EXOC7_HUMAN
ID EXOC7_HUMAN Reviewed; 735 AA.
AC Q9UPT5; B5MC69; B8XXP2; Q8ND93; Q8WV91; Q96FF0; Q9H8C3; Q9H9X3; Q9HA32;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Exocyst complex component 7;
DE AltName: Full=Exocyst complex component Exo70;
GN Name=EXOC7; Synonyms=EXO70, KIAA1067;
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] (ISOFORMS 5 AND 6).
RA Dellago H., Loescher M., Ajuh P., Voglauer R., Fortschegger K.,
RA Eisenhaber F., Lamond A.I., Grillari J.;
RT "EXOC7 is alternatively spliced in cellular senescence.";
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Mammary gland, Placenta, and Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Eye;
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 [7]
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 [8]
RP INTERACTION WITH RAB11FIP3.
RX PubMed=16148947; DOI=10.1038/sj.emboj.7600803;
RA Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X., Hickson G.R.,
RA Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.;
RT "Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane
RT traffic in cytokinesis.";
RL EMBO J. 24:3389-3399(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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 [11]
RP IDENTIFICATION BY 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 [12]
RP TISSUE SPECIFICITY, INVOLVEMENT IN NEDSEBA, AND VARIANTS NEDSEBA SER-48 DEL
RP AND THR-574.
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. In
CC adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the
CC plasma membrane in response to insulin, perhaps directing the vesicle
CC to the precise site of fusion (By similarity). It is required for
CC neuron survival and plays an essential role in cortical development (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:E7FC72}.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with ARHQ in a GTP-dependent
CC manner. Interacts with RAB11FIP3 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UPT5; O14964: HGS; NbExp=4; IntAct=EBI-720048, EBI-740220;
CC Q9UPT5; Q8IY31: IFT20; NbExp=4; IntAct=EBI-720048, EBI-744203;
CC Q9UPT5; Q969G3: SMARCE1; NbExp=5; IntAct=EBI-720048, EBI-455078;
CC Q9UPT5; A1L4H1: SSC5D; NbExp=3; IntAct=EBI-720048, EBI-10172867;
CC Q9UPT5; Q9WMX2; Xeno; NbExp=3; IntAct=EBI-720048, EBI-710918;
CC Q9UPT5-1; Q9Y6D5: ARFGEF2; NbExp=4; IntAct=EBI-6251402, EBI-2837511;
CC Q9UPT5-1; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-6251402, EBI-10175300;
CC Q9UPT5-1; Q8WUE5: CT55; NbExp=3; IntAct=EBI-6251402, EBI-6873363;
CC Q9UPT5-1; Q9NVF7: FBXO28; NbExp=3; IntAct=EBI-6251402, EBI-740282;
CC Q9UPT5-1; O60341: KDM1A; NbExp=3; IntAct=EBI-6251402, EBI-710124;
CC Q9UPT5-1; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-6251402, EBI-14069005;
CC Q9UPT5-1; Q9BQD3: KXD1; NbExp=3; IntAct=EBI-6251402, EBI-739657;
CC Q9UPT5-1; A6NI15: MSGN1; NbExp=3; IntAct=EBI-6251402, EBI-11991020;
CC Q9UPT5-1; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-6251402, EBI-742388;
CC Q9UPT5-1; Q53GL6: RALY; NbExp=3; IntAct=EBI-6251402, EBI-9512693;
CC Q9UPT5-1; Q86UD0: SAPCD2; NbExp=3; IntAct=EBI-6251402, EBI-2561646;
CC Q9UPT5-1; O95295: SNAPIN; NbExp=3; IntAct=EBI-6251402, EBI-296723;
CC Q9UPT5-1; A1L4H1: SSC5D; NbExp=3; IntAct=EBI-6251402, EBI-10172867;
CC Q9UPT5-1; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-6251402, EBI-2130429;
CC Q9UPT5-1; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-6251402, EBI-739895;
CC Q9UPT5-1; Q9NRH1: YAE1; NbExp=3; IntAct=EBI-6251402, EBI-712905;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O35250}. Cell membrane
CC {ECO:0000250|UniProtKB:O35250}; Peripheral membrane protein
CC {ECO:0000305}. Midbody, Midbody ring {ECO:0000269|PubMed:16213214}.
CC Note=Translocates, as a preformed complex with EXOC3/SEC6 and
CC EXOC4/SEC8, to the plasma membrane in response to insulin through the
CC activation of ARHQ (By similarity). Colocalizes with CNTRL/centriolin
CC at the midbody ring (PubMed:16213214). {ECO:0000250|UniProtKB:O35250,
CC ECO:0000269|PubMed:16213214}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=3;
CC IsoId=Q9UPT5-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9UPT5-1; Sequence=VSP_008878;
CC Name=2;
CC IsoId=Q9UPT5-2; Sequence=VSP_001483;
CC Name=4;
CC IsoId=Q9UPT5-4; Sequence=VSP_008876, VSP_008877;
CC Name=5;
CC IsoId=Q9UPT5-5; Sequence=VSP_041098;
CC Name=6;
CC IsoId=Q9UPT5-6; Sequence=VSP_041099;
CC -!- TISSUE SPECIFICITY: Abundant in the ventricular zone, the outer
CC subventricular zone and the cortical plate of the fetal cortex.
