SEC6_YEAST
ID SEC6_YEAST Reviewed; 805 AA.
AC P32844; D6VVL6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Exocyst complex component SEC6;
GN Name=SEC6; OrderedLocusNames=YIL068C;
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=1523887; DOI=10.1002/yea.320080706;
RA Potenza M., Bowser R., Mueller H., Novick P.;
RT "SEC6 encodes an 85 kDa soluble protein required for exocytosis in yeast.";
RL Yeast 8:549-558(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 411-805.
RX PubMed=16699513; DOI=10.1038/nsmb1096;
RA Sivaram M.V., Furgason M.L., Brewer D.N., Munson M.;
RT "The structure of the exocyst subunit Sec6p defines a conserved
RT architecture with diverse roles.";
RL Nat. Struct. Mol. Biol. 13:555-556(2006).
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 P32844; P19658: EXO70; NbExp=3; IntAct=EBI-16874, EBI-6717;
CC P32844; Q06245: SEC10; NbExp=2; IntAct=EBI-16874, EBI-16504;
CC P32844; P89102: SEC5; NbExp=3; IntAct=EBI-16874, EBI-16865;
CC P32844; P32855: SEC8; NbExp=3; IntAct=EBI-16874, EBI-16896;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SEC6 family. {ECO:0000305}.
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DR EMBL; X64738; CAA46004.1; -; Genomic_DNA.
DR EMBL; Z38060; CAA86155.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08482.1; -; Genomic_DNA.
DR PIR; S48411; S48411.
DR RefSeq; NP_012196.1; NM_001179418.1.
DR PDB; 2FJI; X-ray; 2.40 A; 1/2=411-805.
DR PDB; 5YFP; EM; 4.40 A; C=1-805.
DR PDB; 6VKL; EM; 4.40 A; C=1-805.
DR PDBsum; 2FJI; -.
DR PDBsum; 5YFP; -.
DR PDBsum; 6VKL; -.
DR AlphaFoldDB; P32844; -.
DR SMR; P32844; -.
DR BioGRID; 34924; 123.
DR ComplexPortal; CPX-1890; Exocyst.
DR DIP; DIP-5649N; -.
DR IntAct; P32844; 20.
DR MINT; P32844; -.
DR STRING; 4932.YIL068C; -.
DR TCDB; 1.F.2.1.1; the octameric exocyst (exocyst) family.
DR iPTMnet; P32844; -.
DR MaxQB; P32844; -.
DR PaxDb; P32844; -.
DR PRIDE; P32844; -.
DR EnsemblFungi; YIL068C_mRNA; YIL068C; YIL068C.
DR GeneID; 854742; -.
DR KEGG; sce:YIL068C; -.
DR SGD; S000001330; SEC6.
DR VEuPathDB; FungiDB:YIL068C; -.
DR eggNOG; KOG2286; Eukaryota.
DR GeneTree; ENSGT01030000234613; -.
DR HOGENOM; CLU_011776_2_0_1; -.
DR InParanoid; P32844; -.
DR OMA; MNIGPKT; -.
DR BioCyc; YEAST:G3O-31335-MON; -.
DR Reactome; R-SCE-264876; Insulin processing.
DR EvolutionaryTrace; P32844; -.
DR PRO; PR:P32844; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P32844; 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:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IDA:SGD.
DR GO; GO:0051601; P:exocyst localization; 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:0035544; P:negative regulation of SNARE complex assembly; IDA:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IC:ComplexPortal.
DR Gene3D; 1.10.357.70; -; 1.
DR InterPro; IPR010326; EXOC3/Sec6.
DR InterPro; IPR042532; EXOC3/Sec6_C.
DR PANTHER; PTHR21292; PTHR21292; 1.
DR Pfam; PF06046; Sec6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Exocytosis; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..805
FT /note="Exocyst complex component SEC6"
FT /id="PRO_0000118931"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CONFLICT 1..91
FT /note="MSSDPLQQVCDLIKGDLSLERVRDIKEQLLKEKSVVEYQLNKESDKYYGEVE
FT ESLKLLNLSKNSVTSIKQQINEVNKLGNDNRFAINRYDI -> MKLINWVMIIDLQLIV
FT MIY (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="K -> E (in Ref. 1; CAA46004)"
FT /evidence="ECO:0000305"
FT CONFLICT 627..628
FT /note="QQ -> HE (in Ref. 1; CAA46004)"
FT /evidence="ECO:0000305"
FT HELIX 412..447
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 463..481
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 485..522
FT /evidence="ECO:0007829|PDB:2FJI"
FT TURN 523..526
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:2FJI"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 541..567
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 572..583
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 586..606
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 609..612
FT /evidence="ECO:0007829|PDB:2FJI"
FT TURN 613..616
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 625..640
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 641..643
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 646..666
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 667..670
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 677..679
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 680..699
FT /evidence="ECO:0007829|PDB:2FJI"
FT TURN 700..702
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 706..725
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 728..730
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 731..739
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 748..754
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 762..785
FT /evidence="ECO:0007829|PDB:2FJI"
FT HELIX 794..797
FT /evidence="ECO:0007829|PDB:2FJI"
SQ SEQUENCE 805 AA; 93428 MW; 2B09BBBE15389239 CRC64;
MSSDPLQQVC DLIKGDLSLE RVRDIKEQLL KEKSVVEYQL NKESDKYYGE VEESLKLLNL
SKNSVTSIKQ QINEVNKLGN DNRFAINRYD ILFRATKLYE TVNTTSSIYD RIYNFVALME
HIERLLVAEL AEDALETGCP HLLEIHFLLT SARDFQEQVV VMAKEATEDA QRTVMKLFSR
LSGIISKFDK LLDGLTYDIV EMARAEQISL AIRLFKIYDL EEREDLRIEA IRNIIKKKEI
EIEKSSIKKL PNSKNTARLQ DETPKVIEYP TNKGLYQEIM SGTISTRTAP RGYKHFLING
INNSISEMFG EMREKYVGDQ KFDVLDNMDW IFNELIIVKE HIANCCPPHW NIFEVYFDQY
YKELHSLITD LVESEPETII ILDILAFDKT FQDTLKQDFG FTKSEVKSVI GDKEKETLFK
DYLNLIVVKM TEWIGNLEKA EFDVFLERST PPHSDSDGLL FLDGTKTCFQ MFTQQVEVAA
GTNQAKILVG VVERFSDLLT KRQKNWISKI SEEIKKQINY NHKYDIDPES ITPEDECPGG
LVEYLIAVSN DQMKAADYAV AISSKYGKLV SKVYEKQITN HLEGTLDGFA EVAQCSSLGL
ITLMFDDLRK PYQEIFSKTW YMGSQAQQIA DTLDEYLLDI KPQMNSVLFV NFIDNVIGET
IIKFLTALSF EHSFKNKNNK FLEAMKRDFE IFYQLFVKVL DGNESKDTLI TQNFTVMEFF
MDLSCEPIDS ILDIWQKYLE VYWDSRIDLL VGILKCRKDV SSSERKKIVQ QATEMLHEYR
RNMEANGVDR EPTLMRRFVL EFEKQ
