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Protein

Vacuolar protein sorting-associated protein 26A

Gene

Vps26a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3.The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC complex seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (By similarity). Required for retrograde transport of lysosomal enzyme receptor IGF2R (PubMed:15078902). Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Required for the endosomal localization of FAM21 (indicative for the WASH complex). Required for the endosomal localization of TBC1D5. Mediates retromer cargo reognition of SORL1 and is involved in trafficking of SORL1 implicated in sorting and processing of APP (By similarity). Involved in retromer-independent lysosomal sorting of F2R. Involved in recycling of ADRB2 (By similarity). Acts redundantly with VSP26B in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1. Enhances the affinity of SNX27 for PDZ-binding motifs in cargo proteins (PubMed:25136126).By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-3238698. WNT ligand biogenesis and trafficking.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protein sorting-associated protein 26A
Alternative name(s):
H<beta>58 protein
Short name:
H beta 58
Vesicle protein sorting 26A
Short name:
mVPS26
Gene namesi
Name:Vps26a
Synonyms:Vps26
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1353654. Vps26a.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • early endosome Source: UniProtKB
  • endosome Source: MGI
  • endosome membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • retromer complex Source: UniProtKB
  • tubular endosome Source: UniProtKB
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441D → A: Decreases interaction with SNX27. 1 Publication
Mutagenesisi154 – 1541L → A: Decreases interaction with SNX27. 1 Publication
Mutagenesisi235 – 2362IM → DN: Disrupts interaction with VPS35:VPS29 dimer; no endosomal localization.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Vacuolar protein sorting-associated protein 26APRO_0000073008Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei315 – 3151PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP40336.
MaxQBiP40336.
PaxDbiP40336.
PeptideAtlasiP40336.
PRIDEiP40336.

PTM databases

iPTMnetiP40336.
PhosphoSiteiP40336.

Expressioni

Gene expression databases

BgeeiP40336.
CleanExiMM_VPS26A.
GenevisibleiP40336. MM.

Interactioni

Subunit structurei

Component of the heterotrimeric retromer cargo-selective complex (CSC), also described as vacuolar protein sorting subcomplex (VPS), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35 (PubMed:18088321, PubMed:20875039). The CSC has a highly elongated structure with VPS26 and VPS29 binding independently at opposite distal ends of VPS35 as central platform (Probable). The CSC is believed to associate with variable sorting nexins to form functionally distinct retromer complex variants. The originally described retromer complex (also called SNX-BAR retromer) is a pentamer containing the CSC and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity. The CSC associates with SNX3 to form a SNX3-retromer complex. The CSC associates with SNX27, the WASH complex and the SNX-BAR subcomplex to form the SNX27-retromer complex (By similarity). Interacts with VPS29, VPS35, SNX27 (PubMed:18088321, PubMed:20875039, PubMed:25136126). Interacts with SNX1, SNX2, SNX5, SNX6, SNX3, RAB7A, ECM29, EHD1, KIAA0196, SORL1 (By similarity).1 PublicationBy similarity3 Publications

Protein-protein interaction databases

BioGridi206007. 3 interactions.
DIPiDIP-32041N.
IntActiP40336. 4 interactions.
MINTiMINT-1857150.
STRINGi10090.ENSMUSP00000090130.

Structurei

Secondary structure

1
327
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 2010Combined sources
Turni21 – 233Combined sources
Beta strandi26 – 305Combined sources
Beta strandi36 – 427Combined sources
Beta strandi48 – 5811Combined sources
Beta strandi63 – 7715Combined sources
Beta strandi79 – 835Combined sources
Beta strandi86 – 9611Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi105 – 1117Combined sources
Beta strandi127 – 13711Combined sources
Beta strandi143 – 1519Combined sources
Beta strandi154 – 1563Combined sources
Beta strandi164 – 1696Combined sources
Beta strandi171 – 18111Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi190 – 20213Combined sources
Beta strandi204 – 21613Combined sources
Beta strandi225 – 23814Combined sources
Beta strandi246 – 2516Combined sources
Helixi252 – 2543Combined sources
Beta strandi261 – 2644Combined sources
Turni265 – 2673Combined sources
Beta strandi268 – 28013Combined sources
Beta strandi285 – 29713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P2AX-ray2.70A9-327[»]
ProteinModelPortaliP40336.
SMRiP40336. Positions 9-300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the VPS26 family.Curated

Phylogenomic databases

eggNOGiKOG3063. Eukaryota.
ENOG410XSI1. LUCA.
GeneTreeiENSGT00390000002588.
HOGENOMiHOG000191799.
HOVERGENiHBG082914.
InParanoidiP40336.
KOiK18466.
OMAiGPWLGTR.
OrthoDBiEOG7NW699.
PhylomeDBiP40336.
TreeFamiTF300907.