CC {ECO:0000269|PubMed:32103185}.
CC -!- DOMAIN: The N-terminus is involved in SEC8 and ARHQ binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The C-terminus is required for translocation to the plasma
CC membrane. {ECO:0000250}.
CC -!- DISEASE: Neurodevelopmental disorder with seizures and brain atrophy
CC (NEDSEBA) [MIM:619072]: An autosomal recessive disorder characterized
CC by brain atrophy, seizures, and developmental delay. Disease severity
CC is variable. Severely affected individuals develop symptoms in utero,
CC which may lead to spontaneous abortion. Patients at the mildest end of
CC the phenotypic spectrum have onset of seizures later in childhood and
CC show developmental delay with mildly impaired intellectual development
CC and minimal brain atrophy. {ECO:0000269|PubMed:32103185}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the EXO70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83019.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14095.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FJ457119; ACK36853.1; -; mRNA.
DR EMBL; FJ457120; ACK36854.1; -; mRNA.
DR EMBL; AB028990; BAA83019.1; ALT_INIT; mRNA.
DR EMBL; AK022397; BAB14026.1; -; mRNA.
DR EMBL; AK022552; BAB14095.1; ALT_INIT; mRNA.
DR EMBL; AK023832; BAB14694.1; -; mRNA.
DR EMBL; AL834324; CAD38992.2; -; mRNA.
DR EMBL; AC018665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011045; AAH11045.1; -; mRNA.
DR EMBL; BC018466; AAH18466.1; -; mRNA.
DR CCDS; CCDS11741.1; -. [Q9UPT5-2]
DR CCDS; CCDS32738.1; -. [Q9UPT5-1]
DR CCDS; CCDS45781.1; -. [Q9UPT5-5]
DR CCDS; CCDS45782.1; -. [Q9UPT5-3]
DR CCDS; CCDS45783.1; -. [Q9UPT5-6]
DR RefSeq; NP_001013861.1; NM_001013839.3. [Q9UPT5-1]
DR RefSeq; NP_001138769.1; NM_001145297.3. [Q9UPT5-3]
DR RefSeq; NP_001138770.1; NM_001145298.3. [Q9UPT5-5]
DR RefSeq; NP_001138771.1; NM_001145299.3. [Q9UPT5-6]
DR RefSeq; NP_001269242.1; NM_001282313.1.
DR RefSeq; NP_056034.2; NM_015219.4. [Q9UPT5-2]
DR AlphaFoldDB; Q9UPT5; -.
DR SMR; Q9UPT5; -.
DR BioGRID; 116867; 115.
DR ComplexPortal; CPX-4943; Exocyst, EXOC6 variant.
DR ComplexPortal; CPX-4944; Exocyst, EXOC6B variant.
DR CORUM; Q9UPT5; -.
DR DIP; DIP-37604N; -.
DR IntAct; Q9UPT5; 71.
DR MINT; Q9UPT5; -.
DR STRING; 9606.ENSP00000334100; -.
DR TCDB; 1.F.2.1.2; the octameric exocyst (exocyst) family.
DR GlyGen; Q9UPT5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UPT5; -.
DR PhosphoSitePlus; Q9UPT5; -.
DR BioMuta; EXOC7; -.
DR DMDM; 38372889; -.
DR EPD; Q9UPT5; -.
DR jPOST; Q9UPT5; -.
DR MassIVE; Q9UPT5; -.
DR MaxQB; Q9UPT5; -.
DR PaxDb; Q9UPT5; -.
DR PeptideAtlas; Q9UPT5; -.
DR PRIDE; Q9UPT5; -.
DR ProteomicsDB; 85434; -. [Q9UPT5-3]
DR ProteomicsDB; 85435; -. [Q9UPT5-1]
DR ProteomicsDB; 85436; -. [Q9UPT5-2]
DR ProteomicsDB; 85437; -. [Q9UPT5-4]
DR ProteomicsDB; 85438; -. [Q9UPT5-5]
DR ProteomicsDB; 85439; -. [Q9UPT5-6]
DR Antibodypedia; 19667; 198 antibodies from 33 providers.
DR DNASU; 23265; -.
DR Ensembl; ENST00000332065.9; ENSP00000333806.4; ENSG00000182473.22. [Q9UPT5-2]
DR Ensembl; ENST00000335146.11; ENSP00000334100.6; ENSG00000182473.22. [Q9UPT5-3]
DR Ensembl; ENST00000411744.6; ENSP00000404322.2; ENSG00000182473.22. [Q9UPT5-5]
DR Ensembl; ENST00000589210.6; ENSP00000468404.1; ENSG00000182473.22. [Q9UPT5-1]
DR Ensembl; ENST00000634349.1; ENSP00000489266.1; ENSG00000182473.22. [Q9UPT5-6]
DR GeneID; 23265; -.
DR KEGG; hsa:23265; -.
