SEC5_YEAST
ID SEC5_YEAST Reviewed; 971 AA.
AC P89102; D6VSE6; Q03775; Q04128;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Exocyst complex component SEC5;
GN Name=SEC5; OrderedLocusNames=YDR166C; ORFNames=YD8358.20C, YD9489.01C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 69-80.
RX PubMed=8978675; DOI=10.1002/j.1460-2075.1996.tb01039.x;
RA TerBush D.R., Maurice T., Roth D., Novick P.;
RT "The Exocyst is a multiprotein complex required for exocytosis in
RT Saccharomyces cerevisiae.";
RL EMBO J. 15:6483-6494(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane.
CC -!- SUBUNIT: The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8,
CC SEC10, SEC15, EXO70 and EXO84.
CC -!- INTERACTION:
CC P89102; P38261: EXO84; NbExp=5; IntAct=EBI-16865, EBI-21567;
CC P89102; P32844: SEC6; NbExp=3; IntAct=EBI-16865, EBI-16874;
CC -!- MISCELLANEOUS: Present with 3400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SEC5 family. {ECO:0000305}.
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DR EMBL; Y08788; CAA70040.1; -; Genomic_DNA.
DR EMBL; Z47813; CAA87797.1; -; Genomic_DNA.
DR EMBL; Z50046; CAA90386.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12006.1; -; Genomic_DNA.
DR PIR; S50912; S50912.
DR RefSeq; NP_010450.3; NM_001180473.3.
DR PDB; 5YFP; EM; 4.40 A; B=1-971.
DR PDB; 6VKL; EM; 4.40 A; B=1-971.
DR PDBsum; 5YFP; -.
DR PDBsum; 6VKL; -.
DR AlphaFoldDB; P89102; -.
DR SMR; P89102; -.
DR BioGRID; 32217; 127.
DR ComplexPortal; CPX-1890; Exocyst.
DR DIP; DIP-2579N; -.
DR IntAct; P89102; 15.
DR MINT; P89102; -.
DR STRING; 4932.YDR166C; -.
DR TCDB; 1.F.2.1.1; the octameric exocyst (exocyst) family.
DR iPTMnet; P89102; -.
DR MaxQB; P89102; -.
DR PaxDb; P89102; -.
DR PRIDE; P89102; -.
DR EnsemblFungi; YDR166C_mRNA; YDR166C; YDR166C.
DR GeneID; 851744; -.
DR KEGG; sce:YDR166C; -.
DR SGD; S000002573; SEC5.
DR VEuPathDB; FungiDB:YDR166C; -.
DR eggNOG; KOG2347; Eukaryota.
DR GeneTree; ENSGT00390000010872; -.
DR HOGENOM; CLU_339546_0_0_1; -.
DR InParanoid; P89102; -.
DR OMA; SQFYDLE; -.
DR BioCyc; YEAST:G3O-29755-MON; -.
DR Reactome; R-SCE-264876; Insulin processing.
DR PRO; PR:P89102; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P89102; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0000145; C:exocyst; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0048309; P:endoplasmic reticulum inheritance; IMP:SGD.
DR GO; GO:0001927; P:exocyst assembly; IMP:SGD.
DR GO; GO:0006887; P:exocytosis; IMP:SGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IC:ComplexPortal.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:SGD.
DR InterPro; IPR029175; EXOC2/Sec5.
DR InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR PANTHER; PTHR13043; PTHR13043; 1.
DR Pfam; PF15469; Sec5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Direct protein sequencing; Exocytosis;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..971
FT /note="Exocyst complex component SEC5"
FT /id="PRO_0000118924"
FT REGION 558..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 123..182
FT /evidence="ECO:0000255"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 971 AA; 112121 MW; E41AC5A15CE3D1DF CRC64;
MDRFQIGDEQ LLRFYQLKTI NPTHSWAQDS SKLNNEEATS NELGVETSFD ILKDFKYGNQ
ISIDKESRAY LNDESLSYIR DPLNGQEMSK ELQHLPNDSM RLNYLVNSKQ FNVKAFLRDM
HKQDSFNDLN NSLDRLDSDI QDQSIHLKQL VGKNFTKYVK IKNKLDQIYK EFDEKTNEKN
QCDSPKENQI NVESLNKKVD EVIRTTTFKL KPLMDNYQKI LNYQATKKFI ELNKFYFNLP
KSLKRCLTNN DFNEFIIEYS KGLTLRRRFN QSSDASQSLV IKRIWTQIEN LLVTYKDLIW
NSLINSNFNI DQPQETILSL FSKLLNLENF INNNQRESES GNKNTTSSSN ENPILRWMSI
KMNGFQNELN ELSGHMISKI IHSQRLILQN NTNQDKSQGC VELSYYLKIN QLFQIISDTG
KDSEGLKSTV EPNKVNTISG TSYLNLNCQP SSQGLTDSPT IIEMWLLILK YINDLWKICD
QFIEFWEHIE KFLDGTYQNS IINEKRKENI LIGDSNIIES YQKSLILKEE QINEVRLKGE
EFITSVSQNL ISFFTSSQSS LPSSLKDSTG DITRSNKDSG SPLDYGFIPP NCNGLSCLRY
LPKIVEPILK FSTELAQLNI TTNGITICRN TLSTIINRCV GAISSTKLRD ISNFYQLENW
QVYETVTFSS KSQDSSKNLT FEYGVTQFPE IVTSFQEVSI KTTRDLLFAY EKLPIINGIS
VVSYPSKQLL TGIEIQQIIS MEAVLEAILK NAAKDKDNPR NSHTILTLTN LQYFRECAFP
NILQYFDDAF EWNLASKNLE LFSLLSKMES SIFGNYLSDL KINLRDTLEE KFHEINWPMY
TSNSFRVGDY IIEALMILIV VHSECFRIGP QLIHKILIET QIFIARYLFE AFKPYVGNLS
NDGSLQIIVD LEFFQKVMGP LLEKDTEATL RACLQNCFQN DTNRLQKCIN EINPIVSANL
KRTAIQFAAF S
