SEC9_YEAST
ID SEC9_YEAST Reviewed; 651 AA.
AC P40357; D6VUE6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Protein transport protein SEC9;
GN Name=SEC9; Synonyms=HSS7; OrderedLocusNames=YGR009C;
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=7954793; DOI=10.1016/0092-8674(94)90194-5;
RA Brennwald P., Kearns B., Champion K., Keraenen S., Bankaitis V., Novick P.;
RT "Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the
RT effector of Sec4 function in exocytosis.";
RL Cell 79:245-258(1994).
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, AND INTERACTION WITH SRO7 AND SRO77.
RX PubMed=10402465; DOI=10.1083/jcb.146.1.125;
RA Lehman K., Rossi G., Adamo J.E., Brennwald P.;
RT "Yeast homologues of tomosyn and lethal giant larvae function in exocytosis
RT and are associated with the plasma membrane SNARE, Sec9.";
RL J. Cell Biol. 146:125-140(1999).
RN [5]
RP INTERACTION WITH SRO7.
RX PubMed=15964280; DOI=10.1016/j.cub.2005.05.046;
RA Gangar A., Rossi G., Andreeva A., Hales R., Brennwald P.;
RT "Structurally conserved interaction of Lgl family with SNAREs is critical
RT to their cellular function.";
RL Curr. Biol. 15:1136-1142(2005).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-190 AND SER-315, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-92; SER-190; SER-213;
RP SER-271; SER-273; SER-315; THR-355 AND SER-359, AND IDENTIFICATION BY MASS
RP 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 a SNARE complex that may be the effector of SEC4
CC function in exocytosis. {ECO:0000269|PubMed:10402465}.
CC -!- SUBUNIT: Interacts with SRO7 and SRO77. {ECO:0000269|PubMed:10402465,
CC ECO:0000269|PubMed:15964280}.
CC -!- INTERACTION:
CC P40357; Q12038: SRO7; NbExp=10; IntAct=EBI-16904, EBI-17573;
CC P40357; P32867: SSO1; NbExp=14; IntAct=EBI-16904, EBI-2206525;
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; L34336; AAA35034.1; -; Genomic_DNA.
DR EMBL; Z72794; CAA96992.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08107.1; -; Genomic_DNA.
DR PIR; A55100; A55100.
DR RefSeq; NP_011523.3; NM_001181138.3.
DR PDB; 3B5N; X-ray; 1.60 A; C/G/K=433-499, D/H/L=589-650.
DR PDBsum; 3B5N; -.
DR AlphaFoldDB; P40357; -.
DR SMR; P40357; -.
DR BioGRID; 33253; 200.
DR ComplexPortal; CPX-1365; Vesicular SNARE complex SSO1-SEC9-SNC1.
DR ComplexPortal; CPX-1369; Vesicular SNARE complex SSO2-SEC9-SNC1.
DR ComplexPortal; CPX-5463; Vesicular SNARE complex SSO1-SEC9-SNC2.
DR ComplexPortal; CPX-5465; Vesicular SNARE complex SSO2-SEC9-SNC2.
DR ComplexPortal; CPX-5521; Vacuolar SNARE complex SSO1-SEC9-NYV1.
DR DIP; DIP-1460N; -.
DR IntAct; P40357; 14.
DR MINT; P40357; -.
DR STRING; 4932.YGR009C; -.
DR iPTMnet; P40357; -.
DR MaxQB; P40357; -.
DR PaxDb; P40357; -.
DR PRIDE; P40357; -.
DR EnsemblFungi; YGR009C_mRNA; YGR009C; YGR009C.
DR GeneID; 852892; -.
DR KEGG; sce:YGR009C; -.
DR SGD; S000003241; SEC9.
DR VEuPathDB; FungiDB:YGR009C; -.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR HOGENOM; CLU_020823_1_0_1; -.
DR InParanoid; P40357; -.
DR OMA; LDINVHM; -.
DR BioCyc; YEAST:G3O-30739-MON; -.
DR Reactome; R-SCE-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013026; RHOB GTPase cycle.
DR EvolutionaryTrace; P40357; -.
DR PRO; PR:P40357; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P40357; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IC:ComplexPortal.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IDA:SGD.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IPI:CAFA.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IGI:SGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IC:ComplexPortal.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IC:ComplexPortal.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0035493; P:SNARE complex assembly; IMP:CAFA.
DR GO; GO:0006906; P:vesicle fusion; IDA:SGD.
DR GO; GO:0099500; P:vesicle fusion to plasma membrane; IC:ComplexPortal.
DR DisProt; DP00128; -.
DR InterPro; IPR000727; T_SNARE_dom.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..651
FT /note="Protein transport protein SEC9"
FT /id="PRO_0000213613"
FT DOMAIN 434..496
FT /note="t-SNARE coiled-coil homology 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 588..650
FT /note="t-SNARE coiled-coil homology 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 355
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 433..499
FT /evidence="ECO:0007829|PDB:3B5N"
FT HELIX 589..648
FT /evidence="ECO:0007829|PDB:3B5N"
SQ SEQUENCE 651 AA; 73624 MW; EA314D73D20A10C7 CRC64;
MGLKKFFKIK PPEEATPEQN KDTLMELGIS VKNPSKKRKE KFAAYGKFAN DKAEDKVYAP
PGYEQYARPQ DELEDLNASP LDANANEATA GSNRGSSGTQ DLGNGAESNS MQDPYAIEND
DYRYDDDPYA RFQANKSNGR GSVNAAPYGD YGGGYNGTSL NSYNNDGPYS NQNTSNSWVN
ANGRNSLNHS NSTLNVGPSR QTRQPPVSTS TNSLSLDQRS PLANPMQEKR NPYADMNSYG
GAYDSNTNRS SGTRQGSSKN ANPYASMAND SYSNGNLNRS ANPYSSRSVR QPQSQQAPMT
YTPSFIASDE AARNSEVDLN EEPRTGEFDF EEVYADKSAE NRAALDEPDL NAVMTNEDSI
DLNASEVDHS SRQQQQQQWF MDEQQQQQQH FNATNNQYGD QRGYKTFEEI QKEEEARQQQ
EEDEAVDEIK QEIKFTKQSS VASTRNTLKM AQDAERAGMN TLGMLGHQSE QLNNVEGNLD
LMKVQNKVAD EKVAELKKLN RSILAVHVSN PFNSKRRRRE REEQLKNRKI EEKLMREQTS
QQLSQSTQRI EGAMNANNNI SEVRERYQRK NVLEKAKRYQ FENDEEDDEM ELEIDRNLDQ
IQQVSNRLKK MALTTGKELD SQQKRLNNIE ESTDDLDINL HMNTNRLAGI R
