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Protein

Vacuolar protein sorting-associated protein 22 homolog 1

Gene

VP22-1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-ATH-917729. Endosomal Sorting Complex Required For Transport (ESCRT).

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protein sorting-associated protein 22 homolog 1
Short name:
AtVPS22-1
Alternative name(s):
ESCRT-II complex subunit VPS22 homolog 1
Gene namesi
Name:VP22-1
Ordered Locus Names:At4g27040
ORF Names:F10M23.380
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G27040.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 250250Vacuolar protein sorting-associated protein 22 homolog 1PRO_0000368191Add
BLAST

Proteomic databases

PaxDbiQ5M759.
PRIDEiQ5M759.

Expressioni

Gene expression databases

GenevisibleiQ5M759. AT.

Interactioni

Subunit structurei

Component of the endosomal sorting complex required for transport II (ESCRT-II), composed of VPS22, VPS25 and VPS36.By similarity

Protein-protein interaction databases

BioGridi14099. 6 interactions.
IntActiQ5M759. 5 interactions.
STRINGi3702.AT4G27040.1.

Structurei

3D structure databases

ProteinModelPortaliQ5M759.
SMRiQ5M759. Positions 35-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili35 – 5521Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 164Poly-Ala

Sequence similaritiesi

Belongs to the SNF8 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3341. Eukaryota.
ENOG410XPVM. LUCA.
HOGENOMiHOG000170930.
InParanoidiQ5M759.
KOiK12188.
OMAiWFPSLFP.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR007286. EAP30.
IPR016689. ESCRT-2_cplx_Snf8.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12806. PTHR12806. 1 hit.
PfamiPF04157. EAP30. 1 hit.
[Graphical view]
PIRSFiPIRSF017215. ESCRT2_Vps22. 1 hit.
SUPFAMiSSF46785. SSF46785. 2 hits.

Sequencei

Sequence statusi: Complete.

Q5M759-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRRPGIGGL QKAAAARDQY RLLGENVAKL RTDMMKEQLS TFRSQLEEFA
60 70 80 90 100
RKHKNDIRKN PAFRAQFHEM CANIGVDPLA SNKGFWAELL GIGDFYYELG
110 120 130 140 150
VQIIEVCMLT RSHNGGLISL QELCNHLRQR RKKDREAVTE DDCLRAISKL
160 170 180 190 200
KVLGSGFEVI TIGKKKLVRS VPTELNKDHN QILELAQGQG FVIVEEVQRR
210 220 230 240 250
LSWTSGRVID ALETLLEEGL AMIDNGHKDG KCRYWFPCVS SVYSSIGSDT
Length:250
Mass (Da):28,310
Last modified:May 3, 2011 - v2
Checksum:i0BED008163F0C744
GO

Sequence cautioni

The sequence CAB36550.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB79559.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171R → G in AAV91335 (Ref. 4) Curated
Sequence conflicti17 – 171R → G in AAW70398 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035440 Genomic DNA. Translation: CAB36550.1. Sequence problems.
AL161566 Genomic DNA. Translation: CAB79559.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85287.1.
CP002687 Genomic DNA. Translation: AEE85288.1.
CP002687 Genomic DNA. Translation: AEE85289.1.
CP002687 Genomic DNA. Translation: AEE85290.1.
AY299265 mRNA. No translation available.
BT020389 mRNA. Translation: AAV91335.1.
BT020552 mRNA. Translation: AAW70398.1.
PIRiT04827.
RefSeqiNP_001119065.1. NM_001125593.1.
NP_001119066.1. NM_001125594.1.
NP_001119067.1. NM_001125595.1.
NP_194434.2. NM_118838.4.
UniGeneiAt.48906.
At.68943.
At.68944.
At.68945.