DR MANE-Select; ENST00000589210.6; ENSP00000468404.1; NM_001013839.4; NP_001013861.1. [Q9UPT5-1]
DR UCSC; uc002jqq.5; human. [Q9UPT5-3]
DR CTD; 23265; -.
DR DisGeNET; 23265; -.
DR GeneCards; EXOC7; -.
DR HGNC; HGNC:23214; EXOC7.
DR HPA; ENSG00000182473; Low tissue specificity.
DR MalaCards; EXOC7; -.
DR MIM; 608163; gene.
DR MIM; 619072; phenotype.
DR neXtProt; NX_Q9UPT5; -.
DR OpenTargets; ENSG00000182473; -.
DR PharmGKB; PA134988420; -.
DR VEuPathDB; HostDB:ENSG00000182473; -.
DR eggNOG; KOG2344; Eukaryota.
DR GeneTree; ENSGT00390000003595; -.
DR InParanoid; Q9UPT5; -.
DR OMA; GPIYGNT; -.
DR OrthoDB; 410847at2759; -.
DR PhylomeDB; Q9UPT5; -.
DR TreeFam; TF324243; -.
DR PathwayCommons; Q9UPT5; -.
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; Q9UPT5; -.
DR SIGNOR; Q9UPT5; -.
DR BioGRID-ORCS; 23265; 317 hits in 1081 CRISPR screens.
DR ChiTaRS; EXOC7; human.
DR GeneWiki; EXOC7; -.
DR GenomeRNAi; 23265; -.
DR Pharos; Q9UPT5; Tbio.
DR PRO; PR:Q9UPT5; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UPT5; protein.
DR Bgee; ENSG00000182473; Expressed in right uterine tube and 201 other tissues.
DR ExpressionAtlas; Q9UPT5; baseline and differential.
DR Genevisible; Q9UPT5; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:BHF-UCL.
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; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; IMP:AgBase.
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; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR004140; Exo70.
DR InterPro; IPR046364; Exo70_C.
DR PANTHER; PTHR12542; PTHR12542; 1.
DR Pfam; PF03081; Exo70; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasm; Epilepsy;
KW Exocytosis; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..735
FT /note="Exocyst complex component 7"
FT /id="PRO_0000118960"
FT REGION 239..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..42
FT /evidence="ECO:0000255"
FT COILED 63..85
FT /evidence="ECO:0000255"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54922"
FT VAR_SEQ 269..327
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_041098"
FT VAR_SEQ 271..352
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_001483"
FT VAR_SEQ 271..283
FT /note="TIRKAQNLLKQYS -> EPPSWPISATARG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008876"
FT VAR_SEQ 284..735
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008877"
FT VAR_SEQ 301..328
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_041099"
FT VAR_SEQ 302..352
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_008878"
FT VARIANT 48
FT /note="Missing (in NEDSEBA; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32103185"
FT /id="VAR_085057"
FT VARIANT 574
FT /note="A -> T (in NEDSEBA; unknown pathological
FT significance; dbSNP:rs762553587)"
FT /evidence="ECO:0000269|PubMed:32103185"
FT /id="VAR_085058"
FT CONFLICT 234
FT /note="L -> Q (in Ref. 3; BAB14694)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="D -> N (in Ref. 3; BAB14694)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="N -> I (in Ref. 6; AAH18466)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="D -> G (in Ref. 3; BAB14694)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 735 AA; 83382 MW; 6B929762542854B6 CRC64;
MIPPQEASAR RREIEDKLKQ EEETLSFIRD SLEKSDQLTK NMVSILSSFE SRLMKLENSI
IPVHKQTENL QRLQENVEKT LSCLDHVISY YHVASDTEKI IREGPTGRLE EYLGSMAKIQ
KAVEYFQDNS PDSPELNKVK LLFERGKEAL ESEFRSLMTR HSKVVSPVLI LDLISGDDDL
EAQEDVTLEH LPESVLQDVI RISRWLVEYG RNQDFMNVYY QIRSSQLDRS IKGLKEHFHK
SSSSSGVPYS PAIPNKRKDT PTKKPVKRPG TIRKAQNLLK QYSQHGLDGK KGGSNLIPLE
GLLPCTPRGG LPGPWINAAC VCAADISPGH EHDFRVKHLS EALNDKHGPL AGRDDMLDVE
TDAYIHCVSA FVKLAQSEYQ LLADIIPEHH QKKTFDSLIQ DALDGLMLEG ENIVSAARKA
IVRHDFSTVL TVFPILRHLK QTKPEFDQVL QGTAASTKNK LPGLITSMET IGAKALEDFA
DNIKNDPDKE YNMPKDGTVH ELTSNAILFL QQLLDFQETA GAMLASQETS SSATSYSSEF
SKRLLSTYIC KVLGNLQLNL LSKSKVYEDP ALSAIFLHNN YNYILKSLEK SELIQLVAVT
QKTAERSYRE HIEQQIQTYQ RSWLKVTDYI AEKNLPVFQP GVKLRDKERQ IIKERFKGFN
DGLEELCKIQ KAWAIPDTEQ RDRIRQAQKT IVKETYGAFL QKFGSVPFTK NPEKYIKYGV
EQVGDMIDRL FDTSA
