EXOC8_HUMAN
ID EXOC8_HUMAN Reviewed; 725 AA.
AC Q8IYI6; B3KU33; Q5TE82;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Exocyst complex component 8;
DE AltName: Full=Exocyst complex 84 kDa subunit;
GN Name=EXOC8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH EXOC2; RALA AND RALB.
RX PubMed=14525976; DOI=10.1074/jbc.m308702200;
RA Moskalenko S., Tong C., Rosse C., Mirey G., Formstecher E., Daviet L.,
RA Camonis J., White M.A.;
RT "Ral GTPases regulate exocyst assembly through dual subunit interactions.";
RL J. Biol. Chem. 278:51743-51748(2003).
RN [6]
RP INTERACTION WITH RALA AND RALB.
RX PubMed=18756269; DOI=10.1038/emboj.2008.166;
RA Cascone I., Selimoglu R., Ozdemir C., Del Nery E., Yeaman C., White M.,
RA Camonis J.;
RT "Distinct roles of RalA and RalB in the progression of cytokinesis are
RT supported by distinct RalGEFs.";
RL EMBO J. 27:2375-2387(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP INTERACTION WITH SH3BP1.
RX PubMed=21658605; DOI=10.1016/j.molcel.2011.03.032;
RA Parrini M.C., Sadou-Dubourgnoux A., Aoki K., Kunida K., Biondini M.,
RA Hatzoglou A., Poullet P., Formstecher E., Yeaman C., Matsuda M., Rosse C.,
RA Camonis J.;
RT "SH3BP1, an exocyst-associated RhoGAP, inactivates Rac1 at the front to
RT drive cell motility.";
RL Mol. Cell 42:650-661(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP VARIANT GLY-265.
RX PubMed=22700954; DOI=10.1126/scitranslmed.3003544;
RA Dixon-Salazar T.J., Silhavy J.L., Udpa N., Schroth J., Bielas S.,
RA Schaffer A.E., Olvera J., Bafna V., Zaki M.S., Abdel-Salam G.H.,
RA Mansour L.A., Selim L., Abdel-Hadi S., Marzouki N., Ben-Omran T.,
RA Al-Saana N.A., Sonmez F.M., Celep F., Azam M., Hill K.J., Collazo A.,
RA Fenstermaker A.G., Novarino G., Akizu N., Garimella K.V., Sougnez C.,
RA Russ C., Gabriel S.B., Gleeson J.G.;
RT "Exome sequencing can improve diagnosis and alter patient management.";
RL Sci. Transl. Med. 4:138RA78-138RA78(2012).
RN [12]
RP INVOLVEMENT IN NEDMISB.
RX PubMed=32103185; DOI=10.1038/s41436-020-0758-9;
RA Coulter M.E., Musaev D., DeGennaro E.M., Zhang X., Henke K., James K.N.,
RA Smith R.S., Hill R.S., Partlow J.N., Al-Saffar M., Kamumbu A.S., Hatem N.,
RA Barkovich A.J., Aziza J., Chassaing N., Zaki M.S., Sultan T., Burglen L.,
RA Rajab A., Al-Gazali L., Mochida G.H., Harris M.P., Gleeson J.G.,
RA Walsh C.A.;
RT "Regulation of human cerebral cortical development by EXOC7 and EXOC8,
RT components of the exocyst complex, and roles in neural progenitor cell
RT proliferation and survival.";
RL Genet. Med. 22:1040-1050(2020).
CC -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts (via PH
CC domain) with GTP-bound RALA and RALB (PubMed:14525976,
CC PubMed:18756269). Interacts with SH3BP1; required for the localization
CC of both SH3BP1 and the exocyst to the leading edge of migrating cells
CC (PubMed:21658605). {ECO:0000250|UniProtKB:O54924,
CC ECO:0000269|PubMed:14525976, ECO:0000269|PubMed:18756269,
CC ECO:0000269|PubMed:21658605}.
