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Database: UniProt
Entry: A0A9D3TDK9_MEGAT
LinkDB: A0A9D3TDK9_MEGAT
Original site: A0A9D3TDK9_MEGAT 
ID   A0A9D3TDK9_MEGAT        Unreviewed;       900 AA.
AC   A0A9D3TDK9;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   18-JUN-2025, entry version 10.
DE   RecName: Full=Exocyst complex component 1 {ECO:0000256|ARBA:ARBA00068988};
DE   AltName: Full=Exocyst complex component Sec3 {ECO:0000256|ARBA:ARBA00079611};
GN   ORFNames=MATL_G00038950 {ECO:0000313|EMBL:KAG7488858.1};
OS   Megalops atlanticus (Tarpon) (Clupea gigantea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Elopiformes; Megalopidae; Megalops.
OX   NCBI_TaxID=7932 {ECO:0000313|EMBL:KAG7488858.1, ECO:0000313|Proteomes:UP001046870};
RN   [1] {ECO:0000313|EMBL:KAG7488858.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YG-15Mar2019-1 {ECO:0000313|EMBL:KAG7488858.1};
RC   TISSUE=Brain {ECO:0000313|EMBL:KAG7488858.1};
RA   Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA   Lampietro C., Louis A., Herpin A., Echchiki A., Berthelot C., Parey E.,
RA   Roest-Crollius H., Braasch I., Postlethwait J., Bobe J., Montfort J.,
RA   Bouchez O., Begum T., Mejri S., Adams A., Chen W.-J., Guiguen Y.;
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC       exocytic vesicles with fusion sites on the plasma membrane.
CC       {ECO:0000256|ARBA:ARBA00002660}.
CC   -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC       EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with EEF1A1. Interacts with
CC       SLC6A9; interaction increases the transporter capacity of SLC6A9
CC       probably by promoting its insertion into the cell membrane.
CC       {ECO:0000256|ARBA:ARBA00061758}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Midbody,
CC       Midbody ring {ECO:0000256|ARBA:ARBA00004476}.
CC   -!- SIMILARITY: Belongs to the SEC3 family.
CC       {ECO:0000256|ARBA:ARBA00006518}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAG7488858.1}.
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DR   EMBL; JAFDVH010000002; KAG7488858.1; -; Genomic_DNA.
DR   OrthoDB; 27109at2759; -.
DR   Proteomes; UP001046870; Chromosome 2.
DR   GO; GO:0000145; C:exocyst; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:TreeGrafter.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:TreeGrafter.
DR   CDD; cd14683; PH-EXOC1; 1.
DR   FunFam; 2.30.29.90:FF:000001; exocyst complex component 1 isoform X1; 1.
DR   Gene3D; 2.30.29.90; -; 1.
DR   InterPro; IPR028258; Sec3-PIP2_bind.
DR   InterPro; IPR048628; Sec3_C.
DR   InterPro; IPR019160; Sec3_CC.
DR   PANTHER; PTHR16092:SF14; EXOCYST COMPLEX COMPONENT 1 ISOFORM X1; 1.
DR   PANTHER; PTHR16092; SEC3/SYNTAXIN-RELATED; 1.
DR   Pfam; PF15277; Sec3-PIP2_bind; 1.
DR   Pfam; PF20654; Sec3_C-term; 1.
DR   Pfam; PF09763; Sec3_CC; 1.
DR   SMART; SM01313; Sec3-PIP2_bind; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP001046870};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          31..122
FT                   /note="Exocyst complex component Sec3 PIP2-binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01313"
FT   REGION          141..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          213..261
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        451..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..480
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..497
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   900 AA;  102832 MW;  D79689A3C72FE94A CRC64;
     MTAIKHALQR DIFTPNDERL LSIVNVCKAG KKKKNCFLCA TVTTERPVQV KVVKVKKSDK
     GDFYKRQVAW ELRDLTEVDA KDANKENPEF DLHFEKVYKW VASSTAEKNS FISCIWKLNQ
     RYLRKKVEFV NVSPQLLEEL PKAEESVPSG ENQSVAGGDE DALDDYQELN AREEQDIENM
     MEVCEYAISN AEAFAEKLSR ELQVLDGANI QSIMASEKQV NILMQLLDEA LAEVDTIEGK
     LSSYEEMLQS VKEQMDQISQ SNRLIQLSST NNLRLLDEIN FLVNYMDLSK GHIRALQEGD
     LSSPKGIEAC INASEALLQC MNVALRPGHD KLLAVKQQQH LFNELRDSFS RRLTNHLNNV
     FVHQGHDQSS SLSQHSAELM LPKHNVLHRD LLRYAKLMEW LKNTQREKYE GLTGTYVDYM
     TRLYEREIKD FFEVAKMKIA GTSKEGKKFA TLPRKESALK QETESLHGSS GKLTGSTSSL
     NKLTVQGSSS RRSQSSSLLD MGNMSASDLD VADRTKFDKI FEQVLSELEP LCLAEQDFIS
     KFFKLQQHPS QGVPQGEMSE AEGTVHSRLS SAGEHRHSMS EKDMVRLMMN NIFHCIEVEL
     NSLIALGDKM DSFHSLYMLV KMSHHVWTAE NVDPASYLST TLGNVLVTVK RNFDKCISSQ
     IRQMEEVKIS KKSKVGILPF VTGFEEFAEL AETIFRNAER RGDLDKAYVK LIRAVYMNVE
     KVASESLKTP RDVVLMENFH HIFSTLSRLK ISCLETERRE AKHKYTEHLQ AYVITSLGQP
     LEKLNHFFEG VEARVAQGVR EEEVSYQLAF SKQELRKVIK EYPGKEVKKG LDNLYKKVDK
     HLCEEENLLQ VVWHSMQDEF IRQYKHFVGL IGRCYPGSGI TMDFTIQDIL EYFSSIAQSH
//
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