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Protein

Exocyst complex component 8

Gene

Exoc8

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.

GO - Biological processi

  • cellular protein localization Source: RGD
  • endosome organization Source: Ensembl
  • exocyst assembly Source: GO_Central
  • exocyst localization Source: GO_Central
  • exocytosis Source: RGD
  • extracellular matrix disassembly Source: Ensembl
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-264876. Insulin processing.
R-RNO-5620916. VxPx cargo-targeting to cilium.

Names & Taxonomyi

Protein namesi
Recommended name:
Exocyst complex component 8
Alternative name(s):
Exocyst complex 84 kDa subunit
Gene namesi
Name:Exoc8
Synonyms:Exo84
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi620245. Exoc8.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cytoplasmperinuclear region 1 Publication
  • Cell projectiongrowth cone 1 Publication

  • Note: Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during cell differentiation.By similarity

GO - Cellular componenti

  • exocyst Source: RGD
  • growth cone Source: UniProtKB-SubCell
  • late endosome Source: Ensembl
  • membrane Source: Ensembl
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi228 – 2281A → W: Strongly reduces interaction with RALA. 1 Publication
Mutagenesisi233 – 2331K → W: Strongly reduces interaction with RALA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 716716Exocyst complex component 8PRO_0000227552Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151PhosphoserineBy similarity
Modified residuei313 – 3131PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO54924.
PRIDEiO54924.

PTM databases

iPTMnetiO54924.
PhosphoSiteiO54924.

Expressioni

Gene expression databases

GenevisibleiO54924. RN.

Interactioni

Subunit structurei

The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with the GTP-bound form of RALB via its PH domain (By similarity). Interacts with RALA via its PH domain.By similarity3 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026757.

Structurei

Secondary structure

1
716
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi174 – 18411Combined sources
Turni185 – 1873Combined sources
Beta strandi190 – 20920Combined sources
Beta strandi216 – 2238Combined sources
Turni224 – 2263Combined sources
Beta strandi228 – 2325Combined sources
Beta strandi238 – 2469Combined sources
Beta strandi249 – 2546Combined sources
Helixi258 – 27821Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZC3X-ray2.00B/D167-279[»]
1ZC4X-ray2.50B/D167-286[»]
ProteinModelPortaliO54924.
SMRiO54924. Positions 171-283.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO54924.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini173 – 273101PHPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi104 – 1096Poly-Ala

Sequence similaritiesi

Belongs to the EXO84 family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2215. Eukaryota.
ENOG410XT7U. LUCA.
GeneTreeiENSGT00390000015936.
HOGENOMiHOG000006737.
HOVERGENiHBG081489.
InParanoidiO54924.
KOiK19986.
OMAiRNFEQYT.
OrthoDBiEOG7NSB1Q.
PhylomeDBiO54924.
TreeFamiTF105819.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR016159. Cullin_repeat-like_dom.
IPR032403. Exo84_C.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF16528. Exo84_C. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF74788. SSF74788. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O54924-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSGASRLR RQLESGGFEA RLYVKQLSQQ SDGDRDLQEH RQRVQALAEE
60 70 80 90 100
TAQNLKRNVY QNYRQFIETA REISYLESEM YQLSHLLTEQ KSSLESIPLA
110 120 130 140 150
LLPAAAAGAS TGEDTAGAGP RERGAAQAGF LPGPAGVPRE GPGTGEEGKQ
160 170 180 190 200
RTLTTLLEKV EGCRDLLETP GQYLVYNGDL VEYEADHMAQ LQRVHGFLMN
210 220 230 240 250
DCLLVATWLP QRRGMYRYNA LYPLDRLAVV NVKDNPPMKD MFKLLMFPES
260 270 280 290 300
RIFQAENAKI KREWLEVLEE TKRALSDKRR REQEEAAALR APPPVTSKGS
310 320 330 340 350
NPFEDEAEEE LATPEAEEEK VDLSMEWIQE LPEDLDVCIA QRDFEGAVDL
360 370 380 390 400
LDKLNHYLED KPSPPSVKEL RAKVDERVRQ LTEVLVFELS PDRSLRGGPK
410 420 430 440 450
ATRRAVSQLI RLGQCTKACE LFLRNRAAAV HTAIRQLRIE GATLLYIHKL
460 470 480 490 500
CHVFFTSLLE TAREFETDFA GTDSGCYSAF VVWARSAMGM FVDAFSKQVF
510 520 530 540 550
DSKESLSTAA ECVKVAKEHC QQLGEIGLDL TFIIHALLVK DIQGALLSYK
560 570 580 590 600
EIIIEATKHR NSEEMWRRMN LMTPEALGKL KEEMRSCGVS NFEQYTGDDC
610 620 630 640 650
WVNLSYTVVA FTKQTMGFLE EALKLYFPEL HMVLLESLVE VILVAVQHVD
660 670 680 690 700
YSLRCEQDPE KKTFIRQNAS FLYDTVLPVV ERRFEEGVGK PAKQLQDLRN
710
ASRLLRVNPE STTSVV
Length:716
Mass (Da):81,043
Last modified:June 1, 1998 - v1
Checksum:iEE6945C7F25B18AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032669 mRNA. Translation: AAC01581.1.
PIRiT09222.
RefSeqiNP_620612.1. NM_139043.1.
UniGeneiRn.10901.