CC -!- INTERACTION:
CC Q8IYI6; Q13155: AIMP2; NbExp=5; IntAct=EBI-742102, EBI-745226;
CC Q8IYI6; Q8N2N9-4: ANKRD36B; NbExp=3; IntAct=EBI-742102, EBI-12170453;
CC Q8IYI6; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-742102, EBI-12811889;
CC Q8IYI6; Q14457: BECN1; NbExp=4; IntAct=EBI-742102, EBI-949378;
CC Q8IYI6; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-742102, EBI-745073;
CC Q8IYI6; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-742102, EBI-1012434;
CC Q8IYI6; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-742102, EBI-465872;
CC Q8IYI6; Q9UL45: BLOC1S6; NbExp=4; IntAct=EBI-742102, EBI-465781;
CC Q8IYI6; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-742102, EBI-2548012;
CC Q8IYI6; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-742102, EBI-10193358;
CC Q8IYI6; P20807-4: CAPN3; NbExp=3; IntAct=EBI-742102, EBI-11532021;
CC Q8IYI6; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-742102, EBI-10175300;
CC Q8IYI6; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-742102, EBI-10181988;
CC Q8IYI6; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-742102, EBI-5453285;
CC Q8IYI6; Q9NPF5: DMAP1; NbExp=3; IntAct=EBI-742102, EBI-399105;
CC Q8IYI6; O00472: ELL2; NbExp=3; IntAct=EBI-742102, EBI-395274;
CC Q8IYI6; Q96DF8: ESS2; NbExp=3; IntAct=EBI-742102, EBI-3928124;
CC Q8IYI6; Q96A65: EXOC4; NbExp=5; IntAct=EBI-742102, EBI-355383;
CC Q8IYI6; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-742102, EBI-19153639;
CC Q8IYI6; Q08379: GOLGA2; NbExp=3; IntAct=EBI-742102, EBI-618309;
CC Q8IYI6; Q6IC98: GRAMD4; NbExp=3; IntAct=EBI-742102, EBI-10962409;
CC Q8IYI6; P29084: GTF2E2; NbExp=5; IntAct=EBI-742102, EBI-2853321;
CC Q8IYI6; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-742102, EBI-8638439;
CC Q8IYI6; Q9UKT9: IKZF3; NbExp=7; IntAct=EBI-742102, EBI-747204;
CC Q8IYI6; Q9ULR0: ISY1; NbExp=3; IntAct=EBI-742102, EBI-2557660;
CC Q8IYI6; Q9ULR0-1: ISY1; NbExp=3; IntAct=EBI-742102, EBI-18398632;
CC Q8IYI6; Q5T5P2-6: KIAA1217; NbExp=3; IntAct=EBI-742102, EBI-10188326;
CC Q8IYI6; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-742102, EBI-14069005;
CC Q8IYI6; P08727: KRT19; NbExp=4; IntAct=EBI-742102, EBI-742756;
CC Q8IYI6; Q15323: KRT31; NbExp=3; IntAct=EBI-742102, EBI-948001;
CC Q8IYI6; O76011: KRT34; NbExp=3; IntAct=EBI-742102, EBI-1047093;
CC Q8IYI6; O76013-2: KRT36; NbExp=4; IntAct=EBI-742102, EBI-11958506;
CC Q8IYI6; Q01546: KRT76; NbExp=3; IntAct=EBI-742102, EBI-2952745;
CC Q8IYI6; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-742102, EBI-1216080;
CC Q8IYI6; Q9H992: MARCHF7; NbExp=3; IntAct=EBI-742102, EBI-949983;
CC Q8IYI6; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-742102, EBI-12516603;
CC Q8IYI6; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-742102, EBI-10182361;
CC Q8IYI6; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-742102, EBI-2548751;
CC Q8IYI6; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-742102, EBI-11522433;
CC Q8IYI6; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-742102, EBI-5662487;
CC Q8IYI6; Q15742: NAB2; NbExp=3; IntAct=EBI-742102, EBI-8641936;
CC Q8IYI6; O14777: NDC80; NbExp=3; IntAct=EBI-742102, EBI-715849;
CC Q8IYI6; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-742102, EBI-741048;
CC Q8IYI6; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-742102, EBI-10302990;
CC Q8IYI6; Q15154-3: PCM1; NbExp=3; IntAct=EBI-742102, EBI-11742977;
CC Q8IYI6; P0CG20: PRR35; NbExp=3; IntAct=EBI-742102, EBI-11986293;
CC Q8IYI6; Q6NUQ1: RINT1; NbExp=5; IntAct=EBI-742102, EBI-726876;
CC Q8IYI6; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-742102, EBI-6257312;
CC Q8IYI6; Q6ZMJ2-2: SCARA5; NbExp=3; IntAct=EBI-742102, EBI-12823227;
CC Q8IYI6; Q16533: SNAPC1; NbExp=3; IntAct=EBI-742102, EBI-11915024;
CC Q8IYI6; Q9NZ72: STMN3; NbExp=3; IntAct=EBI-742102, EBI-725557;
CC Q8IYI6; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-742102, EBI-6872807;
