EXOC4_HUMAN
ID EXOC4_HUMAN Reviewed; 974 AA.
AC Q96A65; E9PED2; Q541U8; Q9C0G4; Q9H9K0; Q9P102;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Exocyst complex component 4;
DE AltName: Full=Exocyst complex component Sec8;
GN Name=EXOC4; Synonyms=KIAA1699, SEC8, SEC8L1;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Sha J.H.;
RT "Human secretory protein Sec8 related to testis development.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Melanoma, and Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
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 [7]
RP PROTEIN SEQUENCE OF 2-11; 224-239; 314-325 AND 889-896, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Foreskin fibroblast;
RA Bienvenut W.V., Campbell A., Ozanne B.W.;
RL Submitted (JUN-2009) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-974 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 338-974 (ISOFORM 1).
RA Luo W.Q., Chen J.H., Huang X.W., Zhou Y., Zhou H.J., Hu S.N., Yuan J.G.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=16213214; DOI=10.1016/j.cell.2005.07.027;
RA Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S.,
RA Guha M., Sillibourne J., Doxsey S.J.;
RT "Centriolin anchoring of exocyst and SNARE complexes at the midbody is
RT required for secretory-vesicle-mediated abscission.";
RL Cell 123:75-87(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP INTERACTION WITH BIRC6/BRUCE.
RX PubMed=18329369; DOI=10.1016/j.cell.2008.01.012;
RA Pohl C., Jentsch S.;
RT "Final stages of cytokinesis and midbody ring formation are controlled by
RT BRUCE.";
RL Cell 132:832-845(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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 [18]
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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-226; THR-233; THR-237
RP AND SER-468, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP VARIANTS [LARGE SCALE ANALYSIS] PHE-220 AND THR-599.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with
CC BIRC6/bruce (PubMed:18329369). Interacts with MYRIP (By similarity).
CC Interacts with SH3BP1; required for the localization of both SH3BP1 and
CC the exocyst to the leading edge of migrating cells (PubMed:21658605).
CC Interacts with SLC6A9 (By similarity). {ECO:0000250|UniProtKB:Q62824,
CC ECO:0000269|PubMed:18329369, ECO:0000269|PubMed:21658605}.
CC -!- INTERACTION:
CC Q96A65; Q9NR09: BIRC6; NbExp=3; IntAct=EBI-355383, EBI-1765160;
CC Q96A65; P00533: EGFR; NbExp=2; IntAct=EBI-355383, EBI-297353;
CC Q96A65; Q9NV70: EXOC1; NbExp=5; IntAct=EBI-355383, EBI-1045313;
CC Q96A65; Q8IYI6: EXOC8; NbExp=5; IntAct=EBI-355383, EBI-742102;
CC Q96A65; Q86VI4: LAPTM4B; NbExp=2; IntAct=EBI-355383, EBI-3267258;
CC Q96A65; Q13496: MTM1; NbExp=2; IntAct=EBI-355383, EBI-2864109;
CC Q96A65; O60271: SPAG9; NbExp=3; IntAct=EBI-355383, EBI-1023301;
CC Q96A65; O70172: Pip4k2a; Xeno; NbExp=3; IntAct=EBI-355383, EBI-644828;
CC Q96A65-2; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-17869840, EBI-10175300;
CC Q96A65-2; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-17869840, EBI-11962928;
CC Q96A65-2; Q92805: GOLGA1; NbExp=3; IntAct=EBI-17869840, EBI-6164177;
CC Q96A65-2; Q9UK53-2: ING1; NbExp=3; IntAct=EBI-17869840, EBI-8068204;
CC Q96A65-2; O95983-2: MBD3; NbExp=3; IntAct=EBI-17869840, EBI-11978579;
CC Q96A65-2; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-17869840, EBI-455078;
CC -!- SUBCELLULAR LOCATION: Midbody, Midbody ring
CC {ECO:0000269|PubMed:16213214}. Cell projection
CC {ECO:0000250|UniProtKB:Q62824}. Note=Colocalizes with CNTRL/centriolin
CC at the midbody ring (PubMed:16213214). Localizes at the leading edge of
CC migrating cells (By similarity). {ECO:0000250|UniProtKB:Q62824,
CC ECO:0000269|PubMed:16213214}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96A65-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96A65-2; Sequence=VSP_047159;
CC -!- SIMILARITY: Belongs to the SEC8 family. {ECO:0000305}.
