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Protein

Exocyst complex component SEC3

Gene

SEC3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.

GO - Molecular functioni

  • GTP-Rho binding Source: SGD
  • phosphatidylinositol-4,5-bisphosphate binding Source: SGD

GO - Biological processi

  • endoplasmic reticulum inheritance Source: SGD
  • exocyst assembly Source: SGD
  • exocyst localization Source: SGD
  • exocytosis Source: SGD
  • Golgi to plasma membrane transport Source: SGD
  • protein transport Source: UniProtKB-KW
  • vesicle tethering involved in exocytosis Source: SGD
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30195-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Exocyst complex component SEC3
Alternative name(s):
Protein PSL1
Gene namesi
Name:SEC3
Synonyms:PSL1
Ordered Locus Names:YER008C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome V

Organism-specific databases

CYGDiYER008c.
EuPathDBiFungiDB:YER008C.
SGDiS000000810. SEC3.

Subcellular locationi

GO - Cellular componenti

  • cellular bud neck Source: SGD
  • cellular bud tip Source: SGD
  • exocyst Source: SGD
  • incipient cellular bud site Source: SGD
  • mating projection tip Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13361336Exocyst complex component SEC3PRO_0000118917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei290 – 2901Phosphothreonine1 Publication
Modified residuei606 – 6061Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP33332.
PaxDbiP33332.
PRIDEiP33332.

Interactioni

Subunit structurei

The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8, SEC10, SEC15, EXO70 and EXO84.

Protein-protein interaction databases

BioGridi36739. 115 interactions.
DIPiDIP-5992N.
IntActiP33332. 17 interactions.
MINTiMINT-629249.

Structurei

Secondary structure

1
1336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi76 – 9318Combined sources
Beta strandi94 – 963Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi107 – 12317Combined sources
Helixi131 – 1333Combined sources
Beta strandi134 – 14310Combined sources
Beta strandi151 – 1588Combined sources
Helixi160 – 1623Combined sources
Beta strandi164 – 1718Combined sources
Helixi172 – 1743Combined sources
Beta strandi177 – 1804Combined sources
Beta strandi187 – 19913Combined sources
Helixi203 – 21917Combined sources
Turni221 – 2233Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi235 – 2384Combined sources
Helixi240 – 2467Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A58X-ray2.60A/C/E1-320[»]
3HIEX-ray2.00A/B/C/D71-241[»]
ProteinModelPortaliP33332.
SMRiP33332. Positions 76-260.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33332.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili319 – 464146Sequence AnalysisAdd
BLAST
Coiled coili1309 – 133628Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the SEC3 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG81454.
HOGENOMiHOG000142343.
InParanoidiP33332.
OMAiNNYITHV.
OrthoDBiEOG7SFJ59.

