RAB26_DROME
ID RAB26_DROME Reviewed; 388 AA.
AC Q9VP48; Q95R32;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ras-related protein Rab-26;
DE Flags: Precursor;
GN Name=Rab26 {ECO:0000312|EMBL:AAF51708.2}; ORFNames=CG34410;
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] {ECO:0000312|EMBL:AAF51708.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF51708.2}
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] {ECO:0000305, ECO:0000312|EMBL:AAL27637.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND RNA EDITING OF POSITION 365.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL27637.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
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] {ECO:0000305}
RP RNA EDITING OF POSITION 365.
RX PubMed=17018572; DOI=10.1261/rna.254306;
RA Stapleton M., Carlson J.W., Celniker S.E.;
RT "RNA editing in Drosophila melanogaster: new targets and functional
RT consequences.";
RL RNA 12:1922-1932(2006).
CC -!- FUNCTION: Participates in exocrine secretion.
CC {ECO:0000250|UniProtKB:P51156}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51156};
CC Lipid-anchor {ECO:0000250|UniProtKB:P51156}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P51156}.
CC -!- RNA EDITING: Modified_positions=365 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}; Note=Partially edited. Target of Adar.
CC {ECO:0000269|PubMed:17018572};
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000255}.
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DR EMBL; AE014296; AAF51708.2; -; Genomic_DNA.
DR EMBL; AY061826; AAL27637.1; -; mRNA.
DR RefSeq; NP_001287142.1; NM_001300213.1.
DR RefSeq; NP_649303.2; NM_141046.4.
DR AlphaFoldDB; Q9VP48; -.
DR SMR; Q9VP48; -.
DR BioGRID; 65607; 21.
DR IntAct; Q9VP48; 2.
DR PRIDE; Q9VP48; -.
DR DNASU; 40359; -.
DR EnsemblMetazoa; FBtr0112677; FBpp0111589; FBgn0086913.
DR EnsemblMetazoa; FBtr0345428; FBpp0311553; FBgn0086913.
DR GeneID; 40359; -.
DR KEGG; dme:Dmel_CG34410; -.
DR UCSC; CG34410-RB; d. melanogaster.
DR CTD; 25837; -.
DR FlyBase; FBgn0086913; Rab26.
DR VEuPathDB; VectorBase:FBgn0086913; -.
DR eggNOG; KOG0083; Eukaryota.
DR GeneTree; ENSGT00940000167571; -.
DR HOGENOM; CLU_041217_5_0_1; -.
DR InParanoid; Q9VP48; -.
DR OMA; PPRHGYY; -.
DR OrthoDB; 1018397at2759; -.
DR PhylomeDB; Q9VP48; -.
DR Reactome; R-DME-8873719; RAB geranylgeranylation.
DR SignaLink; Q9VP48; -.
DR BioGRID-ORCS; 40359; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Rab26; fly.
DR GenomeRNAi; 40359; -.
DR PRO; PR:Q9VP48; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0086913; Expressed in brain and 5 other tissues.
DR ExpressionAtlas; Q9VP48; baseline and differential.
DR Genevisible; Q9VP48; DM.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; HDA:FlyBase.
DR GO; GO:0045202; C:synapse; HDA:FlyBase.
DR GO; GO:0031982; C:vesicle; ISS:FlyBase.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:FlyBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; ISS:FlyBase.
DR GO; GO:0017157; P:regulation of exocytosis; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:FlyBase.
DR GO; GO:0046718; P:viral entry into host cell; HMP:FlyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Palmitate; Prenylation; Protein transport;
KW Reference proteome; RNA editing; Transport.
FT CHAIN 1..385
FT /note="Ras-related protein Rab-26"
FT /id="PRO_0000274548"
FT PROPEP 386..388
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370824"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 219..228
FT /note="Effector region"
FT /evidence="ECO:0000250|UniProtKB:P35285"
FT COMPBIAS 40..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..113
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197..204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P35285"
FT BINDING 246..250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P35285"
FT BINDING 304..307
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P35285"
FT MOD_RES 385
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 382
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 385
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT VARIANT 365
FT /note="K -> R (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
SQ SEQUENCE 388 AA; 43037 MW; 24F55244CA53493D CRC64;
MASTAVGLGG GEGDPGAGGP PAGSAHPDDA SSMSDDVFED AETTQARIEE LRRRPFGDGS
YNPPAAPASV SASITTTTTQ QQQQHHNPSH HHQSSHHQPS HHHHHHHHSQ LSLTGSHHYH
DDAIMAPVQR SATGYPGYRP SREAMQMYAY GTDDYDDDYN DGWRSYRYDE VDMHPAPSNA
HQQPFDDTVN HKTILLGDSG VGKTSFLVKY NTGEFRLGSF SATVGIALTN KVVVVDGTRV
KLQIWDTAGQ ERFRSVTHAY YRDAHALLLL YDVTNKTTYD NIRAWLGEIR EYAQEDVVIV
LIGNKADCSG SERQVKREDG ERLGREHNVP FMETSAKTGL NVELSFTAVA RQLKSRGYEH
GDDGKFNVHD FVRDNTKARS VCAQCRNM
