Exocyst complex component SEC3

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• phosphatidylinositol-4,5-bisphosphate binding Source: SGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Membrane association and functional regulation of Sec3 by phospholipids and Cdc42."
    Zhang X., Orlando K., He B., Xi F., Zhang J., Zajac A., Guo W.
    J Cell Biol 180:145-158(2008) [PubMed] [Europe PMC] [Abstract]
• small GTPase binding Source: SGDInferred from direct assayⁱ
  • "Spatial regulation of the exocyst complex by Rho1 GTPase."
    Guo W., Tamanoi F., Novick P.
    Nat. Cell Biol. 3:353-360(2001) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• endoplasmic reticulum inheritance Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Sec3p is needed for the spatial regulation of secretion and for the inheritance of the cortical endoplasmic reticulum."
    Wiederkehr A., Du Y., Pypaert M., Ferro-Novick S., Novick P.
    Mol Biol Cell 14:4770-4782(2003) [PubMed] [Europe PMC] [Abstract]
  • "Functional specialization within a vesicle tethering complex: bypass of a subset of exocyst deletion mutants by Sec1p or Sec4p."
    Wiederkehr A., De Craene J.-O., Ferro-Novick S., Novick P.
    J. Cell Biol. 167:875-887(2004) [PubMed] [Europe PMC] [Abstract]
• exocyst assembly Source: SGDInferred from mutant phenotypeⁱ
  • "Functional specialization within a vesicle tethering complex: bypass of a subset of exocyst deletion mutants by Sec1p or Sec4p."
    Wiederkehr A., De Craene J.-O., Ferro-Novick S., Novick P.
    J. Cell Biol. 167:875-887(2004) [PubMed] [Europe PMC] [Abstract]
• exocyst localization Source: SGD <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Exo70 interacts with phospholipids and mediates the targeting of the exocyst to the plasma membrane."
    He B., Xi F., Zhang X., Zhang J., Guo W.
    EMBO J 26:4053-4065(2007) [PubMed] [Europe PMC] [Abstract]
  • "An internal domain of Exo70p is required for actin-independent localization and mediates assembly of specific exocyst components."
    Hutagalung A.H., Coleman J., Pypaert M., Novick P.J.
    Mol Biol Cell 20:153-163(2009) [PubMed] [Europe PMC] [Abstract]
• exocytosis Source: SGDInferred from direct assayⁱ
  • "Cell cycle-regulated trafficking of Chs2 controls actomyosin ring stability during cytokinesis."
    VerPlank L., Li R.
    Mol Biol Cell 16:2529-2543(2005) [PubMed] [Europe PMC] [Abstract]
• Golgi to plasma membrane transport Source: SGDInferred from mutant phenotypeⁱ
  • "Order of events in the yeast secretory pathway."
    Novick P., Ferro S., Schekman R.W.
    Cell 25:461-469(1981) [PubMed] [Europe PMC] [Abstract]
• protein transport Source: UniProtKB-KW
• vesicle tethering involved in exocytosis Source: SGD <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence<br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ic">GO evidence code guide</a></p> Inferred by curatorⁱ
  • Ref.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.

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• small GTPase binding Source: SGDInferred from direct assayⁱ
  • "Spatial regulation of the exocyst complex by Rho1 GTPase."
    Guo W., Tamanoi F., Novick P.
    Nat. Cell Biol. 3:353-360(2001) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Coiled coil

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        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                

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

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