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P33332

- SEC3_YEAST

UniProt

P33332 - SEC3_YEAST

Protein

Exocyst complex component SEC3

Gene

SEC3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. GTP-Rho binding Source: SGD
    2. phosphatidylinositol-4,5-bisphosphate binding Source: SGD

    GO - Biological processi

    1. endoplasmic reticulum inheritance Source: SGD
    2. exocyst assembly Source: SGD
    3. exocyst localization Source: SGD
    4. exocytosis Source: SGD
    5. Golgi to plasma membrane transport Source: SGD
    6. protein transport Source: UniProtKB-KW
    7. vesicle tethering involved in exocytosis Source: SGD

    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: Chromosome V

    Organism-specific databases

    CYGDiYER008c.
    SGDiS000000810. SEC3.

    Subcellular locationi

    GO - Cellular componenti

    1. cellular bud neck Source: SGD
    2. cellular bud tip Source: SGD
    3. exocyst Source: SGD
    4. incipient cellular bud site Source: SGD
    5. mating projection tip Source: SGD

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriP33332.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi36739. 114 interactions.
    DIPiDIP-5992N.
    IntActiP33332. 16 interactions.
    MINTiMINT-629249.
    STRINGi4932.YER008C.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiFKILAPE.
    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

    MRSSKSPFKR KSHSRETSHD ENTSFFHKRT ISGSSAHHSR NVSQGAVPSS     50
    APPVSGGNYS HKRNVSRASN SSQTSNFLAE QYERDRKAII NCCFSRPDHK 100
    TGEPPNNYIT HVRIIEDSKF PSSRPPPDSK LENKKKRLLI LSAKPNNAKL 150
    IQIHKARENS DGSFQIGRTW QLTELVRVEK DLEISEGFIL TMSKKYYWET 200
    NSAKERTVFI KSLITLYIQT FEGHVPELVN WDLSLFYLDE RSYQRAVITN 250
    RPGSVSPIKS PTSNFTTNTT QSVGSVPFSA PTERTRRSET ESVNPVSTPA 300
    SVEYHAGMKS LNKAPYSSNS TLNEVNKRYE LEQQQQQEEA ELRRLEEQKR 350
    LQLQKENEMK RLEEERRIKQ EERKRQMELE HQRQLEEEER KRQMELEAKK 400
    QMELKRQRQF EEEQRLKKER ELLEIQRKQR EQETAERLKK EEQEALAKKE 450
    EEEKSKRNKV DNESYTQEIN GKVDNLLEDL NAVLAEETET TPTMQNGTYV 500
    PERSTARAHD QLKKPLNIAK VESLGGSDLN DSISLSDEIA GLNTSNLSGE 550
    DQDEKNDLSF EKGDEVRYSN NFEGEAPHVY HEVSIIQEEA PAVSQKLILP 600
    EENNESEALI ESKEEIKTME NIDDEVLLEI LTDINWSIED DADSMIERID 650
    LRLAETEYLF NQNLLSLQKI GPNIRPYEDK VNDECHRIIP TLSLFLMEMS 700
    NFSNDIENVE SQDNGLQVES ANKKLLWNTL DELLKTVSLD EISLNQLLEC 750
    PIREKNLPWM ENQLNLLLKA FQAIGSDGNE VEYNLREISG LKQRLQFYEK 800
    VTKIFLNRIV EEMQKKFSNI RGQDISHDQM IRILTTLLIF SPLILFCKEI 850
    SQKSYQAIVE NWNVSIQPVY MELWTKKISQ LQGIDTNDEK MNELSLSQLL 900
    NEWDTFRKER KTNDINPVFK NSFSLLTECL QTMRQECIVY QNFVEVFFHI 950
    SSKHNFEEYI KHFNDPDAPP ILLDTVKVMQ SDREAAVIET QLVSRIFQPI 1000
    VTRLSSYFVE LVKAEPTVAP ALTFYLENEI KSLESSNHEF LLSAVTRMYT 1050
    QIKQVWSDNV EEQVLHFERI SNATTNGEIL PGILDLPVGL KNSEDLFQFA 1100
    KRSMDIKDTD EGYESIELMN SSFRKLSIAA TRSITHKEVN SSINPNLSDT 1150
    AALNNDYMET ISLLVNSNWL TEMLSMLNFN KDGIFDTSLQ NVKKVFDVEK 1200
    ESYASFLLRD TMPKLTAFVY GVSNIIENTN NVNMTNPSRW AAYSRQNLEN 1250
    ILLAYTSHEI ETLVKRLHTH MVNDFGYHQE NAINNVLCDK LWSCIQGQTV 1300
    SLYLKLYTVI DKHYRGTNIR FTKNDIISAF EEYKNA 1336
    Length:1,336
    Mass (Da):154,695
    Last modified:February 1, 1994 - v1
    Checksum:i6F0C1BF13A77985E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22204 Genomic DNA. Translation: AAB49380.1 .
    U18778 Genomic DNA. Translation: AAB64541.1 .
    BK006939 Genomic DNA. Translation: DAA07659.1 .
    PIRi S41794.
    RefSeqi NP_010924.1. NM_001178899.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3A58 X-ray 2.60 A/C/E 1-320 [» ]
    3HIE X-ray 2.00 A/B/C/D 71-241 [» ]
    ProteinModelPortali P33332.
    SMRi P33332. Positions 76-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36739. 114 interactions.
    DIPi DIP-5992N.
    IntActi P33332. 16 interactions.
    MINTi MINT-629249.
    STRINGi 4932.YER008C.

    Proteomic databases

    MaxQBi P33332.
    PaxDbi P33332.
    PRIDEi P33332.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER008C ; YER008C ; YER008C .
    GeneIDi 856726.
    KEGGi sce:YER008C.

    Organism-specific databases

    CYGDi YER008c.
    SGDi S000000810. SEC3.

    Phylogenomic databases

    eggNOGi NOG81454.
    HOGENOMi HOG000142343.
    OMAi FKILAPE.
    OrthoDBi EOG7SFJ59.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30195-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P33332.
    NextBioi 982829.

    Gene expression databases

    Genevestigatori P33332.

    Family and domain databases

    InterProi IPR019160. Exocyst_Exoc1/SEC3.
    IPR028258. Sec3-PIP2_bind.
    [Graphical view ]
    Pfami PF15277. Sec3-PIP2_bind. 1 hit.
    PF09763. Sec3_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 121 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