EXOC8_MOUSE
ID EXOC8_MOUSE Reviewed; 716 AA.
AC Q6PGF7;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Exocyst complex component 8;
DE AltName: Full=Exocyst complex 84 kDa subunit;
GN Name=Exoc8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-313, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts (via PH
CC domain) with GTP-bound RALA and RALB (By similarity). Interacts with
CC SH3BP1; required for the localization of both SH3BP1 and the exocyst to
CC the leading edge of migrating cells (By similarity).
CC {ECO:0000250|UniProtKB:O54924, ECO:0000250|UniProtKB:Q8IYI6}.
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=Binds lipids with
CC phosphatidylinositol 3,4,5-trisphosphate groups (By similarity).
CC Perinuclear in undifferentiated PC12 cells. Redistributes to growing
CC neurites and growth cones during NGF-induced neuronal differentiation
CC (By similarity). Localizes at the leading edge of migrating cells (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:O54924}.
CC -!- SIMILARITY: Belongs to the EXO84 family. {ECO:0000305}.
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DR EMBL; BC057052; AAH57052.1; -; mRNA.
DR CCDS; CCDS22777.1; -.
DR RefSeq; NP_932771.1; NM_198103.2.
DR AlphaFoldDB; Q6PGF7; -.
DR BioGRID; 221786; 11.
DR ComplexPortal; CPX-4982; Exocyst, Exoc6 variant.
DR ComplexPortal; CPX-4983; Exocyst, Exoc6b variant.
DR IntAct; Q6PGF7; 2.
DR STRING; 10090.ENSMUSP00000095915; -.
DR iPTMnet; Q6PGF7; -.
DR PhosphoSitePlus; Q6PGF7; -.
DR EPD; Q6PGF7; -.
DR MaxQB; Q6PGF7; -.
DR PaxDb; Q6PGF7; -.
DR PeptideAtlas; Q6PGF7; -.
DR PRIDE; Q6PGF7; -.
DR ProteomicsDB; 275557; -.
DR Antibodypedia; 20797; 96 antibodies from 18 providers.
DR DNASU; 102058; -.
DR Ensembl; ENSMUST00000098312; ENSMUSP00000095915; ENSMUSG00000074030.
DR GeneID; 102058; -.
DR KEGG; mmu:102058; -.
DR UCSC; uc009nxw.1; mouse.
DR CTD; 149371; -.
DR MGI; MGI:2142527; Exoc8.
DR VEuPathDB; HostDB:ENSMUSG00000074030; -.
DR eggNOG; KOG2215; Eukaryota.
DR GeneTree; ENSGT00390000015936; -.
DR HOGENOM; CLU_025760_0_0_1; -.
DR InParanoid; Q6PGF7; -.
DR OMA; SACVKWA; -.
DR OrthoDB; 1357584at2759; -.
DR PhylomeDB; Q6PGF7; -.
DR TreeFam; TF105819; -.
DR Reactome; R-MMU-264876; Insulin processing.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 102058; 13 hits in 74 CRISPR screens.
DR ChiTaRS; Exoc8; mouse.
DR PRO; PR:Q6PGF7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6PGF7; protein.
DR Bgee; ENSMUSG00000074030; Expressed in spermatocyte and 238 other tissues.
DR Genevisible; Q6PGF7; MM.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0000145; C:exocyst; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0007032; P:endosome organization; ISO:MGI.
DR GO; GO:0006887; P:exocytosis; ISO:MGI.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Exocytosis; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..716
FT /note="Exocyst complex component 8"
FT /id="PRO_0000227551"
FT DOMAIN 173..273
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 129..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYI6"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747"
SQ SEQUENCE 716 AA; 81035 MW; E512707F1DEF36E1 CRC64;
MSDSGASRLR RQLESGGFEA RLYVKQLSQQ SDGDRDLQEH RQRVQALAEE TAQNLKRNVY
QNYRQFIETA REISYLESEM YQLSHLLTEQ KSSLESIPLA LLPAAAAGAS AGEDTAGAGP
RERGAVQAGF LPGPAGVPRE GSGTGEEGKQ RTLTTLLEKV EGCRDLLETP GQYLVYNGDL
VEYDADHMAQ LQRVHGFLMN DCLLVATWLP QRRGMYRYNA LYPLDRLAVV NVKDNPPMKD
MFKLLMFPES RIFQAENAKI KREWLEVLEE TKRALSDKRR REQEEAAAPR APPPVTSKGS
NPFEDEDDEE LATPEAEEEK VDLSMEWIQE LPEDLDVCIA QRDFEGAVDL LDKLNHYLED
KPSPPPVKEL RAKVDERVRQ LTEVLVFELS PDRSLRGGPK ATRRAVSQLI RLGQCTKACE
LFLRNRAAAV HTAIRQLRIE GATLLYIHKL CHVFFTSLLE TAREFETDFA GTDSGCYSAF
VVWARSAMGM FVDAFSKQVF DSKESLSTAA ECVKVAKEHC QQLGEIGLDL TFIIHALLVK
DIQGALHSYK EIIIEATKHR NSEEMWRRMN LMTPEALGKL KEEMKSCGVS NFEQYTGDDC
WVNLSYTVVA FTKQTMGFLE EALKLYFPEL HMVLLESLVE IILVAVQHVD YSLRCEQDPE
KKAFIRQNAS FLYETVLPVV ERRFEEGVGK PAKQLQDLRN ASRLLRVNPE STTSVV