Genome annotation databases

EnsembliENSRNOT00000026757; ENSRNOP00000026757; ENSRNOG00000019766.
GeneIDi245709.
KEGGirno:245709.
UCSCiRGD:620245. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032669 mRNA. Translation: AAC01581.1.
PIRiT09222.
RefSeqiNP_620612.1. NM_139043.1.
UniGeneiRn.10901.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZC3X-ray2.00B/D167-279[»]
1ZC4X-ray2.50B/D167-286[»]
ProteinModelPortaliO54924.
SMRiO54924. Positions 171-283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026757.

PTM databases

iPTMnetiO54924.
PhosphoSiteiO54924.

Proteomic databases

PaxDbiO54924.
PRIDEiO54924.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026757; ENSRNOP00000026757; ENSRNOG00000019766.
GeneIDi245709.
KEGGirno:245709.
UCSCiRGD:620245. rat.

Organism-specific databases

CTDi149371.
RGDi620245. Exoc8.

Phylogenomic databases

eggNOGiKOG2215. Eukaryota.
ENOG410XT7U. LUCA.
GeneTreeiENSGT00390000015936.
HOGENOMiHOG000006737.
HOVERGENiHBG081489.
InParanoidiO54924.
KOiK19986.
OMAiRNFEQYT.
OrthoDBiEOG7NSB1Q.
PhylomeDBiO54924.
TreeFamiTF105819.

Enzyme and pathway databases

ReactomeiR-RNO-264876. Insulin processing.
R-RNO-5620916. VxPx cargo-targeting to cilium.

Miscellaneous databases

EvolutionaryTraceiO54924.
PROiO54924.

Gene expression databases

GenevisibleiO54924. RN.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR016159. Cullin_repeat-like_dom.
IPR032403. Exo84_C.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF16528. Exo84_C. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF74788. SSF74788. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBUNIT.
    Tissue: Brain.
  2. "Immunological characterization of exocyst complex subunits in cell differentiation."
    Wang S., Hsu S.C.
    Hybrid. Hybridomics 22:159-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase."
    Jin R., Junutula J.R., Matern H.T., Ervin K.E., Scheller R.H., Brunger A.T.
    EMBO J. 24:2064-2074(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 167-286 IN COMPLEX WITH RALA, MUTAGENESIS OF ALA-228 AND LYS-233.

Entry informationi

Entry nameiEXOC8_RAT
AccessioniPrimary (citable) accession number: O54924
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.