Genome annotation databases

EnsemblPlantsiAT4G27040.1; AT4G27040.1; AT4G27040.
AT4G27040.2; AT4G27040.2; AT4G27040.
AT4G27040.3; AT4G27040.3; AT4G27040.
AT4G27040.4; AT4G27040.4; AT4G27040.
GeneIDi828812.
GrameneiAT4G27040.1; AT4G27040.1; AT4G27040.
AT4G27040.2; AT4G27040.2; AT4G27040.
AT4G27040.3; AT4G27040.3; AT4G27040.
AT4G27040.4; AT4G27040.4; AT4G27040.
KEGGiath:AT4G27040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035440 Genomic DNA. Translation: CAB36550.1. Sequence problems.
AL161566 Genomic DNA. Translation: CAB79559.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85287.1.
CP002687 Genomic DNA. Translation: AEE85288.1.
CP002687 Genomic DNA. Translation: AEE85289.1.
CP002687 Genomic DNA. Translation: AEE85290.1.
AY299265 mRNA. No translation available.
BT020389 mRNA. Translation: AAV91335.1.
BT020552 mRNA. Translation: AAW70398.1.
PIRiT04827.
RefSeqiNP_001119065.1. NM_001125593.1.
NP_001119066.1. NM_001125594.1.
NP_001119067.1. NM_001125595.1.
NP_194434.2. NM_118838.4.
UniGeneiAt.48906.
At.68943.
At.68944.
At.68945.

3D structure databases

ProteinModelPortaliQ5M759.
SMRiQ5M759. Positions 35-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14099. 6 interactions.
IntActiQ5M759. 5 interactions.
STRINGi3702.AT4G27040.1.

Proteomic databases

PaxDbiQ5M759.
PRIDEiQ5M759.

Protocols and materials databases

DNASUi828812.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G27040.1; AT4G27040.1; AT4G27040.
AT4G27040.2; AT4G27040.2; AT4G27040.
AT4G27040.3; AT4G27040.3; AT4G27040.
AT4G27040.4; AT4G27040.4; AT4G27040.
GeneIDi828812.
GrameneiAT4G27040.1; AT4G27040.1; AT4G27040.
AT4G27040.2; AT4G27040.2; AT4G27040.
AT4G27040.3; AT4G27040.3; AT4G27040.
AT4G27040.4; AT4G27040.4; AT4G27040.
KEGGiath:AT4G27040.

Organism-specific databases

TAIRiAT4G27040.

Phylogenomic databases

eggNOGiKOG3341. Eukaryota.
ENOG410XPVM. LUCA.
HOGENOMiHOG000170930.
InParanoidiQ5M759.
KOiK12188.
OMAiWFPSLFP.

Enzyme and pathway databases

ReactomeiR-ATH-917729. Endosomal Sorting Complex Required For Transport (ESCRT).

Miscellaneous databases

PROiQ5M759.

Gene expression databases

GenevisibleiQ5M759. AT.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR007286. EAP30.
IPR016689. ESCRT-2_cplx_Snf8.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12806. PTHR12806. 1 hit.
PfamiPF04157. EAP30. 1 hit.
[Graphical view]
PIRSFiPIRSF017215. ESCRT2_Vps22. 1 hit.
SUPFAMiSSF46785. SSF46785. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Whole genome shotgun sequencing of Brassica oleracea and its application to gene discovery and annotation in Arabidopsis."
    Ayele M., Haas B.J., Kumar N., Wu H., Xiao Y., Van Aken S., Utterback T.R., Wortman J.R., White O.R., Town C.D.
    Genome Res. 15:487-495(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Arabidopsis ORF clones."
    Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. Cited for: IDENTIFICATION, NOMENCLATURE.
  6. "Exploring the ESCRTing machinery in eukaryotes."
    Winter V., Hauser M.-T.
    Trends Plant Sci. 11:115-123(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiVP221_ARATH
AccessioniPrimary (citable) accession number: Q5M759
Secondary accession number(s): Q9SZ43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 3, 2011
Last modified: February 17, 2016
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.