EXOC6_DROME
ID EXOC6_DROME Reviewed; 766 AA.
AC Q9VDE6; Q53YF7;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Exocyst complex component 6;
DE AltName: Full=Exocyst complex component Sec15;
GN Name=Sec15 {ECO:0000312|FlyBase:FBgn0266674};
GN ORFNames=CG7034 {ECO:0000312|FlyBase:FBgn0266674};
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;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 382-699, INTERACTION WITH RAB3;
RP RAB8; RAB11 AND RAB27, MUTAGENESIS OF ASN-659; MET-663 AND PHE-667, AND
RP TISSUE SPECIFICITY.
RX PubMed=16155582; DOI=10.1038/nsmb987;
RA Wu S., Mehta S.Q., Pichaud F., Bellen H.J., Quiocho F.A.;
RT "Sec15 interacts with Rab11 via a novel domain and affects Rab11
RT localization in vivo.";
RL Nat. Struct. Mol. Biol. 12:879-885(2005).
CC -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane.
CC {ECO:0000250}.
CC -!- SUBUNIT: The exocyst complex is composed of Sec3/Exoc1, Sec5/Exoc2,
CC Sec6/Exoc3, Sec8/Exoc4, Sec10/Exoc5, Sec15/Exoc6, Exo70/Exoc7 and
CC Exo84/Exoc8 (By similarity). Interacts with RAB3, RAB8, RAB11 and
CC RAB27. {ECO:0000250, ECO:0000269|PubMed:16155582}.
CC -!- TISSUE SPECIFICITY: Detected in developing rhabdomeres in photoreceptor
CC cells. {ECO:0000269|PubMed:16155582}.
CC -!- SIMILARITY: Belongs to the SEC15 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF55848.1; -; Genomic_DNA.
DR EMBL; BT003492; AAO39495.1; -; mRNA.
DR RefSeq; NP_650942.1; NM_142685.3.
DR PDB; 2A2F; X-ray; 2.50 A; X=382-699.
DR PDBsum; 2A2F; -.
DR AlphaFoldDB; Q9VDE6; -.
DR SMR; Q9VDE6; -.
DR BioGRID; 67470; 12.
DR DIP; DIP-24010N; -.
DR IntAct; Q9VDE6; 2.
DR STRING; 7227.FBpp0083436; -.
DR PaxDb; Q9VDE6; -.
DR PRIDE; Q9VDE6; -.
DR DNASU; 42499; -.
DR EnsemblMetazoa; FBtr0084034; FBpp0083436; FBgn0266674.
DR GeneID; 42499; -.
DR KEGG; dme:Dmel_CG7034; -.
DR UCSC; CG7034-RA; d. melanogaster.
DR CTD; 42499; -.
DR FlyBase; FBgn0266674; Sec15.
DR VEuPathDB; VectorBase:FBgn0266674; -.
DR eggNOG; KOG2176; Eukaryota.
DR GeneTree; ENSGT00390000005739; -.
DR HOGENOM; CLU_009437_0_0_1; -.
DR InParanoid; Q9VDE6; -.
DR OMA; RDHYNEV; -.
DR OrthoDB; 185623at2759; -.
DR PhylomeDB; Q9VDE6; -.
DR Reactome; R-DME-264876; Insulin processing.
DR Reactome; R-DME-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 42499; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q9VDE6; -.
DR GenomeRNAi; 42499; -.
DR PRO; PR:Q9VDE6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0266674; Expressed in oocyte and 21 other tissues.
DR Genevisible; Q9VDE6; DM.
DR GO; GO:0043679; C:axon terminus; IDA:FlyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
DR GO; GO:0005768; C:endosome; IDA:FlyBase.
DR GO; GO:0000145; C:exocyst; IDA:FlyBase.
DR GO; GO:0055037; C:recycling endosome; IDA:FlyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0032456; P:endocytic recycling; IMP:FlyBase.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0042331; P:phototaxis; IMP:FlyBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:FlyBase.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:FlyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:FlyBase.
DR Gene3D; 1.10.357.30; -; 1.
DR Gene3D; 1.20.58.670; -; 1.
DR InterPro; IPR007225; EXOC6/Sec15.
DR InterPro; IPR042045; EXOC6/Sec15_C_dom1.
