ID   SEC15_YEAST             Reviewed;         910 AA.
AC   P22224; D6VVA1;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=Exocyst complex component SEC15;
GN   Name=SEC15; OrderedLocusNames=YGL233W;
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].
RX   PubMed=2504727; DOI=10.1083/jcb.109.3.1023;
RA   Salminen A., Novick P.J.;
RT   "The Sec15 protein responds to the function of the GTP binding protein,
RT   Sec4, to control vesicular traffic in yeast.";
RL   J. Cell Biol. 109:1023-1036(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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   FUNCTION.
RX   PubMed=1512289; DOI=10.1083/jcb.118.5.1041;
RA   Bowser R., Mueller H., Govindan B., Novick P.;
RT   "Sec8p and Sec15p are components of a plasma membrane-associated 19.5S
RT   particle that may function downstream of Sec4p to control exocytosis.";
RL   J. Cell Biol. 118:1041-1056(1992).
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286, 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).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC       exocytic vesicles with fusion sites on the plasma membrane.
CC       {ECO:0000269|PubMed:1512289}.
CC   -!- SUBUNIT: The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8,
CC       SEC10, SEC15, EXO70 and EXO84. Interacts with SEC4.
CC   -!- INTERACTION:
CC       P22224; P19658: EXO70; NbExp=2; IntAct=EBI-16543, EBI-6717;
CC       P22224; P38261: EXO84; NbExp=3; IntAct=EBI-16543, EBI-21567;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC       protein. Note=25% cytoplasmic. 75% is associated with the cell
CC       membrane.
CC   -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SEC15 family. {ECO:0000305}.
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DR   EMBL; Z72755; CAA96951.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07885.1; -; Genomic_DNA.
DR   PIR; S07838; S07838.
DR   RefSeq; NP_011281.1; NM_001181099.1.
DR   PDB; 5YFP; EM; 4.40 A; F=1-910.
DR   PDB; 6VKL; EM; 4.40 A; F=1-910.
DR   PDBsum; 5YFP; -.
DR   PDBsum; 6VKL; -.
DR   AlphaFoldDB; P22224; -.
DR   SMR; P22224; -.
DR   BioGRID; 33006; 257.
DR   ComplexPortal; CPX-1890; Exocyst.
DR   DIP; DIP-2681N; -.
DR   IntAct; P22224; 24.
DR   MINT; P22224; -.
DR   STRING; 4932.YGL233W; -.
DR   TCDB; 1.F.2.1.1; the octameric exocyst (exocyst) family.
DR   iPTMnet; P22224; -.
DR   MaxQB; P22224; -.
DR   PaxDb; P22224; -.
DR   PRIDE; P22224; -.
DR   EnsemblFungi; YGL233W_mRNA; YGL233W; YGL233W.
DR   GeneID; 852618; -.
DR   KEGG; sce:YGL233W; -.
DR   SGD; S000003202; SEC15.
DR   VEuPathDB; FungiDB:YGL233W; -.
DR   eggNOG; KOG2176; Eukaryota.
DR   GeneTree; ENSGT00390000005739; -.
DR   HOGENOM; CLU_009437_1_0_1; -.
DR   InParanoid; P22224; -.
DR   OMA; RDHYNEV; -.
DR   BioCyc; YEAST:G3O-30707-MON; -.
DR   Reactome; R-SCE-264876; Insulin processing.
DR   PRO; PR:P22224; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P22224; protein.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR   GO; GO:0031267; F:small GTPase binding; IDA:SGD.
DR   GO; GO:0006887; P:exocytosis; IMP:SGD.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:SGD.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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   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; Cell membrane; Coiled coil; Cytoplasm; Exocytosis; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..910
FT                   /note="Exocyst complex component SEC15"
FT                   /id="PRO_0000118959"
FT   COILED          88..116
FT                   /evidence="ECO:0000255"
FT   MOD_RES         286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   910 AA;  105064 MW;  818A5D27A1691D17 CRC64;
     MDQEGQPLLS KDFQQVLLAT ASGNNSSWTE RAVLNNESTD AVKHEPALGQ NDVFDLDPLS
     FDKWVPFLRR ALDKNQLDPV IDELENSIED NFQGLELQLL QDSQMNDKLE TSIDEIANIQ
     GMVQDTLSSE ISKFQIRLSE SANELIVKKQ MYVNNKKISL KISEATILIT KVVRILELSS
     KCQELITERK FFKVLQNLDS LEKLYLQEFK NYNFQFLIEI YNSIPFLQKV TKDECINLIR
     NSLNLNLGKN LIKVGQEFVA IYENELLPQW LETRSKMKLT NFKFNSPIEI SMRDESFLAK
     LNLGEFFQLD DFHDSIMIFQ NLNELSVLSG EFNKEYELRK TKLMYPLIWK KNKTAAYQMD
     SLLRGTGTTP GSTAHDVSTD DPFTQSLSLH FLQDYFLKIL GFLLYDINLN KATEFILVDN
     NYNSTNEFWD GLMDRLSPYL SYFIDEKLKT EEDMIKLKDF LCIYVAILEN FKLNIEPLYK
     ILVSIFEKFC SVSLRAFDDE FQILLNDDDF MPLSINDKTL YEKVLKICWM KEGEHLSLPD
     PTNGEPFAVT LPFSPLYPMT CTLAKKTYSK ITAFLSIFYR HELHTLNNIL VKTMDDIFND
     IVNKKIRSKL ESTSREEIAQ ILVNLDYFII AAKEFSNFMT RENILQNPDM EIRLSSIKYL
     AESRKLAETK LIELIDSKIS DILETIEIDW QITEVRQDPD ISIIDLAQFL EMMFASTLQN
     LPYSVQTLLI FREFDSLTRQ FMGLLLHDTP STITHESIMN FEVDVNYLES IIPRIFPSTP
     GTIDSNGYQS PMTPSTPTFP NANGVDAPTL FENNIKSLEA TFMELKQCIE LLKTQGKDYN
     EPEIRLRKYS RIRQEDAALL LSKIQHFVSS VEGANGDDTS VMDSSSIFNS ESASVIDSNT
     SRIAKFFNRR