ID   EXOC1_CAEEL             Reviewed;         848 AA.
AC   Q20678;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Exocyst complex component 1;
DE   AltName: Full=Exocyst complex component Sec3;
GN   Name=sec-3; ORFNames=F52E4.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC       exocytic vesicles with fusion sites on the plasma membrane.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: The exocyst complex is composed of sec-3/exoc1, sec-5/exoc2,
CC       sec-6/exoc3, sec-8/exoc4, sec-10/exoc5, sec-15/exoc6, exo-70/exoc7 and
CC       exo-84/exoc8. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q20678; A0A0S4XR43: ccar-1; NbExp=3; IntAct=EBI-322886, EBI-313448;
CC   -!- SIMILARITY: Belongs to the SEC3 family. {ECO:0000305}.
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DR   EMBL; FO080758; CCD66482.1; -; Genomic_DNA.
DR   PIR; T16430; T16430.
DR   RefSeq; NP_508530.1; NM_076129.3.
DR   AlphaFoldDB; Q20678; -.
DR   SMR; Q20678; -.
DR   BioGRID; 45541; 7.
DR   ComplexPortal; CPX-712; Exocyst.
DR   DIP; DIP-24392N; -.
DR   IntAct; Q20678; 3.
DR   STRING; 6239.F52E4.7; -.
DR   EPD; Q20678; -.
DR   PaxDb; Q20678; -.
DR   PeptideAtlas; Q20678; -.
DR   EnsemblMetazoa; F52E4.7.1; F52E4.7.1; WBGene00018703.
DR   GeneID; 180598; -.
DR   KEGG; cel:CELE_F52E4.7; -.
DR   UCSC; F52E4.7; c. elegans.
DR   CTD; 180598; -.
DR   WormBase; F52E4.7; CE10836; WBGene00018703; sec-3.
DR   eggNOG; KOG2148; Eukaryota.
DR   GeneTree; ENSGT00940000173251; -.
DR   HOGENOM; CLU_015381_1_0_1; -.
DR   InParanoid; Q20678; -.
DR   OMA; KEAKKCY; -.
DR   OrthoDB; 201698at2759; -.
DR   PhylomeDB; Q20678; -.
DR   Reactome; R-CEL-264876; Insulin processing.
DR   Reactome; R-CEL-5620916; VxPx cargo-targeting to cilium.
DR   PRO; PR:Q20678; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00018703; Expressed in embryo and 4 other tissues.
DR   GO; GO:0000145; C:exocyst; ISS:WormBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0090522; P:vesicle tethering involved in exocytosis; IMP:ComplexPortal.
DR   InterPro; IPR028258; Sec3-PIP2_bind.
DR   InterPro; IPR019160; Sec3_C.
DR   Pfam; PF15277; Sec3-PIP2_bind; 1.
DR   Pfam; PF09763; Sec3_C; 1.
DR   SMART; SM01313; Sec3-PIP2_bind; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Exocytosis; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..848
FT                   /note="Exocyst complex component 1"
FT                   /id="PRO_0000118915"
FT   COILED          230..257
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   848 AA;  97297 MW;  83DEA2584B9DC180 CRC64;
     MSAIRKIIQR QLFQKDDERI QAIVNVSKLD GKKKKNQTLL CLAVTIEHPI AVRLYFVKGE
     KDDTFKKKDR FNLREVREID GINPKKASPE FHITIGDHQY VILAGSAEEK DEFIRELYKL
     SCQYLPVQMP DFCNFSLPQL ESETSIIPIE LPEHDMAMQS DYQPISNKED ADFRKLIARA
     NLTIGEAHIF AEMLTEQLQS LDGANINSMM DSENSVNQLL SSIDAALTGV ESVEKELDRC
     DDILAFVRNS IELIEEKDSL SVVERKNKQR LNEEIVSFVN SLQAVTDSHI ETLKQANFSN
     PESVQRCTDA ARAVAQFWHG RISKPMLQMK AYQDRNDELT AVDVFVDRLM SHLSALFSNL
     NDLSLDHEWH ELCIPKQSQR FRALSPLSDL INWLKTNRPK ACNLVLQKYI DSTNLLYKRL
     FDNFFETLIN KVPKANSSEK KSKANESANI SLRSDNQSFL STSSEIDTEV LPQLIETVLA
     ELSAVIDAEQ KFVVRFFHIN SELLAQFDTT STGSGDSSSL GGRSMEKHMN EQVRHVMGNL
     FDSLNIHLDS FCRAVCRHNP SNVLLLFVIM SKKVLLPQDP SSYFSITFGS LVVLIKRQFD
     AFIQMECSQY SEVRIAKKTR IGILPSIFRF ANFVRRAEII FENAERRTDL EKAYFNLCRA
     VCDGIQKAAA NQYSKSPSSV VKFENYHELY LTLSELKISC LDQQRKDAKA LKEEHIDAYV
     KEFMGRPLKE IQTFFDNVNN FIETRGIRPD EISYQQQFSR IELKKVISQH PGKEVKKGLE
     QLYKKIEKNL VANSSLLQVV WRDMQEQFVK QIAEYNKLIL TCYPGSKIEL EVSTDTVLQF
     FSEIAQQH