EXOC1_DICDI
ID EXOC1_DICDI Reviewed; 879 AA.
AC Q54NV1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Exocyst complex component 1;
DE AltName: Full=Exocyst complex component Sec3;
GN Name=exoc1; Synonyms=sec3; ORFNames=DDB_G0285067;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 sec3/exoc1, sec5/exoc2,
CC sec6/exoc3, sec8/exoc4, sec10/exoc5, sec15/exoc6, exo70/exoc7 and
CC exo84/exoc8. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q9NV70}.
CC -!- SIMILARITY: Belongs to the SEC3 family. {ECO:0000305}.
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DR EMBL; AAFI02000073; EAL64997.1; -; Genomic_DNA.
DR RefSeq; XP_639966.1; XM_634874.1.
DR AlphaFoldDB; Q54NV1; -.
DR STRING; 44689.DDB0233960; -.
DR PaxDb; Q54NV1; -.
DR EnsemblProtists; EAL64997; EAL64997; DDB_G0285067.
DR GeneID; 8624877; -.
DR KEGG; ddi:DDB_G0285067; -.
DR dictyBase; DDB_G0285067; exoc1.
DR eggNOG; KOG2148; Eukaryota.
DR HOGENOM; CLU_327459_0_0_1; -.
DR InParanoid; Q54NV1; -.
DR OMA; KEAKKCY; -.
DR PhylomeDB; Q54NV1; -.
DR Reactome; R-DDI-264876; Insulin processing.
DR PRO; PR:Q54NV1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
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 InterPro; IPR019160; Sec3_C.
DR Pfam; PF09763; Sec3_C; 1.
PE 3: Inferred from homology;
KW Coiled coil; Exocytosis; Protein transport; Reference proteome; Transport.
FT CHAIN 1..879
FT /note="Exocyst complex component 1"
FT /id="PRO_0000329039"
FT REGION 29..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 165..187
FT /evidence="ECO:0000255"
FT COILED 226..248
FT /evidence="ECO:0000255"
FT COMPBIAS 38..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 100175 MW; 00C5E5E4CD531E2E CRC64;
MDHLGYSGGI SRVGIQHNRY SGQFSDRYSQ YSESEYDPSE TTHSESDSEN HHHSNIPILE
YPSFLSQSND NVSNGPSNNT LSSSATSLGN NDGDEDLENV INNYLSFEKD VDILTERLGK
TLSTLETEMI VGVLDSGVGV NEVISQLGDK DGTHLTGVTA WIEYYNKQLQ DMKKYIEHIE
GKNNKMEIVS RNQKLLYSEL NNLIGLMTLS DNTISTLTAP QFNDTKGLKM AIEAAEDLKR
ALTTKLKSGM DNMMAVKDQR KVFETYKISF ARKVAALVEN IFKTTDKEIG KHVITTTSQT
PGEEKFPDYL EYYDLLRKFK PLVNWLKEMD HEKLIPLIVS YIKAFRRIYE SDIKLFFSTI
QQSLEKESKD QNDFFSSSSS SKKSIDSLNN NTSTSTPSKN SSSSSSSSSG KDGIKKRKIN
RLFKYALSCL EIYIMTKQNF VMDFFLYQDP PRLAGQRNHH SNSSGGGSGS NKDGKDRKDK
KSSKKDKKDK KDKKDKKDKK KKDPDSSSSP SLDNDKPIDS NSPKSPNNAV NGSLSSTEES
SPPPPPPPPP KESPDAPLDL ILSAMFNGVV PELINMVEKA DQVNPFYLLT MLLETELYID
AHSRKDSHHS SYFVKILAEV QKSIKTLFNK FLEVQVDAIK STQTSLKRCG VLPHFRNFHI
FVKELQKYKS ESDTGSSTLL IESSYKKIIL ELFNWLDGLV EKLPEDKKYK FISKLENHYF
FYLKLQELNI NCLTQHKDTS QSIFKENLEI YVNFLIDLKF KPLIEYYTKM DELLLTLPPS
DIQFQQSHSK QQFKKIVEKF KTENIEKGLL KALGNVQKNI TKDSQLILVI WERLEEVFIE
KYEHFQDITS DCYNQTMPVS SDQIKGIFGT VYKKNPNKH
