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Protein

Exocyst complex component 2

Gene

Exoc2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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

Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Exocyst complex component 2
Alternative name(s):
Exocyst complex component Sec5
Short name:
rSec5
Gene namesi
Name:Exoc2
Synonyms:Sec5, Sec5l1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619961. Exoc2.

Subcellular locationi

GO - Cellular componenti

  • exocyst Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 924924Exocyst complex component 2PRO_0000118920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei454 – 4541N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO54921.
PRIDEiO54921.

PTM databases

iPTMnetiO54921.
PhosphoSiteiO54921.

Interactioni

Subunit structurei

The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with EXOC3L1 (By similarity). Interacts with RALA and GNEFR/DELGEF. Interaction with GNEFR occurs only in the presence of magnesium or manganese and is stimulated by dCTP or GTP.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RALAP112332EBI-1036795,EBI-1036803From a different organism.

Protein-protein interaction databases

IntActiO54921. 6 interactions.
MINTiMINT-4996218.
STRINGi10116.ENSRNOP00000050367.

Structurei

Secondary structure

1
924
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 1911Combined sources
Beta strandi23 – 297Combined sources
Helixi35 – 373Combined sources
Beta strandi38 – 436Combined sources
Helixi49 – 513Combined sources
Beta strandi53 – 564Combined sources
Beta strandi59 – 635Combined sources
Beta strandi68 – 714Combined sources
Beta strandi74 – 785Combined sources
Turni79 – 813Combined sources
Beta strandi85 – 884Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UADX-ray2.10C/D1-99[»]
ProteinModelPortaliO54921.
SMRiO54921. Positions 4-95.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO54921.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 9386IPT/TIGAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili240 – 26021Sequence analysisAdd
BLAST

Domaini

Interacts with RALA through the TIG domain.

Sequence similaritiesi

Belongs to the SEC5 family.Curated
Contains 1 IPT/TIG domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2347. Eukaryota.
ENOG410XSY3. LUCA.
HOGENOMiHOG000044231.
HOVERGENiHBG028469.
InParanoidiO54921.
KOiK17637.
PhylomeDBiO54921.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR029175. EXOC2/Sec5.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
[Graphical view]
PANTHERiPTHR13043. PTHR13043. 1 hit.
PfamiPF01833. TIG. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

O54921-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRSRQPPLV TGISPNEGIP WTKVTIRGEN LGTGPTDLIG LTICGHNCLL
60 70 80 90 100
TAEWMSASKI VCRVGQAKND KGDIIVTTKS GGRGTSTVSF KLLKPEKIGI
110 120 130 140 150
LDQSAVWVDE MNYYDMRTDR NKGIPPLSLR PANPLGIEIE KCKLPQKNLE
160 170 180 190 200
VLFHGMSADF TSENFSAAWY LIENHSNTSF EQLKMAVTNL KRQANKKSEG
210 220 230 240 250
SLAYVKGGLS TFFEAQDALS AIHQKLEADG TEKVEGSMTQ KLENVLNRAS
260 270 280 290 300
NTADTLFQEV LGRKDKADST RNALNVLQRF KFLFNLPLNI KRNIQKGDYD
310 320 330 340 350
VVINDYEKAK SLFGKTEVQV FKKYYAEVEA GIEDLRELLL KKLLETPSTL
360 370 380 390 400
HDQKRYIRYL SDLHAPGDPA WQCIGAQHKW TLKLMQDCKE GHMKSLKGNP
410 420 430 440 450
GPHSPMLDLD NDARPSVLGH LSQTASLKRG SSFQSGRDDT WRYKTPHRVA
460 470 480 490 500
FVEKLTKLVL SQLPNFWKLW ISYVNGSLFS ETAEKSGQIE RSKNVRQRQN
510 520 530 540 550
DFKKMIQEVM HSLVKLIRGA LLPFSLREGD GRQYGGWEVQ AELSGQWLAH
560 570 580 590 600
VIQTIRLTYE SLTALEIPND MLQIIQDLIL DLRIHCIMVT LQHTAEEIKR
610 620 630 640 650
LAEKEDWIVD NEGLTSLPCQ FEQSIVHSLQ SLKGVVDCKP GEASVFQQPK
660 670 680 690 700
TQEEVCQLCI SIMQVFIYCL EQLSTKPDAD IDTTHLSVDV SSPDLFGSIH
710 720 730 740 750
EDFGLTSEQR LLIVLSNCCY LERHTFLNIA EHFEKHNFQG IEKITQVSMA
760 770 780 790 800
SLKELDQRLF ENYIELKADP IVGSLETGIY AGYFDWKDCL PPAGVRNYLK
810 820 830 840 850
EALVNIIAVH AEVFTISKEL VPRVLARVIE AVSEELSRLM QCVSSFSRNG
860 870 880 890 900
ALQARLEICA LRDTVAIYLT PESRSSFKQA LEALPQLASG ADKKLLEELL
910 920
NKFKSSMHLQ LTCFQAASPT VMKT
Length:924
Mass (Da):104,031
Last modified:June 1, 1998 - v1
Checksum:i1903C0593B113373
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032666 mRNA. Translation: AAC01578.1.
PIRiT09220.
RefSeqiNP_599241.2. NM_134414.2.
UniGeneiRn.2869.

Genome annotation databases

GeneIDi171455.
KEGGirno:171455.
UCSCiRGD:619961. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032666 mRNA. Translation: AAC01578.1.
PIRiT09220.
RefSeqiNP_599241.2. NM_134414.2.
UniGeneiRn.2869.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UADX-ray2.10C/D1-99[»]
ProteinModelPortaliO54921.
SMRiO54921. Positions 4-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO54921. 6 interactions.
MINTiMINT-4996218.
STRINGi10116.ENSRNOP00000050367.

PTM databases

iPTMnetiO54921.
PhosphoSiteiO54921.

Proteomic databases

PaxDbiO54921.
PRIDEiO54921.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi171455.
KEGGirno:171455.
UCSCiRGD:619961. rat.

Organism-specific databases

CTDi55770.
RGDi619961. Exoc2.

Phylogenomic databases

eggNOGiKOG2347. Eukaryota.
ENOG410XSY3. LUCA.
HOGENOMiHOG000044231.
HOVERGENiHBG028469.
InParanoidiO54921.
KOiK17637.
PhylomeDBiO54921.

Miscellaneous databases

EvolutionaryTraceiO54921.
NextBioi622397.
PROiO54921.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR029175. EXOC2/Sec5.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
[Graphical view]
PANTHERiPTHR13043. PTHR13043. 1 hit.
PfamiPF01833. TIG. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The exocyst complex binds the small GTPase RalA to mediate filopodia formation."
    Sugihara K., Asano S., Tanaka K., Iwamatsu A., Okawa K., Ohta Y.
    Nat. Cell Biol. 4:73-78(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RALA.
  3. "Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex."
    Fukai S., Matern H.T., Jagath J.R., Scheller R.H., Brunger A.T.
    EMBO J. 22:3267-3278(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-99 IN COMPLEX WITH RALA.

Entry informationi

Entry nameiEXOC2_RAT
AccessioniPrimary (citable) accession number: O54921
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 121 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, 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.