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Protein

Exocyst complex component 5

Gene

Exoc5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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.By similarity

GO - Molecular functioni

  1. protein N-terminus binding Source: UniProtKB
  2. Ral GTPase binding Source: MGI

GO - Biological processi

  1. exocytosis Source: UniProtKB-KW
  2. protein transport Source: UniProtKB-KW
  3. vesicle docking Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_298481. Insulin processing.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_315493. VxPx cargo-targeting to cilium.

Names & Taxonomyi

Protein namesi
Recommended name:
Exocyst complex component 5
Alternative name(s):
Exocyst complex component Sec10
Gene namesi
Name:Exoc5
Synonyms:Sec10l1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:2145645. Exoc5.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 708707Exocyst complex component 5PRO_0000118944Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei122 – 1221PhosphothreonineBy similarity
Modified residuei395 – 3951PhosphothreonineBy similarity
Modified residuei405 – 4051PhosphothreonineBy similarity
Modified residuei412 – 4121PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ3TPX4.
PaxDbiQ3TPX4.
PRIDEiQ3TPX4.

PTM databases

PhosphoSiteiQ3TPX4.

Expressioni

Gene expression databases

BgeeiQ3TPX4.
CleanExiMM_EXOC5.
ExpressionAtlasiQ3TPX4. baseline and differential.
GenevestigatoriQ3TPX4.

Interactioni

Subunit structurei

The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with EXOC3L1.By similarity1 Publication

Protein-protein interaction databases

BioGridi222868. 1 interaction.
IntActiQ3TPX4. 2 interactions.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili40 – 10162Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the SEC10 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG261139.
GeneTreeiENSGT00390000012837.
HOGENOMiHOG000007911.
HOVERGENiHBG055591.
InParanoidiQ3TPX4.
OMAiPYTEGQR.
OrthoDBiEOG7SJD3Z.
PhylomeDBiQ3TPX4.
TreeFamiTF314966.

Family and domain databases

InterProiIPR009976. Sec10-like.
[Graphical view]
PANTHERiPTHR12100. PTHR12100. 1 hit.
PfamiPF07393. Sec10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3TPX4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATTAELFEE PFVADEYIER LVWRTPGGGS RGGPEAFDPK RLLEEFVNHI
60 70 80 90 100
QELQIMDERI QRKVEKLEQQ CQKEAKEFAK KVQELQKSNQ VAFQHFQELD
110 120 130 140 150
EHISYVATKV CHLGDQLEGV NTPRQRAVEA QKLMKYFNEF LDGELKSDVF
160 170 180 190 200
TNSEKIKEAA DVIQKLHLIA QELPFDRFSE VKSKIASKYH DLECQLIQEF
210 220 230 240 250
TSAQRRGEVS RMREVAAVLL HFKGYSHCID VYIKQCQEGA YLRNDIFEDA
260 270 280 290 300
AILCQRVNKQ VGDIFSNPEA VLAKLIQSVF EIKLQSFVKD QLEECRKSDA
310 320 330 340 350
EQYLKSLYDL YTRTTGLSSK LMEFNLGTDK QTFLSKLIKS IFISYLENYI
360 370 380 390 400
EVEIGYLKSR SAMILQRYYD SKNHQKRSIG TGGIQDLKER IRQRTNLPLG
410 420 430 440 450
PSIDTHGETF LSQEVVVNLL QETKQAFERC HRLSDPSDLP RNAFRIFTIL
460 470 480 490 500
VEFLCIEHID YALETGLAGI PSSDSRNANL YFLDVVQQAN TIFHLFDKQF
510 520 530 540 550
NDHLMPLISS SPKLSECLQK KKEIIEQMEM KLDTGIDRTL NCMIGQMKHI
560 570 580 590 600
LAAEQKKTDF KPEDENNVLI QYTNACVKVC VYVRKQVEKI KNSMDGKNVD
610 620 630 640 650
TVLMELGVRF HRLIYEHLQQ YSYSCMGGML AICDVAEYRK CAKDFKIPMV
660 670 680 690 700
LHLFDTLHAL CNLLVVAPDN LKQVCSGEQL ANLDKNILHS FVQLRADYRS

ARLARHFS
Length:708
Mass (Da):81,738
Last modified:July 27, 2011 - v2
Checksum:i257374EE3EA58356
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti628 – 6281G → D in BAE37611 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK164067 mRNA. Translation: BAE37611.1.
AK157473 mRNA. Translation: BAE34093.1.
AK167145 mRNA. Translation: BAE39290.1.
AK171012 mRNA. Translation: BAE42183.1.
CH466605 Genomic DNA. Translation: EDL20783.1.
BC049967 mRNA. Translation: AAH49967.1.
CCDSiCCDS49474.1.
RefSeqiNP_997097.1. NM_207214.3.
UniGeneiMm.31607.

Genome annotation databases

EnsembliENSMUST00000162175; ENSMUSP00000125434; ENSMUSG00000061244.
GeneIDi105504.
KEGGimmu:105504.
UCSCiuc007tjv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK164067 mRNA. Translation: BAE37611.1.
AK157473 mRNA. Translation: BAE34093.1.
AK167145 mRNA. Translation: BAE39290.1.
AK171012 mRNA. Translation: BAE42183.1.
CH466605 Genomic DNA. Translation: EDL20783.1.
BC049967 mRNA. Translation: AAH49967.1.
CCDSiCCDS49474.1.
RefSeqiNP_997097.1. NM_207214.3.
UniGeneiMm.31607.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222868. 1 interaction.
IntActiQ3TPX4. 2 interactions.

PTM databases

PhosphoSiteiQ3TPX4.

Proteomic databases

MaxQBiQ3TPX4.
PaxDbiQ3TPX4.
PRIDEiQ3TPX4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000162175; ENSMUSP00000125434; ENSMUSG00000061244.
GeneIDi105504.
KEGGimmu:105504.
UCSCiuc007tjv.2. mouse.

Organism-specific databases

CTDi10640.
MGIiMGI:2145645. Exoc5.

Phylogenomic databases

eggNOGiNOG261139.
GeneTreeiENSGT00390000012837.
HOGENOMiHOG000007911.
HOVERGENiHBG055591.
InParanoidiQ3TPX4.
OMAiPYTEGQR.
OrthoDBiEOG7SJD3Z.
PhylomeDBiQ3TPX4.
TreeFamiTF314966.

Enzyme and pathway databases

ReactomeiREACT_298481. Insulin processing.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_315493. VxPx cargo-targeting to cilium.

Miscellaneous databases

ChiTaRSiExoc5. mouse.
NextBioi357738.
PROiQ3TPX4.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TPX4.
CleanExiMM_EXOC5.
ExpressionAtlasiQ3TPX4. baseline and differential.
GenevestigatoriQ3TPX4.

Family and domain databases

InterProiIPR009976. Sec10-like.
[Graphical view]
PANTHERiPTHR12100. PTHR12100. 1 hit.
PfamiPF07393. Sec10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Spleen.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "Involvement of Exoc3l, a protein structurally related to the exocyst subunit Sec6, in insulin secretion."
    Saito T., Shibasaki T., Seino S.
    Biomed. Res. 29:85-91(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EXOC3L1.

Entry informationi

Entry nameiEXOC5_MOUSE
AccessioniPrimary (citable) accession number: Q3TPX4
Secondary accession number(s): Q80VK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.