Family and domain databases

InterProiIPR028934. Vps26-related.
[Graphical view]
PfamiPF03643. Vps26. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P40336-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSFLGGFFGP ICEIDVALND GETRKMAEMK TEDGKVEKHY LFYDGESVSG
60 70 80 90 100
KVNLAFKQPG KRLEHQGIRI EFVGQIELFN DKSNTHEFVN LVKELALPGE
110 120 130 140 150
LTQSRSYDFE FMQVEKPYES YIGANVRLRY FLKVTIVRRL TDLVKEYDLI
160 170 180 190 200
VHQLATYPDV NNSIKMEVGI EDCLHIEFEY NKSKYHLKDV IVGKIYFLLV
210 220 230 240 250
RIKIQHMELQ LIKKEITGIG PSTTTETETI AKYEIMDGAP VKGESIPIRL
260 270 280 290 300
FLAGYDPTPT MRDVNKKFSV RYFLNLVLVD EEDRRYFKQQ EIILWRKAPE
310 320
KLRKQRTNFH QRFESPDSQA SAEQPEM
Length:327
Mass (Da):38,114
Last modified:February 1, 1995 - v1
Checksum:i419DAED54264AC13
GO
Isoform 2 (identifier: P40336-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSEPLPAFLDRLWGPWLGTRSPPSRSSAASPSK

Note: No experimental confirmation available.
Show »
Length:359
Mass (Da):41,548
Checksum:iE09FDBE565B7E20B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371E → Q in BAC25745 (PubMed:16141072).Curated
Sequence conflicti71 – 711E → G in BAE35367 (PubMed:16141072).Curated
Sequence conflicti79 – 791F → L in BAE40171 (PubMed:16141072).Curated
Sequence conflicti188 – 1881K → R in BAE40415 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MSEPLPAFLDRLWGPWLGTR SPPSRSSAASPSK in isoform 2. 1 PublicationVSP_019926

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S41204 mRNA. Translation: AAB22718.1.
AK028096 mRNA. Translation: BAC25745.1.
AK150244 mRNA. Translation: BAE29408.1.
AK147989 mRNA. Translation: BAE28271.1.
AK151360 mRNA. Translation: BAE30335.1.
AK159783 mRNA. Translation: BAE35367.1.
AK167592 mRNA. Translation: BAE39650.1.
AK165853 mRNA. Translation: BAE38415.1.
AK168213 mRNA. Translation: BAE40171.1.
AK168537 mRNA. Translation: BAE40415.1.
BC007148 mRNA. Translation: AAH07148.1.
CCDSiCCDS35921.1. [P40336-1]
CCDS48579.1. [P40336-2]
PIRiA44882.
B44882.
RefSeqiNP_001106826.1. NM_001113355.1. [P40336-2]
NP_598433.1. NM_133672.3. [P40336-1]
UniGeneiMm.260703.
Mm.473468.

Genome annotation databases

EnsembliENSMUST00000092473; ENSMUSP00000090130; ENSMUSG00000020078. [P40336-2]
ENSMUST00000105447; ENSMUSP00000101087; ENSMUSG00000020078. [P40336-1]
GeneIDi30930.
KEGGimmu:30930.
UCSCiuc007fhf.2. mouse. [P40336-2]
uc007fhg.2. mouse. [P40336-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S41204 mRNA. Translation: AAB22718.1.
AK028096 mRNA. Translation: BAC25745.1.
AK150244 mRNA. Translation: BAE29408.1.
AK147989 mRNA. Translation: BAE28271.1.
AK151360 mRNA. Translation: BAE30335.1.
AK159783 mRNA. Translation: BAE35367.1.
AK167592 mRNA. Translation: BAE39650.1.
AK165853 mRNA. Translation: BAE38415.1.
AK168213 mRNA. Translation: BAE40171.1.
AK168537 mRNA. Translation: BAE40415.1.
BC007148 mRNA. Translation: AAH07148.1.
CCDSiCCDS35921.1. [P40336-1]
CCDS48579.1. [P40336-2]
PIRiA44882.
B44882.
RefSeqiNP_001106826.1. NM_001113355.1. [P40336-2]
NP_598433.1. NM_133672.3. [P40336-1]
UniGeneiMm.260703.
Mm.473468.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P2AX-ray2.70A9-327[»]
ProteinModelPortaliP40336.
SMRiP40336. Positions 9-300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206007. 3 interactions.
DIPiDIP-32041N.
IntActiP40336. 4 interactions.
MINTiMINT-1857150.
STRINGi10090.ENSMUSP00000090130.

