SEC8_YEAST
ID SEC8_YEAST Reviewed; 1065 AA.
AC P32855; D6W461;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Exocyst complex component SEC8;
GN Name=SEC8; OrderedLocusNames=YPR055W; ORFNames=YP9499.11;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, 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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 P32855; P38261: EXO84; NbExp=4; IntAct=EBI-16896, EBI-21567;
CC P32855; P43603: LSB3; NbExp=3; IntAct=EBI-16896, EBI-22980;
CC P32855; P39743: RVS167; NbExp=2; IntAct=EBI-16896, EBI-14500;
CC P32855; P32844: SEC6; NbExp=3; IntAct=EBI-16896, EBI-16874;
CC P32855; P32793: YSC84; NbExp=4; IntAct=EBI-16896, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC protein. Note=75% cytoplasmic. 25% associated with the cell membrane.
CC -!- SIMILARITY: Belongs to the SEC8 family. {ECO:0000305}.
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DR EMBL; X64693; CAA45926.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89173.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95000.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11477.1; -; Genomic_DNA.
DR PIR; A43421; A43421.
DR RefSeq; NP_015380.1; NM_001184152.1.
DR PDB; 5YFP; EM; 4.40 A; D=1-1065.
DR PDB; 6VKL; EM; 4.40 A; D=1-1065.
DR PDBsum; 5YFP; -.
DR PDBsum; 6VKL; -.
DR AlphaFoldDB; P32855; -.
DR SMR; P32855; -.
DR BioGRID; 36229; 226.
DR ComplexPortal; CPX-1890; Exocyst.
DR DIP; DIP-2937N; -.
DR IntAct; P32855; 13.
DR MINT; P32855; -.
DR STRING; 4932.YPR055W; -.
DR TCDB; 1.F.2.1.1; the octameric exocyst (exocyst) family.
DR iPTMnet; P32855; -.
DR MaxQB; P32855; -.
DR PaxDb; P32855; -.
DR PRIDE; P32855; -.
DR EnsemblFungi; YPR055W_mRNA; YPR055W; YPR055W.
DR GeneID; 856168; -.
DR KEGG; sce:YPR055W; -.
DR SGD; S000006259; SEC8.
DR VEuPathDB; FungiDB:YPR055W; -.
DR eggNOG; KOG3691; Eukaryota.
DR GeneTree; ENSGT00390000001439; -.
DR HOGENOM; CLU_004025_2_0_1; -.
DR InParanoid; P32855; -.
DR OMA; SLPNWTD; -.
DR BioCyc; YEAST:G3O-34207-MON; -.
DR Reactome; R-SCE-264876; Insulin processing.
DR PRO; PR:P32855; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32855; 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; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0048309; P:endoplasmic reticulum inheritance; IMP:SGD.
DR GO; GO:0006887; P:exocytosis; IMP:SGD.
DR GO; GO:0048313; P:Golgi inheritance; 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; IPR039682; Sec8/EXOC4.
DR InterPro; IPR007191; Sec8_exocyst_N.
DR PANTHER; PTHR14146; PTHR14146; 1.
DR Pfam; PF04048; Sec8_exocyst; 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..1065
FT /note="Exocyst complex component SEC8"
FT /id="PRO_0000118942"
FT REGION 1006..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 114..148
FT /evidence="ECO:0000255"
FT COMPBIAS 1025..1050
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1065 AA; 122225 MW; 96FC3139850C07F3 CRC64;
MDYLKPAQKG RRRGLSINSL SETQQSAMNS SLDHLQNDLN RINLQWNRIL SDNTNPLELA
LAFLDDTSVG LGHRYEEFNQ LKSQIGSHLQ DVVNEHSQVF NTNVASYGKA VSSIMQAQEQ
TLNLKNCLKE ANEKITTDKG SLQELNDNNL KYTKMIDVLV NIEELLQIPE KIEENIRKEN
FHQVQILLER GFILMNNKSL KTVEILKPIN QQLELQEHLL FNNLIEEIHD IMYSKSNKTN
FTRVTNNDIF KIISISHNGF TSLENYLYNI VNIDIMEHSK TINKNLEQFI HDQSLNKGNI
MLQENAATQA PLAPSRNQEN EGFNRIGFLL KTINNINKLP VAFNIITERA KEEIHNIIVK
STESIRSKHP SLLKMATSLK NDNHFGLPVQ DILSIILREC FWEIFLKLLY AIQCHRAIFE
MSNILQPTSS AKPAFKFNKI WGKLLDEIEL LLVRYINDPE LISSNNGSIK PINGATNNAP
TLPKRKNPKI FSLEYNIEDN SSVKDQAFEL KALLKDIFPG FSVSSNMDLD SIYVKDESFE
QDEPLVPPSV FNMKVILDPF LLFTQSTSTI VPSVLTQNTI SSLTFFDDYM NKSFLPKIQM
TMDYLFTVEV ESNNPYALEL SDENHNIFKT ALDFQRLFYN LLNVFNTANT FREKISYCIL
DLLNHFYNYY LGLFNSLIGT SDRHLTRKII TAWLQNGILM DQEQKILNGD ETLFHEESIE
LFKEIPHFYQ AGKGLSKSDL FNNLTLDTIL QFSASVLWIL NWLPGLKKAI NIDEVSQEPM
LDADRLRSSW TFSESMDLNY SNPSSSPNSL GNLKILLDDK ASKKFDETID GFKTLKFKLI
TILRFNIRAL CIYDIGSFFQ NTKIWNMDVG SIELDQNIAS LISELRRTES KLKQQLPEKE
KNSIFIGLDI VNNYALIKGA KSIKVLNHNG IKKMLRNVNV LQHAYRNLSS EPSKINMNVT
MNFYSLCGSS EAELFEYIKD NELPHCSVED LKTILRLQFS EEMHRQLKRQ STSSTKGSIK
PSNKRYTEAL EKLSNLEKEQ SKEGARTKIG KLKSKLNAVH TANEK
