SEC3_YEAST
ID SEC3_YEAST Reviewed; 1336 AA.
AC P33332; D3DLQ5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Exocyst complex component SEC3;
DE AltName: Full=Protein PSL1;
GN Name=SEC3; Synonyms=PSL1; OrderedLocusNames=YER008C;
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=8889515; DOI=10.1093/genetics/144.2.495;
RA Haarer B.K., Corbett A., Kweon Y., Petzold A.S., Silver P., Brown S.S.;
RT "SEC3 mutations are synthetically lethal with profilin mutations and cause
RT defects in diploid-specific bud-site selection.";
RL Genetics 144:495-510(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 CHARACTERIZATION.
RX PubMed=9247645; DOI=10.1091/mbc.8.4.647;
RA Finger F.P., Novick P.;
RT "Sec3p is involved in secretion and morphogenesis in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 8:647-662(1997).
RN [5]
RP PROTEIN SEQUENCE OF 793-800.
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-290, 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, 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 [10]
RP IDENTIFICATION BY 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 P33332; P06780: RHO1; NbExp=2; IntAct=EBI-16850, EBI-15121;
CC -!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SEC3 family. {ECO:0000305}.
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DR EMBL; L22204; AAB49380.1; -; Genomic_DNA.
DR EMBL; U18778; AAB64541.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07659.1; -; Genomic_DNA.
DR PIR; S41794; S41794.
DR RefSeq; NP_010924.1; NM_001178899.1.
DR PDB; 3A58; X-ray; 2.60 A; A/C/E=1-320.
DR PDB; 3HIE; X-ray; 2.00 A; A/B/C/D=71-241.
DR PDB; 5LG4; X-ray; 2.90 A; B/C=75-320.
DR PDB; 5M4Y; X-ray; 2.20 A; B/D/F=75-320.
DR PDB; 5YFP; EM; 4.40 A; A=1-1336.
DR PDB; 6VKL; EM; 4.40 A; A=1-1336.
DR PDBsum; 3A58; -.
DR PDBsum; 3HIE; -.
DR PDBsum; 5LG4; -.
DR PDBsum; 5M4Y; -.
DR PDBsum; 5YFP; -.
DR PDBsum; 6VKL; -.
DR AlphaFoldDB; P33332; -.
DR SMR; P33332; -.
DR BioGRID; 36739; 177.
DR ComplexPortal; CPX-1890; Exocyst.
DR DIP; DIP-5992N; -.
DR IntAct; P33332; 17.
DR MINT; P33332; -.
DR STRING; 4932.YER008C; -.
DR TCDB; 1.F.2.1.1; the octameric exocyst (exocyst) family.
DR iPTMnet; P33332; -.
DR MaxQB; P33332; -.
DR PaxDb; P33332; -.
DR PRIDE; P33332; -.
DR EnsemblFungi; YER008C_mRNA; YER008C; YER008C.
DR GeneID; 856726; -.
DR KEGG; sce:YER008C; -.
DR SGD; S000000810; SEC3.
DR VEuPathDB; FungiDB:YER008C; -.
DR eggNOG; ENOG502QSCI; Eukaryota.
DR GeneTree; ENSGT00940000173251; -.
DR HOGENOM; CLU_002075_1_0_1; -.
DR InParanoid; P33332; -.
DR OMA; SFMRVFP; -.
DR BioCyc; YEAST:G3O-30195-MON; -.
DR Reactome; R-SCE-264876; Insulin processing.
DR EvolutionaryTrace; P33332; -.
DR PRO; PR:P33332; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P33332; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA: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; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0031267; F:small GTPase binding; IDA:SGD.
DR GO; GO:0048309; P:endoplasmic reticulum inheritance; IMP:SGD.
DR GO; GO:0001927; P:exocyst assembly; IMP:SGD.
DR GO; GO:0051601; P:exocyst localization; IGI:SGD.
DR GO; GO:0006887; P:exocytosis; IDA: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; IPR028258; Sec3-PIP2_bind.
DR InterPro; IPR019160; Sec3_C.
DR Pfam; PF15277; Sec3-PIP2_bind; 1.
DR Pfam; PF09763; Sec3_C; 1.