PTM databases

iPTMnetiP40336.
PhosphoSiteiP40336.

Proteomic databases

EPDiP40336.
MaxQBiP40336.
PaxDbiP40336.
PeptideAtlasiP40336.
PRIDEiP40336.

Protocols and materials databases

DNASUi30930.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092473; ENSMUSP00000090130; ENSMUSG00000020078. [P40336-2]
ENSMUST00000105447; ENSMUSP00000101087; ENSMUSG00000020078. [P40336-1]
GeneIDi30930.
KEGGimmu:30930.
UCSCiuc007fhf.2. mouse. [P40336-2]
uc007fhg.2. mouse. [P40336-1]

Organism-specific databases

CTDi9559.
MGIiMGI:1353654. Vps26a.

Phylogenomic databases

eggNOGiKOG3063. Eukaryota.
ENOG410XSI1. LUCA.
GeneTreeiENSGT00390000002588.
HOGENOMiHOG000191799.
HOVERGENiHBG082914.
InParanoidiP40336.
KOiK18466.
OMAiGPWLGTR.
OrthoDBiEOG7NW699.
PhylomeDBiP40336.
TreeFamiTF300907.

Enzyme and pathway databases

ReactomeiR-MMU-3238698. WNT ligand biogenesis and trafficking.

Miscellaneous databases

PROiP40336.
SOURCEiSearch...

Gene expression databases

BgeeiP40336.
CleanExiMM_VPS26A.
GenevisibleiP40336. MM.

Family and domain databases

InterProiIPR028934. Vps26-related.
[Graphical view]
PfamiPF03643. Vps26. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a novel, evolutionarily conserved gene disrupted by the murine H beta 58 embryonic lethal transgene insertion."
    Lee J.J., Radice G., Perkins C.P., Costantini F.
    Development 115:277-288(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J and DBA/2.
    Tissue: Amnion, Bone marrow, Lung, Placenta and Testis.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Mammary tumor.
  4. "Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer."
    Seaman M.N.J.
    J. Cell Biol. 165:111-122(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Structure of Vps26B and mapping of its interaction with the retromer protein complex."
    Collins B.M., Norwood S.J., Kerr M.C., Mahony D., Seaman M.N., Teasdale R.D., Owen D.J.
    Traffic 9:366-379(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, MUTAGENESIS OF 235-ILE-MET-236, SUBCELLULAR LOCATION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "Assembly and solution structure of the core retromer protein complex."
    Norwood S.J., Shaw D.J., Cowieson N.P., Owen D.J., Teasdale R.D., Collins B.M.
    Traffic 12:56-71(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "Vps26A and Vps26B subunits define distinct retromer complexes."
    Bugarcic A., Zhe Y., Kerr M.C., Griffin J., Collins B.M., Teasdale R.D.
    Traffic 12:1759-1773(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer."
    Gallon M., Clairfeuille T., Steinberg F., Mas C., Ghai R., Sessions R.B., Teasdale R.D., Collins B.M., Cullen P.J.
    Proc. Natl. Acad. Sci. U.S.A. 111:E3604-E3613(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 9-327, FUNCTION, INTERACTION WITH SNX27, MUTAGENESIS OF ASP-44 AND LEU-154.

Entry informationi

Entry nameiVP26A_MOUSE
AccessioniPrimary (citable) accession number: P40336
Secondary accession number(s): Q3TGY3
, Q3THM5, Q3TW99, Q3UD54, Q8C1E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 132 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.