DR InterPro; IPR042044; EXOC6PINT-1/Sec15/Tip20_C_dom2.
DR InterPro; IPR046361; Sec15_C.
DR PANTHER; PTHR12702; PTHR12702; 1.
DR Pfam; PF04091; Sec15; 1.
DR PIRSF; PIRSF025007; Sec15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Exocytosis; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..766
FT /note="Exocyst complex component 6"
FT /id="PRO_0000118956"
FT COILED 28..90
FT /evidence="ECO:0000255"
FT MUTAGEN 659
FT /note="N->A: Disrupts interaction with RAB11."
FT /evidence="ECO:0000269|PubMed:16155582"
FT MUTAGEN 663
FT /note="M->A: Disrupts interaction with RAB11."
FT /evidence="ECO:0000269|PubMed:16155582"
FT MUTAGEN 667
FT /note="F->A: Disrupts interaction with RAB11."
FT /evidence="ECO:0000269|PubMed:16155582"
FT HELIX 384..415
FT /evidence="ECO:0007829|PDB:2A2F"
FT HELIX 425..432
FT /evidence="ECO:0007829|PDB:2A2F"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:2A2F"
FT HELIX 456..477
FT /evidence="ECO:0007829|PDB:2A2F"
FT HELIX 482..509
FT /evidence="ECO:0007829|PDB:2A2F"
FT HELIX 516..530
FT /evidence="ECO:0007829|PDB:2A2F"
FT HELIX 533..544
FT /evidence="ECO:0007829|PDB:2A2F"
FT HELIX 564..581
FT /evidence="ECO:0007829|PDB:2A2F"
FT HELIX 599..613
FT /evidence="ECO:0007829|PDB:2A2F"
FT TURN 614..618
FT /evidence="ECO:0007829|PDB:2A2F"
FT HELIX 620..642
FT /evidence="ECO:0007829|PDB:2A2F"
FT HELIX 655..669
FT /evidence="ECO:0007829|PDB:2A2F"
FT STRAND 673..676
FT /evidence="ECO:0007829|PDB:2A2F"
FT HELIX 683..686
FT /evidence="ECO:0007829|PDB:2A2F"
FT HELIX 687..697
FT /evidence="ECO:0007829|PDB:2A2F"
SQ SEQUENCE 766 AA; 88726 MW; AACCE87335922C13 CRC64;
MSKVTVQDIE AVDDYWGPTF RSILEGNNTK QIGDQLEQRI RSHDKEIERI CNLYYQGFID
SIQELLQVRT QAQQLHNEVH SLDTSLRQIS ASLIQQGNDL VRARQIESNL ASAIEALKSC
LPALECYMKF TQQAKNKQYY QALRTLETLE TEHLTRLKTH NYRFATQMQI QIPIIKENIR
RSSASDFREF LENIRKFSPR IGELAITHTK QLQKRDINAI IAEHMQQMNG GEAGGAGAGG
DDDGANVSAQ DLIDFSPIYR CLHIYMVLGQ REYFEKDYRQ QRRDQAKLVL QPPPNMHDNL
EAYKTYICAI VGFFVVEDHV KNTAGDVVTS SYLEDLWSSS LTKFVNEISM SSSSCTDPNI
LLRIKNLIML SINTFKCYGY TVNILWELLH NMRDHYNEVL LQRWVHVFRE ILDKEQFLPM
VVQNTEEYEC IIERFPFHSE QLENAPFPKK FPFSRMVPEV YHQAKEFMYA CMKFAEELTL
SPNEVAAMVR KAANLLLTRS FSGCLSVVFR QPSITLTQLI QIIIDTQYLE KAGPFLDEFV
CHMTNTERSV SQTPSAMFHV ARQDAEKQVG LRICSKIDEF FELSAYDWLL VEPPGIASAF
ITDMISYLKS TFDSFAFKLP HIAQAACRRT FEHIAEKIYS IMYDEDVKQI STGALTQINL
DLMQCEFFAA SEPVPGLKEG ELSKYFLRNR QLLDLLILEE WSTYFHDYGK QENRYHLVQP
QSIIVILEKI READKKPIFS LVRKNDKKKL LETVLKQLKH IADRQN