CC Q8IYI6; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-742102, EBI-745392;
CC Q8IYI6; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-742102, EBI-8787464;
CC Q8IYI6; Q99081-3: TCF12; NbExp=3; IntAct=EBI-742102, EBI-11952764;
CC Q8IYI6; P15884-3: TCF4; NbExp=3; IntAct=EBI-742102, EBI-13636688;
CC Q8IYI6; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-742102, EBI-1105213;
CC Q8IYI6; Q14142: TRIM14; NbExp=3; IntAct=EBI-742102, EBI-2820256;
CC Q8IYI6; P19474: TRIM21; NbExp=3; IntAct=EBI-742102, EBI-81290;
CC Q8IYI6; P14373: TRIM27; NbExp=3; IntAct=EBI-742102, EBI-719493;
CC Q8IYI6; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-742102, EBI-2130429;
CC Q8IYI6; Q9BRT2: UQCC2; NbExp=3; IntAct=EBI-742102, EBI-1054584;
CC Q8IYI6; Q8N6Y0: USHBP1; NbExp=5; IntAct=EBI-742102, EBI-739895;
CC Q8IYI6; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-742102, EBI-11975223;
CC Q8IYI6; Q6GMQ7: VPS16; NbExp=3; IntAct=EBI-742102, EBI-17974829;
CC Q8IYI6; Q9H9H4: VPS37B; NbExp=3; IntAct=EBI-742102, EBI-4400866;
CC Q8IYI6; A8K0Z3: WASHC1; NbExp=3; IntAct=EBI-742102, EBI-6160405;
CC Q8IYI6; Q96GY0: ZC2HC1A; NbExp=3; IntAct=EBI-742102, EBI-5458880;
CC Q8IYI6; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-742102, EBI-12272076;
CC Q8IYI6; P13682: ZNF35; NbExp=3; IntAct=EBI-742102, EBI-11041653;
CC Q8IYI6; Q969W8: ZNF566; NbExp=3; IntAct=EBI-742102, EBI-2555762;
CC Q8IYI6; Q5EBL2: ZNF628; NbExp=3; IntAct=EBI-742102, EBI-13086230;
CC Q8IYI6; Q8NAM6: ZSCAN4; NbExp=3; IntAct=EBI-742102, EBI-7252920;
CC Q8IYI6; A0A1U9X8X8; NbExp=5; IntAct=EBI-742102, EBI-17234977;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O54924}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54924}. Cell
CC projection, growth cone {ECO:0000250|UniProtKB:O54924}. Cell projection
CC {ECO:0000250|UniProtKB:O54924}. Note=Perinuclear in undifferentiated
CC PC12 cells. Redistributes to growing neurites and growth cones during
CC neuronal differentiation (By similarity). Binds lipids with
CC phosphatidylinositol 3,4,5-trisphosphate groups (By similarity).
CC Localizes at the leading edge of migrating cells (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:O54924}.
CC -!- DISEASE: Neurodevelopmental disorder with microcephaly, seizures, and
CC brain atrophy (NEDMISB) [MIM:619076]: An autosomal recessive
CC neurodevelopmental disorder characterized by severe global
CC developmental delay, developmental regression with loss of milestones,
CC severe microcephaly, and brain abnormalities, primarily cerebral
CC atrophy and hypoplasia of the corpus callosum. Affected individuals
CC develop seizures in the first year of life. Death in childhood may
CC occur. {ECO:0000269|PubMed:32103185}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the EXO84 family. {ECO:0000305}.
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DR EMBL; AK096460; BAG53295.1; -; mRNA.
DR EMBL; AL117352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471098; EAW69955.1; -; Genomic_DNA.
DR EMBL; BC035763; AAH35763.2; -; mRNA.
DR CCDS; CCDS1593.1; -.
DR RefSeq; NP_787072.2; NM_175876.4.
DR AlphaFoldDB; Q8IYI6; -.
DR SMR; Q8IYI6; -.
DR BioGRID; 127206; 143.
DR ComplexPortal; CPX-4943; Exocyst, EXOC6 variant.
DR ComplexPortal; CPX-4944; Exocyst, EXOC6B variant.
DR CORUM; Q8IYI6; -.
DR IntAct; Q8IYI6; 114.
DR MINT; Q8IYI6; -.
DR STRING; 9606.ENSP00000355605; -.
DR TCDB; 1.F.2.1.2; the octameric exocyst (exocyst) family.
DR iPTMnet; Q8IYI6; -.
DR PhosphoSitePlus; Q8IYI6; -.
DR BioMuta; EXOC8; -.
DR DMDM; 74750763; -.
DR EPD; Q8IYI6; -.
DR jPOST; Q8IYI6; -.
DR MassIVE; Q8IYI6; -.
DR MaxQB; Q8IYI6; -.
DR PaxDb; Q8IYI6; -.
DR PeptideAtlas; Q8IYI6; -.
DR PRIDE; Q8IYI6; -.
DR ProteomicsDB; 71180; -.
DR Antibodypedia; 20797; 96 antibodies from 18 providers.
DR DNASU; 149371; -.
DR Ensembl; ENST00000366645.1; ENSP00000355605.2; ENSG00000116903.7.
