EXOC4_DICDI
ID EXOC4_DICDI Reviewed; 1182 AA.
AC Q54P76;
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 4;
DE AltName: Full=Exocyst complex component Sec8;
GN Name=exoc4; Synonyms=sec8; ORFNames=DDB_G0284833;
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|UniProtKB:Q62824}.
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|UniProtKB:Q62824}.
CC -!- SUBCELLULAR LOCATION: Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q96A65}. Cell projection
CC {ECO:0000250|UniProtKB:Q62824}.
CC -!- SIMILARITY: Belongs to the SEC8 family. {ECO:0000305}.
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DR EMBL; AAFI02000071; EAL65069.1; -; Genomic_DNA.
DR RefSeq; XP_638382.1; XM_633290.1.
DR AlphaFoldDB; Q54P76; -.
DR SMR; Q54P76; -.
DR STRING; 44689.DDB0233962; -.
DR PaxDb; Q54P76; -.
DR PRIDE; Q54P76; -.
DR EnsemblProtists; EAL65069; EAL65069; DDB_G0284833.
DR GeneID; 8624751; -.
DR KEGG; ddi:DDB_G0284833; -.
DR dictyBase; DDB_G0284833; exoc4.
DR eggNOG; KOG3691; Eukaryota.
DR HOGENOM; CLU_009514_0_0_1; -.
DR InParanoid; Q54P76; -.
DR OMA; SLPNWTD; -.
DR PhylomeDB; Q54P76; -.
DR Reactome; R-DDI-264876; Insulin processing.
DR PRO; PR:Q54P76; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0000145; C:exocyst; IDA:dictyBase.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IEA:InterPro.
DR InterPro; IPR039682; Sec8/EXOC4.
DR InterPro; IPR007191; Sec8_exocyst_N.
DR PANTHER; PTHR14146; PTHR14146; 1.
DR Pfam; PF04048; Sec8_exocyst; 1.
PE 3: Inferred from homology;
KW Cell projection; Exocytosis; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..1182
FT /note="Exocyst complex component 4"
FT /id="PRO_0000329041"
FT REGION 236..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1182 AA; 133912 MW; 613726E26425B7E6 CRC64;
MDDNEEKKLD ENKISKVLSS IPEQYHKTSF QARRTALDYM RSSNRKELLN QIGDWLDEVN
VETDNIVDVY FQGFNKSIHN YSRILEFMGT SHGNALLMSK EVEETNKLIN FNGTGIERLW
KRNLEYYYMI EILEKMEELK KVPDLLNKYI KGNHFVHAAN ILVNSISTLN ERDLVNVNAL
MDLRQMLVEK KESFKDMLVE KLNDHIYLKT KSSLKAFEYD DENNLQSNFK KILLSNKNSN
SNNSNNTFKS PLPPTTTSPF KPQFTGAFQT KASQEKAEKA AANLYNQERL SQSNQPEVLK
LEEISKTSNS KEDLNIDPEQ DGKLFMTLLV EALNVLEYLS PAVGLILGRI SIELKTAITN
SITLITNVYH SEGRVIPKMP GESSNSSNGS NGSNGGGNNS MNGSGGINGN GSTASSSSPT
SSTSSNIGAN GLSPSVLSKN SHIGSATFSN IDEYSAAFNF LTETFNRNDL LANQTHNIPL
VDLLKMIFNK VNMVFKNHLQ LSKIFNDAIR KSELKIRANK FDFKEETEGG GGDSDNDFEG
TPKPTKLQKS KVEIADVYDA SLVWEIIQKE IREMLRVHLQ DTSSLLLSTK SRLNPDGTES
NSGKSQRLFS FTNSIVTDNW NGSISPMVTT SPTSPNGTSG ADAIDSNSGG PAVISIFKAS
QYNVTPIYPM IVKFTDHLDK TLRDRTGTPT TTKTTTTITT TTTNSYHNQN SKKGLLRLYI
DDFVHRNFLQ HIKNDYKDRF AHSIESTEAF KPLERYKLVF RLKETKPILN STLQIFQFVI
ELFSDIVAMS HYVVEFGAII QVSLLRYYEK CLSKFSQEID PTLTNQLLNT DLYKYLLASL
AVSSKKQDVA KFQDSREEEY EFKLESDLFN HPEKPVLKNQ LILNIEKLTM LANMSHSLNW
LADKIVQLLI VQEDQKEKYT QQQQQQQQQQ QQVDSIKTPS KLNSGINSGG NSTASNKENN
STTTGSNNFI GTFNQMSAES IEALKTMEEP IKDIAQRFKD LSKRCLLALR IEYRIHCFYF
LEGFKRAQYM CEEERTDPDS FIVELNKDLS ASEEMMSIYL TSDKCNFLFS GIAKLIGKLL
ISKLVHVNSI NDNGVAKLCK NVFTLQQNLS NIIVKREIFF DRIRQFYQAL SAEDELLNYL
LEKMSQPFFS LEEGKIIIDF LQRTKRISPN AILTLEAKYK NM