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DR EMBL; AF380839; AAK57456.1; -; mRNA.
DR EMBL; AK022751; BAB14225.1; -; mRNA.
DR EMBL; AK027688; BAB55298.1; -; mRNA.
DR EMBL; AL831989; CAD89977.1; -; mRNA.
DR EMBL; AL834475; CAD39134.1; -; mRNA.
DR EMBL; AC007790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC083872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC083875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24073.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83804.1; -; Genomic_DNA.
DR EMBL; AB051486; BAB21790.1; -; mRNA.
DR EMBL; AF132734; AAF66445.1; -; mRNA.
DR CCDS; CCDS43648.1; -. [Q96A65-2]
DR CCDS; CCDS5829.1; -. [Q96A65-1]
DR RefSeq; NP_068579.3; NM_021807.3. [Q96A65-1]
DR AlphaFoldDB; Q96A65; -.
DR SMR; Q96A65; -.
DR BioGRID; 121906; 166.
DR ComplexPortal; CPX-4943; Exocyst, EXOC6 variant.
DR ComplexPortal; CPX-4944; Exocyst, EXOC6B variant.
DR CORUM; Q96A65; -.
DR DIP; DIP-32976N; -.
DR IntAct; Q96A65; 78.
DR MINT; Q96A65; -.
DR STRING; 9606.ENSP00000253861; -.
DR TCDB; 1.F.2.1.2; the octameric exocyst (exocyst) family.
DR GlyGen; Q96A65; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96A65; -.
DR PhosphoSitePlus; Q96A65; -.
DR BioMuta; EXOC4; -.
DR DMDM; 24418674; -.
DR EPD; Q96A65; -.
DR jPOST; Q96A65; -.
DR MassIVE; Q96A65; -.
DR MaxQB; Q96A65; -.
DR PaxDb; Q96A65; -.
DR PeptideAtlas; Q96A65; -.
DR PRIDE; Q96A65; -.
DR ProteomicsDB; 19862; -.
DR ProteomicsDB; 75923; -. [Q96A65-1]
DR Antibodypedia; 18039; 184 antibodies from 28 providers.
DR DNASU; 60412; -.
DR Ensembl; ENST00000253861.5; ENSP00000253861.4; ENSG00000131558.15. [Q96A65-1]
DR Ensembl; ENST00000393161.6; ENSP00000376868.2; ENSG00000131558.15. [Q96A65-2]
DR GeneID; 60412; -.
DR KEGG; hsa:60412; -.
DR MANE-Select; ENST00000253861.5; ENSP00000253861.4; NM_021807.4; NP_068579.3.
DR UCSC; uc003vrj.4; human. [Q96A65-1]
DR CTD; 60412; -.
DR DisGeNET; 60412; -.
DR GeneCards; EXOC4; -.
DR HGNC; HGNC:30389; EXOC4.
DR HPA; ENSG00000131558; Low tissue specificity.
DR MIM; 608185; gene.
DR neXtProt; NX_Q96A65; -.
DR OpenTargets; ENSG00000131558; -.
DR PharmGKB; PA134944654; -.
DR VEuPathDB; HostDB:ENSG00000131558; -.
DR eggNOG; KOG3691; Eukaryota.
DR GeneTree; ENSGT00390000001439; -.
DR HOGENOM; CLU_029933_0_0_1; -.
DR InParanoid; Q96A65; -.
DR OMA; SLPNWTD; -.
DR OrthoDB; 96167at2759; -.
DR PhylomeDB; Q96A65; -.
