EXOC2_DROME
ID EXOC2_DROME Reviewed; 894 AA.
AC Q9VQQ9;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Exocyst complex component 2;
DE AltName: Full=Exocyst complex component Sec5;
GN Name=Sec5 {ECO:0000312|FlyBase:FBgn0266670};
GN ORFNames=CG8843 {ECO:0000312|FlyBase:FBgn0266670};
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).
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|UniProtKB:Q96KP1}.
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. {ECO:0000250|UniProtKB:O54921}.
CC -!- SIMILARITY: Belongs to the SEC5 family. {ECO:0000305}.
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DR EMBL; AE014134; AAF51106.1; -; Genomic_DNA.
DR EMBL; AY069793; AAL39938.1; -; mRNA.
DR RefSeq; NP_608780.1; NM_134936.3.
DR AlphaFoldDB; Q9VQQ9; -.
DR SMR; Q9VQQ9; -.
DR BioGRID; 59774; 59.
DR DIP; DIP-17879N; -.
DR IntAct; Q9VQQ9; 2.
DR STRING; 7227.FBpp0077208; -.
DR PaxDb; Q9VQQ9; -.
DR PRIDE; Q9VQQ9; -.
DR DNASU; 33563; -.
DR EnsemblMetazoa; FBtr0077519; FBpp0077208; FBgn0266670.
DR GeneID; 33563; -.
DR KEGG; dme:Dmel_CG8843; -.
DR UCSC; CG8843-RA; d. melanogaster.
DR CTD; 33563; -.
DR FlyBase; FBgn0266670; Sec5.
DR VEuPathDB; VectorBase:FBgn0266670; -.
DR eggNOG; KOG2347; Eukaryota.
DR GeneTree; ENSGT00390000010872; -.
DR HOGENOM; CLU_005811_1_0_1; -.
DR InParanoid; Q9VQQ9; -.
DR OMA; LFPDACG; -.
DR OrthoDB; 97000at2759; -.
DR PhylomeDB; Q9VQQ9; -.
DR Reactome; R-DME-264876; Insulin processing.
DR Reactome; R-DME-5620916; VxPx cargo-targeting to cilium.
DR SignaLink; Q9VQQ9; -.
DR BioGRID-ORCS; 33563; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33563; -.
DR PRO; PR:Q9VQQ9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0266670; Expressed in oviduct (Drosophila) and 26 other tissues.
DR Genevisible; Q9VQQ9; DM.
DR GO; GO:0005642; C:annulate lamellae; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0000145; C:exocyst; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0055037; C:recycling endosome; IDA:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0035003; C:subapical complex; IDA:FlyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0032456; P:endocytic recycling; IMP:FlyBase.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:FlyBase.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IDA:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR GO; GO:0048599; P:oocyte development; IMP:FlyBase.
DR GO; GO:0048215; P:positive regulation of Golgi vesicle fusion to target membrane; IMP:FlyBase.
DR GO; GO:0071896; P:protein localization to adherens junction; IMP:FlyBase.
DR GO; GO:0072697; P:protein localization to cell cortex; IMP:FlyBase.
DR GO; GO:0072657; P:protein localization to membrane; IDA:FlyBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:FlyBase.
DR GO; GO:0060074; P:synapse maturation; IDA:SynGO.
DR GO; GO:0016081; P:synaptic vesicle docking; NAS:FlyBase.
DR GO; GO:0016080; P:synaptic vesicle targeting; NAS:FlyBase.
DR GO; GO:0045056; P:transcytosis; IMP:FlyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:FlyBase.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR029175; EXOC2/Sec5.
DR InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR PANTHER; PTHR13043; PTHR13043; 1.
DR Pfam; PF15469; Sec5; 1.
DR Pfam; PF01833; TIG; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Exocytosis; Protein transport; Reference proteome; Transport.
FT CHAIN 1..894
FT /note="Exocyst complex component 2"
FT /id="PRO_0000118922"
FT DOMAIN 5..89
FT /note="IPT/TIG"
FT REGION 398..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 100729 MW; 3BE241DAAD7963D9 CRC64;
MAPQPVVTGL SPKEGPPGTR VIIRGEFLGT RVQDLIGLKI CGSDCLLSAE WKSPNKIIAR
TGPAKGKGDI IVTTLSGGVG TSTVQFRAYH ETIGPLKESA VWIEESPSQN FAWGRRTLAQ
SGLTQEDPLG LSIEGNEQKI PEDLRDLFPE ACGDLSQEHF SPAWFLLENH LATSFEDLKA
GLSYLKRKVE SQKEGQLSFL KSNAGSVIDQ LDTLMNIRDK LQEDVKLHGN ETLNILETSI
ENSISESQKI FTDVLVRKEK ADSTRSVLFA LSRHKFLFCL PNSVDRRAKA GEYDIVVNDY
SRAKNLFGKT EIPIFRKVLE EVDHRILSIR KQLHEKVVKM PQSVEQQKKL IKALISLELQ
QSGTPIGDKL RNIDPAWDAI EARAKYLEWT FRQTFDQHTS KDSGAQEKAK NRDSSQAPNR
VNFCEELCDI AASQLPDLWR LGQLYFTGEL RGPHDPKPGD FKRMVLNAIE KFCVYLRLAI
LIATDQRALR QSSGLAWPIG SASATHQFLP WIPQCLRFTR IAYATLISLD LPSEALDIIQ
KLIDEVRLFC FSIIFKRATD RCKKLGSQET WELGVEEYPG ATLLPAALET LLIETLDEVQ
SVCMQRETRE GNLLEPQSDG QREVTQRLQE FLSAFSAVIE ELAFHSHDEE TPTHNVSQLL
GFPNAQQPDS VAGSGGAAAV TWEQRMLCCL ANYAYCNKIF FPRLGDIFVR YGYPLPTLAI
ETARYTVNQL FTNLLEEYVE HKGDPLVGTI EPSMYLGRFQ WDHEMEIGQL RPYAHECCDN
LVGVYSEIYS ISPALLRPIL ESIVQTISEE LARLMSCVQR FSFTGAIQAH VDIRLLRDSL
EGYVNETAKN YFMEALEAIN PPLSGEQKRK ADEILERVKR NMRLQLLCFS VKDP
