SEC10_YEAST
ID SEC10_YEAST Reviewed; 871 AA.
AC Q06245; D6VYH2; P87329;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Exocyst complex component SEC10;
GN Name=SEC10; OrderedLocusNames=YLR166C; ORFNames=L9362.12;
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 347-353 AND
RP 856-867.
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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-142 AND SER-485, AND
RP IDENTIFICATION BY 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-485 AND SER-507, AND
RP IDENTIFICATION BY 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-485, 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 Q06245; P19658: EXO70; NbExp=2; IntAct=EBI-16504, EBI-6717;
CC Q06245; P38261: EXO84; NbExp=5; IntAct=EBI-16504, EBI-21567;
CC Q06245; P32844: SEC6; NbExp=2; IntAct=EBI-16504, EBI-16874;
CC -!- MISCELLANEOUS: Present with 2340 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SEC10 family. {ECO:0000305}.
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DR EMBL; Y08789; CAA70041.1; -; Genomic_DNA.
DR EMBL; U51921; AAB67490.1; -; Genomic_DNA.
DR EMBL; U17246; AAB67476.2; -; Genomic_DNA.
DR EMBL; BK006945; DAA09488.1; -; Genomic_DNA.
DR PIR; S68482; S68482.
DR RefSeq; NP_013267.1; NM_001182053.1.
DR PDB; 5YFP; EM; 4.40 A; E=1-871.
DR PDB; 6VKL; EM; 4.40 A; E=1-871.
DR PDBsum; 5YFP; -.
DR PDBsum; 6VKL; -.
DR AlphaFoldDB; Q06245; -.
DR SMR; Q06245; -.
DR BioGRID; 31439; 207.
DR ComplexPortal; CPX-1890; Exocyst.
DR DIP; DIP-1724N; -.
DR IntAct; Q06245; 16.
DR MINT; Q06245; -.
DR STRING; 4932.YLR166C; -.
DR TCDB; 1.F.2.1.1; the octameric exocyst (exocyst) family.
DR iPTMnet; Q06245; -.
DR MaxQB; Q06245; -.
DR PaxDb; Q06245; -.
DR PRIDE; Q06245; -.
DR EnsemblFungi; YLR166C_mRNA; YLR166C; YLR166C.
DR GeneID; 850863; -.
DR KEGG; sce:YLR166C; -.
DR SGD; S000004156; SEC10.
DR VEuPathDB; FungiDB:YLR166C; -.
DR eggNOG; KOG3745; Eukaryota.
DR GeneTree; ENSGT00390000012837; -.
DR HOGENOM; CLU_008002_1_0_1; -.
DR InParanoid; Q06245; -.
DR OMA; PLCKHHY; -.
DR BioCyc; YEAST:G3O-32296-MON; -.
DR Reactome; R-SCE-264876; Insulin processing.
DR PRO; PR:Q06245; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06245; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0000145; C:exocyst; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA: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; IPR033960; EXOC5/Sec10.
DR InterPro; IPR009976; Sec10-like.
DR PANTHER; PTHR12100; PTHR12100; 1.
DR PANTHER; PTHR12100:SF0; PTHR12100:SF0; 1.
DR Pfam; PF07393; Sec10; 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..871
FT /note="Exocyst complex component SEC10"
FT /id="PRO_0000118950"
FT COILED 74..101
FT /evidence="ECO:0000255"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 871 AA; 100342 MW; A32073099815388D CRC64;
MNSLYELDPK WKKLLKTDNF LGGLTVNEFV QELSKDHRND VLIDANTKNL PTNEKDQDAI
REAIWKQLDP KPYIRTFEST LKELKNLNEE TLNKRQYFSE QVATQEVIHS ENVIKLSKDL
HTTLLTFDKL DDRLTNVTQV VSPLGDKLET AIKKKQNYIQ SVELIRRYND FYSMGKSDIV
EQLRLSKNWK LNLKSVKLMK NLLILSSKLE TSSIPKTINT KLVIEKYSEM MENELLENFN
SAYRENNFTK LNEIAIILNN FNGGVNVIQS FINQHDYFID TKQIDLENEF ENVFIKNVKF
KEQLIDFENH SVIIETSMQN LINDVETVIK NESKIVKRVF EEKATHVIQL FIQRVFAQKI
EPRFEVLLRN SLSISNLAYV RILHGLFTLF GKFTKSLIDY FQLLEIDDSN QILSTTLEQC
FADLFSHYLY DRSKYFGIEK RSLEAILVDM TSKFTVNYDK EINKRVLLDK YKEKLSTNVD
AFMHSPRGNT HSRQDSTSRS KLSQFNSFLK THLDKDHLSL NRTNTLSDSF NNSSSSTQYD
VANNSSSLVN SSFTASDIDN SPNSPANYSL NDVDSMLKCV VESTARVMEL IPNKAHLYIL
EILKIMFLGI VDSYMEIALE VAYWKICKVD INKTAGVVNL NFLKFISMST EILDLLSISI
KSIFLPLLNN SPEIKAQIIE MTNSQIQKME ILINIILQET ITVISTKFSA ILCKQKKKDF
VPKSQELLDQ DTLPAIEIVN ILNLIFEQSS KFLKGKNLQT FLTLIGEELY GLLLSHYSHF
QVNSIGGVVV TKDIIGYQTA IEDWGVASLI DKFATLRELA NLFTVQPELL ESLTKEGHLA
DIGRDIIQSY ISNREDFNHD NFINSVKLNF R