Family and domain databases

InterProiIPR019160. Exocyst_Exoc1/SEC3.
IPR028258. Sec3-PIP2_bind.
[Graphical view]
PfamiPF15277. Sec3-PIP2_bind. 1 hit.
PF09763. Sec3_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P33332-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSSKSPFKR KSHSRETSHD ENTSFFHKRT ISGSSAHHSR NVSQGAVPSS
60 70 80 90 100
APPVSGGNYS HKRNVSRASN SSQTSNFLAE QYERDRKAII NCCFSRPDHK
110 120 130 140 150
TGEPPNNYIT HVRIIEDSKF PSSRPPPDSK LENKKKRLLI LSAKPNNAKL
160 170 180 190 200
IQIHKARENS DGSFQIGRTW QLTELVRVEK DLEISEGFIL TMSKKYYWET
210 220 230 240 250
NSAKERTVFI KSLITLYIQT FEGHVPELVN WDLSLFYLDE RSYQRAVITN
260 270 280 290 300
RPGSVSPIKS PTSNFTTNTT QSVGSVPFSA PTERTRRSET ESVNPVSTPA
310 320 330 340 350
SVEYHAGMKS LNKAPYSSNS TLNEVNKRYE LEQQQQQEEA ELRRLEEQKR
360 370 380 390 400
LQLQKENEMK RLEEERRIKQ EERKRQMELE HQRQLEEEER KRQMELEAKK
410 420 430 440 450
QMELKRQRQF EEEQRLKKER ELLEIQRKQR EQETAERLKK EEQEALAKKE
460 470 480 490 500
EEEKSKRNKV DNESYTQEIN GKVDNLLEDL NAVLAEETET TPTMQNGTYV
510 520 530 540 550
PERSTARAHD QLKKPLNIAK VESLGGSDLN DSISLSDEIA GLNTSNLSGE
560 570 580 590 600
DQDEKNDLSF EKGDEVRYSN NFEGEAPHVY HEVSIIQEEA PAVSQKLILP
610 620 630 640 650
EENNESEALI ESKEEIKTME NIDDEVLLEI LTDINWSIED DADSMIERID
660 670 680 690 700
LRLAETEYLF NQNLLSLQKI GPNIRPYEDK VNDECHRIIP TLSLFLMEMS
710 720 730 740 750
NFSNDIENVE SQDNGLQVES ANKKLLWNTL DELLKTVSLD EISLNQLLEC
760 770 780 790 800
PIREKNLPWM ENQLNLLLKA FQAIGSDGNE VEYNLREISG LKQRLQFYEK
810 820 830 840 850
VTKIFLNRIV EEMQKKFSNI RGQDISHDQM IRILTTLLIF SPLILFCKEI
860 870 880 890 900
SQKSYQAIVE NWNVSIQPVY MELWTKKISQ LQGIDTNDEK MNELSLSQLL
910 920 930 940 950
NEWDTFRKER KTNDINPVFK NSFSLLTECL QTMRQECIVY QNFVEVFFHI
960 970 980 990 1000
SSKHNFEEYI KHFNDPDAPP ILLDTVKVMQ SDREAAVIET QLVSRIFQPI
1010 1020 1030 1040 1050
VTRLSSYFVE LVKAEPTVAP ALTFYLENEI KSLESSNHEF LLSAVTRMYT
1060 1070 1080 1090 1100
QIKQVWSDNV EEQVLHFERI SNATTNGEIL PGILDLPVGL KNSEDLFQFA
1110 1120 1130 1140 1150
KRSMDIKDTD EGYESIELMN SSFRKLSIAA TRSITHKEVN SSINPNLSDT
1160 1170 1180 1190 1200
AALNNDYMET ISLLVNSNWL TEMLSMLNFN KDGIFDTSLQ NVKKVFDVEK
1210 1220 1230 1240 1250
ESYASFLLRD TMPKLTAFVY GVSNIIENTN NVNMTNPSRW AAYSRQNLEN
1260 1270 1280 1290 1300
ILLAYTSHEI ETLVKRLHTH MVNDFGYHQE NAINNVLCDK LWSCIQGQTV
1310 1320 1330
SLYLKLYTVI DKHYRGTNIR FTKNDIISAF EEYKNA
Length:1,336
Mass (Da):154,695
Last modified:February 1, 1994 - v1
Checksum:i6F0C1BF13A77985E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22204 Genomic DNA. Translation: AAB49380.1.
U18778 Genomic DNA. Translation: AAB64541.1.
BK006939 Genomic DNA. Translation: DAA07659.1.
PIRiS41794.
RefSeqiNP_010924.1. NM_001178899.1.

Genome annotation databases

EnsemblFungiiYER008C; YER008C; YER008C.
GeneIDi856726.
KEGGisce:YER008C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22204 Genomic DNA. Translation: AAB49380.1.
U18778 Genomic DNA. Translation: AAB64541.1.
BK006939 Genomic DNA. Translation: DAA07659.1.
PIRiS41794.
RefSeqiNP_010924.1. NM_001178899.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A58X-ray2.60A/C/E1-320[»]
3HIEX-ray2.00A/B/C/D71-241[»]
ProteinModelPortaliP33332.
SMRiP33332. Positions 76-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36739. 115 interactions.
DIPiDIP-5992N.
IntActiP33332. 17 interactions.
MINTiMINT-629249.

Proteomic databases

MaxQBiP33332.
PaxDbiP33332.
PRIDEiP33332.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER008C; YER008C; YER008C.
GeneIDi856726.
KEGGisce:YER008C.

Organism-specific databases

CYGDiYER008c.
EuPathDBiFungiDB:YER008C.
SGDiS000000810. SEC3.

Phylogenomic databases

eggNOGiNOG81454.
HOGENOMiHOG000142343.
InParanoidiP33332.
OMAiNNYITHV.
OrthoDBiEOG7SFJ59.

Enzyme and pathway databases

BioCyciYEAST:G3O-30195-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP33332.
NextBioi982829.
PROiP33332.

Family and domain databases

InterProiIPR019160. Exocyst_Exoc1/SEC3.
IPR028258. Sec3-PIP2_bind.
[Graphical view]
PfamiPF15277. Sec3-PIP2_bind. 1 hit.
PF09763. Sec3_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SEC3 mutations are synthetically lethal with profilin mutations and cause defects in diploid-specific bud-site selection."
    Haarer B.K., Corbett A., Kweon Y., Petzold A.S., Silver P., Brown S.S.
    Genetics 144:495-510(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Sec3p is involved in secretion and morphogenesis in Saccharomyces cerevisiae."
    Finger F.P., Novick P.
    Mol. Biol. Cell 8:647-662(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae."
    TerBush D.R., Maurice T., Roth D., Novick P.
    EMBO J. 15:6483-6494(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 793-800.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSEC3_YEAST
AccessioniPrimary (citable) accession number: P33332
Secondary accession number(s): D3DLQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 22, 2015
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 377 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.