic_DNA.
DR EMBL; EU706785; ACF28025.1; -; Genomic_DNA.
DR EMBL; EU706786; ACF28026.1; -; Genomic_DNA.
DR EMBL; EU706787; ACF28027.1; -; Genomic_DNA.
DR EMBL; EU706788; ACF28028.1; -; Genomic_DNA.
DR RefSeq; NP_572704.1; NM_132476.3.
DR AlphaFoldDB; Q9VZ08; -.
DR SMR; Q9VZ08; -.
DR STRING; 7227.FBpp0073304; -.
DR iPTMnet; Q9VZ08; -.
DR PaxDb; Q9VZ08; -.
DR PRIDE; Q9VZ08; -.
DR DNASU; 32070; -.
DR EnsemblMetazoa; FBtr0073448; FBpp0073304; FBgn0030286.
DR GeneID; 32070; -.
DR KEGG; dme:Dmel_CG1657; -.
DR UCSC; CG1657-RA; d. melanogaster.
DR CTD; 26130; -.
DR FlyBase; FBgn0030286; CG1657.
DR VEuPathDB; VectorBase:FBgn0030286; -.
DR eggNOG; KOG2319; Eukaryota.
DR GeneTree; ENSGT00940000156611; -.
DR HOGENOM; CLU_002165_1_0_1; -.
DR InParanoid; Q9VZ08; -.
DR OMA; SCFLGKK; -.
DR OrthoDB; 944088at2759; -.
DR PhylomeDB; Q9VZ08; -.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 32070; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32070; -.
DR PRO; PR:Q9VZ08; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030286; Expressed in cleaving embryo and 23 other tissues.
DR Genevisible; Q9VZ08; DM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032794; F:GTPase activating protein binding; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0051223; P:regulation of protein transport; ISS:UniProtKB.
DR GO; GO:0032483; P:regulation of Rab protein signal transduction; ISM:FlyBase.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 1.20.1050.80; -; 1.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR23101; PTHR23101; 1.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endocytosis; GTPase activation;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1712
FT /note="Receptor-mediated endocytosis protein 6 homolog"
FT /id="PRO_0000324776"
FT DOMAIN 141..362
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 1573..1712
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REGION 438..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1317..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1452..1520
FT /evidence="ECO:0000255"
FT COMPBIAS 440..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..876
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1004
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 1712 AA; 191221 MW; 142CCC89358976EB CRC64;
MEPPAAGNLL EIMDLARTLR QEQLFIQQEQ AAFAQLTGAF ESNAGTITKL AFVCAQQRQI
LNELLLARTD QDPLLFCRRA SAYDSAQFVD AKQLLPYEHA LAYEDLFNYL YNTPYLLALS
LATADRLSLL SASQLGQIIN TIATGLYGNA INTKDVELLL KLLRELIEIQ LLTSEQPRRL
LRTNSSSFAR LYQRLVESLF SARIFLTAAL HAPLMGVLSE HEIWLDLDPH KLMQTFTPKE
REKRFGREGD EEYQRNVARF HAETLGKLHS HVQEFVKSLQ QSWALFPSSL RWLLQTLSQQ
LRQSLRHEEQ EIRQLLTDLV FTHFISPAIA SADLLGIIDV NVSERMRHNL NQIVKLLQRL
ALNDEDSELV QLMELLMLGQ TGEDVVAILP QQSDFERSQL AINQRELAQL VEFFRLLTAR
DEYDISVEER QRLQRILGRI PKQQVQQQQQ TPKDAPDSRE SPEKSKKSNK SLMSLGKAKK
KLAKGMSFSS GSSNHNPVPV SEPLTNGQAN TSNGSGGLGA DLEHCSSHSG SNTSLSSCGA
NMPTTNDPLD MSTSSDPVLV FSLYNAGAKS KLKPLTEEEV LKMNSIGQDG SNLLPAVVTT
APLAPSSNND DVSSLEAMRR PQDDASIGNS DNLEAISEAA HSVASSLDLE EQQERDVHEN
EDNLSDMVSA NVSGRGTPNI SGRDTPSSQV TDGDGAGGDL GHHHGVHARA AANPQMQKML
LSKARSDIED KFCKFELKKF EGDENVSIIS DTWSTDVLAS DSENTLDATV SERGDRDRNF
STPLIPSAVV LPGDNNFVVE ALARAGRVSG VHGPQLDASD QRSESNWSTD VLASDSEKLA
EIDTDDNVSI TTKSDTTAPQ AAVLDDDDED EQTPGSSGDG EPDPDRGNGS ERSQEDSAFF
DAVNSYEDAN LYHGASSLAR SSVRTSYHVL GGESSFQQQY KCSGADSSGR KTTPLMGTSC
MRRQTSAESS ISNQSLNLEE PPPPMGKHHH HHREHHHRDY HHHHRERERE RERERSALKK
KKHQQQEKEH RDLIDFSDCS EDKEELARNR DEEQPPGLVQ QLLDMINQDE QTGAVSSSSP
NVEHRRISIE QRSAIIDGRR NGILAGSMRR HQSLNYENHE IMLNSMLPKT DDDKQEMLLC
VQTQQLQLEE RRGSAGLRPE VDGASGIAAA GGSGLKPPTK ATGAIPKSIS FDASADKDKQ
TYHRDGERDR ERDRERERDR ERDRERDRER DRERDHHGAG IFNKLRQGIF KNRRGASAKN
ASNSSNQSNP AASTSSVQAD IRSVSFDPSA GCDNFGTHYC DTSEDILAKY RRKVSSSSEA
TNSDSTGNGH GVGSTGSVGA AAHLHKHMNG GHIPGVVFGC VKQKLRTVLS RTDLHSGDFR
QTSTTSTTMA TPLQIYLQIQ LAQCISLQRL PQISHVAEAL RCLAQLERPQ HGQLLAELQR
DLERRQSYLQ YLMRHRQQLL LRSEQLEQLE ARLRGEARSS QRCLLQALVR MYLAWSRQQE
KLEQFQAEFA QLRASDERVE LTEEFVESLL QELRSSADLQ DEWQVDAARV AIERMLLEQM
YEQVMFPNED ADVSRDEVLS AHIGKLQRFV HPAHPALCIA QEYLGEAPWT FAQQQLCHMA
AYKTPREKLQ CIINCISSIM SLLRMSSGRV PAADDLLPVL IYVVIMANPP YLLSTVEYIS
CFLGKKLEGE DEFYWTLFGS VVKFIKTMDY LD
