EXOC4_DROME
ID EXOC4_DROME Reviewed; 985 AA.
AC Q9VNH6; Q5ECP5;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Exocyst complex component 4;
DE AltName: Full=Exocyst complex component Sec8;
GN Name=Sec8 {ECO:0000312|FlyBase:FBgn0266672};
GN ORFNames=CG2095 {ECO:0000312|FlyBase:FBgn0266672};
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Oregon-R;
RX PubMed=16351720; DOI=10.1186/1741-7007-3-27;
RA Liebl F.L.W., Chen K., Karr J., Sheng Q., Featherstone D.E.;
RT "Increased synaptic microtubules and altered synapse development in
RT Drosophila sec8 mutants.";
RL BMC Biol. 3:27-27(2005).
RN [2]
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 [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-456; SER-459;
RP SER-682 AND SER-686, 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: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane. Involved in
CC regulation of synaptic microtubule formation, and also regulation of
CC synaptic growth and glutamate receptor trafficking. Does not appear to
CC be required for basal neurotransmission. {ECO:0000269|PubMed:16351720}.
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}.
CC -!- TISSUE SPECIFICITY: Abundant in the embryonic and larval glutamatergic
CC neuromuscular junctions (NMJs), pre and postsynaptically.
CC {ECO:0000269|PubMed:16351720}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:16351720}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit defects in development of
CC glutamatergic neuromuscular junctions (NMJs): increase in synaptic
CC microtubule density. {ECO:0000269|PubMed:16351720}.
CC -!- SIMILARITY: Belongs to the SEC8 family. {ECO:0000305}.
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DR EMBL; AY905551; AAW83821.1; -; mRNA.
DR EMBL; AE014297; AAF51959.3; -; Genomic_DNA.
DR EMBL; AY119660; AAM50314.1; -; mRNA.
DR RefSeq; NP_730996.2; NM_169098.4.
DR AlphaFoldDB; Q9VNH6; -.
DR SMR; Q9VNH6; -.
DR BioGRID; 65917; 9.
DR DIP; DIP-21395N; -.
DR IntAct; Q9VNH6; 6.
DR STRING; 7227.FBpp0078326; -.
DR iPTMnet; Q9VNH6; -.
DR PaxDb; Q9VNH6; -.
DR PRIDE; Q9VNH6; -.
DR EnsemblMetazoa; FBtr0078677; FBpp0078326; FBgn0266672.
DR GeneID; 40712; -.
DR KEGG; dme:Dmel_CG2095; -.
DR UCSC; CG2095-RA; d. melanogaster.
DR CTD; 40712; -.
DR FlyBase; FBgn0266672; Sec8.
DR VEuPathDB; VectorBase:FBgn0266672; -.
DR eggNOG; KOG3691; Eukaryota.
DR HOGENOM; CLU_012416_0_0_1; -.
DR InParanoid; Q9VNH6; -.
DR OMA; SLPNWTD; -.
DR OrthoDB; 96167at2759; -.
DR PhylomeDB; Q9VNH6; -.
DR Reactome; R-DME-264876; Insulin processing.
DR Reactome; R-DME-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 40712; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40712; -.
DR PRO; PR:Q9VNH6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0266672; Expressed in embryonic/larval hemocyte (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q9VNH6; baseline and differential.
DR Genevisible; Q9VNH6; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0009925; C:basal plasma membrane; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0000145; C:exocyst; IDA:FlyBase.
DR GO; GO:0032584; C:growth cone membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0000916; P:actomyosin contractile ring contraction; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
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:0007110; P:meiosis I cytokinesis; IMP:FlyBase.
DR GO; GO:0007111; P:meiosis II cytokinesis; IMP:FlyBase.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR GO; GO:0007009; P:plasma membrane organization; IDA:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IMP:FlyBase.
DR GO; GO:0007286; P:spermatid development; IMP:FlyBase.
DR GO; GO:0016081; P:synaptic vesicle docking; NAS:FlyBase.
DR GO; GO:0016080; P:synaptic vesicle targeting; NAS:FlyBase.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:FlyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:FlyBase.
DR GO; GO:0046718; P:viral entry into host cell; HMP:FlyBase.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR039682; Sec8/EXOC4.
DR InterPro; IPR007191; Sec8_exocyst_N.
DR PANTHER; PTHR14146; PTHR14146; 1.
DR Pfam; PF02828; L27; 1.
DR Pfam; PF04048; Sec8_exocyst; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Exocytosis; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..985
FT /note="Exocyst complex component 4"
FT /id="PRO_0000118938"
FT REGION 434..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 36..70
FT /evidence="ECO:0000255"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 118
FT /note="M -> T (in Ref. 1; AAW83821 and 4; AAM50314)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="E -> D (in Ref. 4; AAM50314)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="D -> N (in Ref. 1; AAW83821)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="S -> T (in Ref. 4; AAM50314)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="Y -> S (in Ref. 1; AAW83821 and 4; AAM50314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 985 AA; 111667 MW; 6BFB0D9C539FEBE7 CRC64;
MDAPPPTKPP RGVKYGKDES AGCGFLVNVI KSLGFSETTE ERQKEKQKIE AEFKRSDLRL
NELVSRHDQQ LTQVLPLFSQ VSSEVTASRE RIHAVKENLG VCKRLLQCRR DELRKMWMDA
VQHKYVLEML EQIQELRKVP QRVVGYTAKR QYLHASKALT DALTTLNGPL QAVEGLSDLR
TDLQTRRQQL YQRLHEELVT QVYTNSANEA LSSFQRTNSS RLNSSFTRGI GARRSTDRIE
ANARVRKALA EMAQSFDLDK AEVIEDADLI YPELSMSYFV AIIVESFGML HKVPDSLETL
RVQIQTELLN VVRHTTHQLS VSGATADTNP LLSLLEVIFK QFKAIAKTHS LLLKNYLSVG
QKYSVVGPQP YDLTDFWAQA QSVLQLLLTD YLDIQNAAAD ESAQTGFSEP TSNINSYFLR
RKVPSTKRSM FKFDKSSHVG TSNNSDAFKE HRRNASDASV DDNLAGQLGG SGKGSTSGLF
PHEKKQREKI LICTPDQSII TKVYLPLMGY IKEIENFMKC KPGQPCSLHD FLDNYIKDTF
LTKGHNRNLQ LTIESLSKNQ DAWRTIISPE EIKALNLSRP LLQSTVMVER RLMETKNLIQ
DLPCYSEDLL KMVCALLKAY REICQAAYRG IVQPDSEDKR IYSVAWLKDE DISRFLKTLP
NWTDLKTYSQ KSRHNRKLHR GSFEPSEEES PLQVQQRNIR EAEMLTSNLG EGGITQQEIL
VEISVLKELA ILQESMEWFS CRVSEFANDL RRPLVNGLNA VPAECGADIA VKDGTIKVMT
NLALEFDELA NTCLLVLHLE VRVQCFHYLR SKSSVRTNSY VGSKDDILEP DRQVQVLTKR
LSEMDEAFSA TLHPRKTRYI FEGLAHLASR ILIQASNYLE HIDQITVQRM CRNAIALQQT
LSNITASREV ALDQARHFYE LLCMEPDEIL NALLERGTQF SEMQLLNALQ LSCKSFGITD
ANLLASYQQK LSDILGAKPS KGVVV
