EXOC8_RAT
ID EXOC8_RAT Reviewed; 716 AA.
AC O54924;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, 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; Synonyms=Exo84;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION IN
RP EXOCYST COMPLEX.
RC TISSUE=Brain;
RX PubMed=9405631; DOI=10.1073/pnas.94.26.14438;
RA Kee Y., Yoo J.-S., Hazuka C.D., Peterson K.E., Hsu S.-C., Scheller R.H.;
RT "Subunit structure of the mammalian exocyst complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14438-14443(1997).
RN [2]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EXOC3 AND EXOC6.
RX PubMed=12954101; DOI=10.1089/153685903322286575;
RA Wang S., Hsu S.C.;
RT "Immunological characterization of exocyst complex subunits in cell
RT differentiation.";
RL Hybrid. Hybridomics 22:159-164(2003).
RN [3]
RP SUBCELLULAR LOCATION.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-313, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 167-286 IN COMPLEX WITH RALA, AND
RP MUTAGENESIS OF ALA-228 AND LYS-233.
RX PubMed=15920473; DOI=10.1038/sj.emboj.7600699;
RA Jin R., Junutula J.R., Matern H.T., Ervin K.E., Scheller R.H.,
RA Brunger A.T.;
RT "Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA
RT GTPase.";
RL EMBO J. 24:2064-2074(2005).
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 (PubMed:9405631, PubMed:12954101).
CC Interacts (via PH domain) with GTP-bound RALA and RALB (By similarity)
CC (PubMed:15920473). Interacts with SH3BP1; required for the localization
CC of both SH3BP1 and the exocyst to the leading edge of migrating cells
CC (By similarity). {ECO:0000250|UniProtKB:Q8IYI6,
CC ECO:0000269|PubMed:12954101, ECO:0000269|PubMed:15920473,
CC ECO:0000269|PubMed:9405631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12954101}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:12954101}. Cell
CC projection, growth cone {ECO:0000269|PubMed:12954101}. Cell projection
CC {ECO:0000269|PubMed:21658605}. 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 (PubMed:12954101). Localizes at the leading edge of migrating cells
CC (PubMed:21658605). {ECO:0000250, ECO:0000269|PubMed:12954101,
CC ECO:0000269|PubMed:21658605}.
CC -!- SIMILARITY: Belongs to the EXO84 family. {ECO:0000305}.
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DR EMBL; AF032669; AAC01581.1; -; mRNA.
DR PIR; T09222; T09222.
DR RefSeq; NP_620612.1; NM_139043.1.
DR PDB; 1ZC3; X-ray; 2.00 A; B/D=167-279.
DR PDB; 1ZC4; X-ray; 2.50 A; B/D=167-286.
DR PDBsum; 1ZC3; -.
DR PDBsum; 1ZC4; -.
DR AlphaFoldDB; O54924; -.
DR SMR; O54924; -.
DR BioGRID; 251437; 1.
DR CORUM; O54924; -.
DR STRING; 10116.ENSRNOP00000026757; -.
DR iPTMnet; O54924; -.
DR PhosphoSitePlus; O54924; -.
DR jPOST; O54924; -.
DR PaxDb; O54924; -.
DR PRIDE; O54924; -.
DR Ensembl; ENSRNOT00000026757; ENSRNOP00000026757; ENSRNOG00000019766.
DR GeneID; 245709; -.
DR KEGG; rno:245709; -.
DR UCSC; RGD:620245; rat.
DR CTD; 149371; -.
DR RGD; 620245; Exoc8.
DR eggNOG; KOG2215; Eukaryota.
DR GeneTree; ENSGT00390000015936; -.
DR HOGENOM; CLU_025760_0_0_1; -.
DR InParanoid; O54924; -.
DR OMA; SACVKWA; -.
DR OrthoDB; 1357584at2759; -.
DR PhylomeDB; O54924; -.
DR TreeFam; TF105819; -.
DR Reactome; R-RNO-264876; Insulin processing.
DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR EvolutionaryTrace; O54924; -.
DR PRO; PR:O54924; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000019766; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; O54924; RN.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0000145; C:exocyst; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0007032; P:endosome organization; ISO:RGD.
DR GO; GO:0006887; P:exocytosis; ISO:RGD.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:RGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 3D-structure; Cell projection; Cytoplasm; Direct protein sequencing;
KW Exocytosis; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..716
FT /note="Exocyst complex component 8"
FT /id="PRO_0000227552"
FT DOMAIN 173..273
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 110..149
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:22673903"
FT MUTAGEN 228
FT /note="A->W: Strongly reduces interaction with RALA."
FT /evidence="ECO:0000269|PubMed:15920473"
FT MUTAGEN 233
FT /note="K->W: Strongly reduces interaction with RALA."
FT /evidence="ECO:0000269|PubMed:15920473"
FT STRAND 174..184
FT /evidence="ECO:0007829|PDB:1ZC3"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:1ZC3"
FT STRAND 190..209
FT /evidence="ECO:0007829|PDB:1ZC3"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:1ZC3"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1ZC3"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1ZC3"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:1ZC3"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:1ZC3"
FT HELIX 258..278
FT /evidence="ECO:0007829|PDB:1ZC3"
SQ SEQUENCE 716 AA; 81043 MW; EE6945C7F25B18AC CRC64;
MSDSGASRLR RQLESGGFEA RLYVKQLSQQ SDGDRDLQEH RQRVQALAEE TAQNLKRNVY
QNYRQFIETA REISYLESEM YQLSHLLTEQ KSSLESIPLA LLPAAAAGAS TGEDTAGAGP
RERGAAQAGF LPGPAGVPRE GPGTGEEGKQ RTLTTLLEKV EGCRDLLETP GQYLVYNGDL
VEYEADHMAQ LQRVHGFLMN DCLLVATWLP QRRGMYRYNA LYPLDRLAVV NVKDNPPMKD
MFKLLMFPES RIFQAENAKI KREWLEVLEE TKRALSDKRR REQEEAAALR APPPVTSKGS
NPFEDEAEEE LATPEAEEEK VDLSMEWIQE LPEDLDVCIA QRDFEGAVDL LDKLNHYLED
KPSPPSVKEL RAKVDERVRQ LTEVLVFELS PDRSLRGGPK ATRRAVSQLI RLGQCTKACE
LFLRNRAAAV HTAIRQLRIE GATLLYIHKL CHVFFTSLLE TAREFETDFA GTDSGCYSAF
VVWARSAMGM FVDAFSKQVF DSKESLSTAA ECVKVAKEHC QQLGEIGLDL TFIIHALLVK
DIQGALLSYK EIIIEATKHR NSEEMWRRMN LMTPEALGKL KEEMRSCGVS NFEQYTGDDC
WVNLSYTVVA FTKQTMGFLE EALKLYFPEL HMVLLESLVE VILVAVQHVD YSLRCEQDPE
KKTFIRQNAS FLYDTVLPVV ERRFEEGVGK PAKQLQDLRN ASRLLRVNPE STTSVV