DR SMART; SM01313; Sec3-PIP2_bind; 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..1336
FT /note="Exocyst complex component SEC3"
FT /id="PRO_0000118917"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 319..464
FT /evidence="ECO:0000255"
FT COILED 1309..1336
FT /evidence="ECO:0000255"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 290
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 76..93
FT /evidence="ECO:0007829|PDB:3HIE"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5M4Y"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3A58"
FT STRAND 107..123
FT /evidence="ECO:0007829|PDB:3HIE"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3HIE"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:3HIE"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:3HIE"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3A58"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:3HIE"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:3HIE"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:3HIE"
FT STRAND 187..199
FT /evidence="ECO:0007829|PDB:3HIE"
FT HELIX 203..219
FT /evidence="ECO:0007829|PDB:3HIE"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:3A58"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3HIE"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:3HIE"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:5M4Y"
SQ SEQUENCE 1336 AA; 154695 MW; 6F0C1BF13A77985E CRC64;
MRSSKSPFKR KSHSRETSHD ENTSFFHKRT ISGSSAHHSR NVSQGAVPSS APPVSGGNYS
HKRNVSRASN SSQTSNFLAE QYERDRKAII NCCFSRPDHK TGEPPNNYIT HVRIIEDSKF
PSSRPPPDSK LENKKKRLLI LSAKPNNAKL IQIHKARENS DGSFQIGRTW QLTELVRVEK
DLEISEGFIL TMSKKYYWET NSAKERTVFI KSLITLYIQT FEGHVPELVN WDLSLFYLDE
RSYQRAVITN RPGSVSPIKS PTSNFTTNTT QSVGSVPFSA PTERTRRSET ESVNPVSTPA
SVEYHAGMKS LNKAPYSSNS TLNEVNKRYE LEQQQQQEEA ELRRLEEQKR LQLQKENEMK
RLEEERRIKQ EERKRQMELE HQRQLEEEER KRQMELEAKK QMELKRQRQF EEEQRLKKER
ELLEIQRKQR EQETAERLKK EEQEALAKKE EEEKSKRNKV DNESYTQEIN GKVDNLLEDL
NAVLAEETET TPTMQNGTYV PERSTARAHD QLKKPLNIAK VESLGGSDLN DSISLSDEIA
GLNTSNLSGE DQDEKNDLSF EKGDEVRYSN NFEGEAPHVY HEVSIIQEEA PAVSQKLILP
EENNESEALI ESKEEIKTME NIDDEVLLEI LTDINWSIED DADSMIERID LRLAETEYLF
NQNLLSLQKI GPNIRPYEDK VNDECHRIIP TLSLFLMEMS NFSNDIENVE SQDNGLQVES
ANKKLLWNTL DELLKTVSLD EISLNQLLEC PIREKNLPWM ENQLNLLLKA FQAIGSDGNE
VEYNLREISG LKQRLQFYEK VTKIFLNRIV EEMQKKFSNI RGQDISHDQM IRILTTLLIF
SPLILFCKEI SQKSYQAIVE NWNVSIQPVY MELWTKKISQ LQGIDTNDEK MNELSLSQLL
NEWDTFRKER KTNDINPVFK NSFSLLTECL QTMRQECIVY QNFVEVFFHI SSKHNFEEYI
KHFNDPDAPP ILLDTVKVMQ SDREAAVIET QLVSRIFQPI VTRLSSYFVE LVKAEPTVAP
ALTFYLENEI KSLESSNHEF LLSAVTRMYT QIKQVWSDNV EEQVLHFERI SNATTNGEIL
PGILDLPVGL KNSEDLFQFA KRSMDIKDTD EGYESIELMN SSFRKLSIAA TRSITHKEVN
SSINPNLSDT AALNNDYMET ISLLVNSNWL TEMLSMLNFN KDGIFDTSLQ NVKKVFDVEK
ESYASFLLRD TMPKLTAFVY GVSNIIENTN NVNMTNPSRW AAYSRQNLEN ILLAYTSHEI
ETLVKRLHTH MVNDFGYHQE NAINNVLCDK LWSCIQGQTV SLYLKLYTVI DKHYRGTNIR
FTKNDIISAF EEYKNA