DR TreeFam; TF313954; -.
DR PathwayCommons; Q96A65; -.
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; Q96A65; -.
DR BioGRID-ORCS; 60412; 322 hits in 1087 CRISPR screens.
DR ChiTaRS; EXOC4; human.
DR GeneWiki; EXOC4; -.
DR GenomeRNAi; 60412; -.
DR Pharos; Q96A65; Tbio.
DR PRO; PR:Q96A65; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96A65; protein.
DR Bgee; ENSG00000131558; Expressed in bone marrow cell and 185 other tissues.
DR Genevisible; Q96A65; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0032584; C:growth cone membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0035748; C:myelin sheath abaxonal region; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; 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:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0048341; P:paraxial mesoderm formation; IEA:Ensembl.
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 InterPro; IPR039682; Sec8/EXOC4.
DR InterPro; IPR007191; Sec8_exocyst_N.
DR PANTHER; PTHR14146; PTHR14146; 1.
DR Pfam; PF04048; Sec8_exocyst; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Coiled coil;
KW Direct protein sequencing; Exocytosis; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378"
FT CHAIN 2..974
FT /note="Exocyst complex component 4"
FT /id="PRO_0000118934"
FT COILED 32..114
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 474..974
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047159"
FT VARIANT 220
FT /note="S -> F (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036292"
FT VARIANT 599
FT /note="A -> T (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs768209201)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036293"
FT CONFLICT 293
FT /note="P -> S (in Ref. 3; CAD39134)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="L -> T (in Ref. 9; AAF66445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 974 AA; 110498 MW; 122CD929C2635786 CRC64;
MAAEAAGGKY RSTVSKSKDP SGLLISVIRT LSTSDDVEDR ENEKGRLEEA YEKCDRDLDE
LIVQHYTELT TAIRTYQSIT ERITNSRNKI KQVKENLLSC KMLLHCKRDE LRKLWIEGIE
HKHVLNLLDE IENIKQVPQK LEQCMASKHY LSATDMLVSA VESLEGPLLQ VEGLSDLRLE
LHSKKMNLHL VLIDELHRHL YIKSTSRVVQ RNKEKGKISS LVKDASVPLI DVTNLPTPRK
FLDTSHYSTA GSSSVREINL QDIKEDLELD PEENSTLFMG ILIKGLAKLK KIPETVKAII
ERLEQELKQI VKRSTTQVAD SGYQRGENVT VENQPRLLLE LLELLFDKFN AVAAAHSVVL
GYLQDTVVTP LTQQEDIKLY DMADVWVKIQ DVLQMLLTEY LDMKNTRTAS EPSAQLSYAS
TGREFAAFFA KKKPQRPKNS LFKFESSSHA ISMSAYLREQ RRELYSRSGE LQGGPDDNLI
EGGGTKFVCK PGARNITVIF HPLLRFIQEI EHALGLGPAK QCPLREFLTV YIKNIFLNQV
LAEINKEIEG VTKTSDPLKI LANADTMKVL GVQRPLLQST IIVEKTVQDL LNLMHDLSAY
SDQFLNMVCV KLQEYKDTCT AAYRGIVQSE EKLVISASWA KDDDISRLLK SLPNWMNMAQ
PKQLRPKREE EEDFIRAAFG KESEVLIGNL GDKLIPPQDI LRDVSDLKAL ANMHESLEWL
ASRTKSAFSN LSTSQMLSPA QDSHTNTDLP PVSEQIMQTL SELAKSFQDM ADRCLLVLHL
EVRVHCFHYL IPLAKEGNYA IVANVESMDY DPLVVKLNKD ISAIEEAMSA SLQQHKFQYI
FEGLGHLISC ILINGAQYFR RISESGIKKM CRNIFVLQQN LTNITMSREA DLDFARQYYE
MLYNTADELL NLVVDQGVKY TELEYIHALT LLHRSQTGVG ELTTQNTRLQ RLKEIICEQA
AIKQATKDKK ITTV