DR GeneID; 149371; -.
DR KEGG; hsa:149371; -.
DR MANE-Select; ENST00000366645.1; ENSP00000355605.2; NM_175876.5; NP_787072.2.
DR UCSC; uc001huq.4; human.
DR CTD; 149371; -.
DR DisGeNET; 149371; -.
DR GeneCards; EXOC8; -.
DR HGNC; HGNC:24659; EXOC8.
DR HPA; ENSG00000116903; Low tissue specificity.
DR MalaCards; EXOC8; -.
DR MIM; 615283; gene.
DR MIM; 619076; phenotype.
DR neXtProt; NX_Q8IYI6; -.
DR OpenTargets; ENSG00000116903; -.
DR PharmGKB; PA134991382; -.
DR VEuPathDB; HostDB:ENSG00000116903; -.
DR eggNOG; KOG2215; Eukaryota.
DR GeneTree; ENSGT00390000015936; -.
DR HOGENOM; CLU_025760_0_0_1; -.
DR InParanoid; Q8IYI6; -.
DR OMA; SACVKWA; -.
DR OrthoDB; 1357584at2759; -.
DR PhylomeDB; Q8IYI6; -.
DR TreeFam; TF105819; -.
DR PathwayCommons; Q8IYI6; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-264876; Insulin processing.
DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR SignaLink; Q8IYI6; -.
DR BioGRID-ORCS; 149371; 272 hits in 1088 CRISPR screens.
DR GeneWiki; EXOC8; -.
DR GenomeRNAi; 149371; -.
DR Pharos; Q8IYI6; Tbio.
DR PRO; PR:Q8IYI6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8IYI6; protein.
DR Bgee; ENSG00000116903; Expressed in epithelial cell of pancreas and 193 other tissues.
DR Genevisible; Q8IYI6; HS.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000145; C:exocyst; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IDA:MGI.
DR GO; GO:0022617; P:extracellular matrix disassembly; IMP:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IC:ComplexPortal.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:ComplexPortal.
DR Gene3D; 1.20.58.1210; -; 1.
DR Gene3D; 1.20.58.1220; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR033961; Exo84.
DR InterPro; IPR032403; Exo84_C.
DR InterPro; IPR042561; Exo84_C_1.
DR InterPro; IPR042560; Exo84_C_2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR21426; PTHR21426; 1.
DR Pfam; PF16528; Exo84_C; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Disease variant; Epilepsy; Exocytosis;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..725
FT /note="Exocyst complex component 8"
FT /id="PRO_0000227550"
FT DOMAIN 182..282
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 137..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 265
FT /note="E -> G (found in a patient with Joubert syndrome;
FT unknown pathological significance; dbSNP:rs483352868)"
FT /evidence="ECO:0000269|PubMed:22700954"
FT /id="VAR_082196"
SQ SEQUENCE 725 AA; 81799 MW; F4E5E344EF24FDCA CRC64;
MAMAMSDSGA SRLRRQLESG GFEARLYVKQ LSQQSDGDRD LQEHRQRIQA LAEETAQNLK
RNVYQNYRQF IETAREISYL ESEMYQLSHL LTEQKSSLES IPLTLLPAAA AAGAAAASGG
EEGVGGAGGR DHLRGQAGFF STPGGASRDG SGPGEEGKQR TLTTLLEKVE GCRHLLETPG
QYLVYNGDLV EYDADHMAQL QRVHGFLMND CLLVATWLPQ RRGMYRYNAL YSLDGLAVVN
VKDNPPMKDM FKLLMFPESR IFQAENAKIK REWLEVLEDT KRALSEKRRR EQEEAAAPRG
PPQVTSKATN PFEDDEEEEP AVPEVEEEKV DLSMEWIQEL PEDLDVCIAQ RDFEGAVDLL
DKLNHYLEDK PSPPPVKELR AKVEERVRQL TEVLVFELSP DRSLRGGPKA TRRAVSQLIR
LGQCTKACEL FLRNRAAAVH TAIRQLRIEG ATLLYIHKLC HVFFTSLLET AREFEIDFAG
TDSGCYSAFV VWARSAMGMF VDAFSKQVFD SKESLSTAAE CVKVAKEHCQ QLGDIGLDLT
FIIHALLVKD IQGALHSYKE IIIEATKHRN SEEMWRRMNL MTPEALGKLK EEMKSCGVSN
FEQYTGDDCW VNLSYTVVAF TKQTMGFLEE ALKLYFPELH MVLLESLVEI ILVAVQHVDY
SLRCEQDPEK KAFIRQNASF LYETVLPVVE KRFEEGVGKP AKQLQDLRNA SRLIRVNPES
TTSVV
