EXOC6_DICDI
ID EXOC6_DICDI Reviewed; 1025 AA.
AC Q54B27;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Exocyst complex component 6;
DE AltName: Full=Exocyst complex component Sec15;
GN Name=exoc6; Synonyms=sec15; ORFNames=DDB_G0293936;
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: Cytoplasm {ECO:0000250|UniProtKB:O54923}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54923}. Midbody,
CC Midbody ring {ECO:0000250|UniProtKB:Q8TAG9}.
CC -!- SIMILARITY: Belongs to the SEC15 family. {ECO:0000305}.
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DR EMBL; AAFI02000224; EAL60467.1; -; Genomic_DNA.
DR RefSeq; XP_628889.1; XM_628887.1.
DR AlphaFoldDB; Q54B27; -.
DR SMR; Q54B27; -.
DR STRING; 44689.DDB0233959; -.
DR PaxDb; Q54B27; -.
DR PRIDE; Q54B27; -.
DR EnsemblProtists; EAL60467; EAL60467; DDB_G0293936.
DR GeneID; 8629504; -.
DR KEGG; ddi:DDB_G0293936; -.
DR dictyBase; DDB_G0293936; exoc6.
DR eggNOG; KOG2176; Eukaryota.
DR HOGENOM; CLU_295343_0_0_1; -.
DR InParanoid; Q54B27; -.
DR OMA; RDHYNEV; -.
DR PhylomeDB; Q54B27; -.
DR Reactome; R-DDI-264876; Insulin processing.
DR PRO; PR:Q54B27; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0000145; C:exocyst; IDA:dictyBase.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; IPI:dictyBase.
DR GO; GO:0070177; P:contractile vacuole discharge; IDA:dictyBase.
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:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IEA:InterPro.
DR Gene3D; 1.10.357.30; -; 1.
DR Gene3D; 1.20.58.670; -; 1.
DR InterPro; IPR007225; EXOC6/Sec15.
DR InterPro; IPR042045; EXOC6/Sec15_C_dom1.
DR InterPro; IPR042044; EXOC6PINT-1/Sec15/Tip20_C_dom2.
DR InterPro; IPR046361; Sec15_C.
DR PANTHER; PTHR12702; PTHR12702; 1.
DR Pfam; PF04091; Sec15; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Exocytosis; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..1025
FT /note="Exocyst complex component 6"
FT /id="PRO_0000329043"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..68
FT /evidence="ECO:0000255"
FT COMPBIAS 21..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1025 AA; 118207 MW; CA7A4689C17192C1 CRC64;
MSNKKQKEEI NTAGGSVILK TMVRDKDKEQ KEEKREKKEK KRLEKKEAEN VKKEKKKEKK
ELKKIGKAGR SGSITSDSST HSGAQEFDSY GNDSNGGGGG LSASIDSNGL SSSGQPMQTR
HLEKEVGEKQ GIYSLSSQDR SSSLPHSSQD DQAKPLITES EIFSSESFLI AVSDTDHLGP
AIKSVFENNK EKEVIKILNA YIAQKDLDIE KICGENHEGF INSVTAFLGL KGENLDLKQD
VINLNYELQE IGRKYVTKAE ELFAYKQIKD NIKRTKEVLN NCQYAILLGM KVDEYVQQKK
YYQAIKNMDQ LHNVYLKKLS DFQFARNMDY NIPVLKEKIK KLVKDEFNQW MVEIKEKSAV
IGKLGMIQTS KKLLKEREIN PLKIKTTFGE NEQIWDKILD IPPIINSSSI GSLALYPTLN
SPVTAPIYSP NSGKTPSSFG FNKQINEKDL KEDINQFSPF DESDIQFHPL YQCLFIHASI
GQLEEFQAYY TLNRLLQFQL VIQPKESGQV WELFLQQILG YFMVESKVID STEPFLSKTT
INDSWNSALV KVTSVLQELF THCVDTQPLI AFKKFVLIFT NTMSFYSYHV QPLYYFLDTM
KEKYCQFSIK EAVERFTIIL ERDSHCSLII ESLEEYKSLI LANKLDILER QQLRQLQNSL
NNNQFQFGDK NLNNNNNNDD DDDYFDEDEN EDDKISKRLP KSFLFSKMVP QFYTLIKKFI
SEFYEFSDQL TENENFIIRS TDTLIKKINE VLYSYLTQSQ AVPQVIQLVI NLQHLISGCS
FFKDYLNSLI LGEDYQKNQS IVNETNKVIL NSQNLLYTTK SHGEKLIIKL CEQKIEDLMS
SAANIEWFPQ NAIDDRPRDY IIDVCTFLEV TLPFISPLSQ NLKEEFITKA FKNISESLFS
LIYDDQLKKL NLQGVKSFDA DLKYIETYVK EKANEKERTT TTSRNMVGYF VELRQLTNFL
LSDNPEDFVD PKIKAKHYNL ITNIPQLLNI LNKYKEESKG FTTSKEIKDR NKKIADAIKK
IKDSL
