VP26A_HUMAN
ID VP26A_HUMAN Reviewed; 327 AA.
AC O75436; A8MZ56; B2RDD3; Q8TBH4; Q9H982;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Vacuolar protein sorting-associated protein 26A;
DE AltName: Full=Vesicle protein sorting 26A;
DE Short=hVPS26;
GN Name=VPS26A {ECO:0000303|PubMed:30213940, ECO:0000312|HGNC:HGNC:12711};
GN Synonyms=VPS26;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH VPS29; VPS35; SNX1
RP AND SNX2, AND SUBUNIT.
RC TISSUE=Colon;
RX PubMed=11102511; DOI=10.1091/mbc.11.12.4105;
RA Renfrew Haft C., de la Luz Sierra M., Bafford R., Lesniak M.A., Barr V.A.,
RA Taylor S.I.;
RT "Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and
RT 35: assembly into multimeric complexes.";
RL Mol. Biol. Cell 11:4105-4116(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 3-249 (ISOFORM 2).
RC TISSUE=Brain, and Embryonic testis carcinoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION.
RX PubMed=15078902; DOI=10.1083/jcb.200312034;
RA Seaman M.N.J.;
RT "Cargo-selective endosomal sorting for retrieval to the Golgi requires
RT retromer.";
RL J. Cell Biol. 165:111-122(2004).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15078903; DOI=10.1083/jcb.200312055;
RA Arighi C.N., Hartnell L.M., Aguilar R.C., Haft C.R., Bonifacino J.S.;
RT "Role of the mammalian retromer in sorting of the cation-independent
RT mannose 6-phosphate receptor.";
RL J. Cell Biol. 165:123-133(2004).
RN [9]
RP FUNCTION.
RX PubMed=15247922; DOI=10.1038/ncb1153;
RA Verges M., Luton F., Gruber C., Tiemann F., Reinders L.G., Huang L.,
RA Burlingame A.L., Haft C.R., Mostov K.E.;
RT "The mammalian retromer regulates transcytosis of the polymeric
RT immunoglobulin receptor.";
RL Nat. Cell Biol. 6:763-769(2004).
RN [10]
RP INDUCTION.
RX PubMed=16315276; DOI=10.1002/ana.20667;
RA Small S.A., Kent K., Pierce A., Leung C., Kang M.S., Okada H., Honig L.,
RA Vonsattel J.-P., Kim T.-W.;
RT "Model-guided microarray implicates the retromer complex in Alzheimer's
RT disease.";
RL Ann. Neurol. 58:909-919(2005).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH VPS35.
RX PubMed=16190980; DOI=10.1111/j.1600-0854.2005.00328.x;
RA Kerr M.C., Bennetts J.S., Simpson F., Thomas E.C., Flegg C., Gleeson P.A.,
RA Wicking C., Teasdale R.D.;
RT "A novel mammalian retromer component, Vps26B.";
RL Traffic 6:991-1001(2005).
RN [12]
RP FUNCTION.
RX PubMed=16407403; DOI=10.1091/mbc.e05-09-0899;
RA Gullapalli A., Wolfe B.L., Griffin C.T., Magnuson T., Trejo J.;
RT "An essential role for SNX1 in lysosomal sorting of protease-activated
RT receptor-1: evidence for retromer-, Hrs-, and Tsg101-independent functions
RT of sorting nexins.";
RL Mol. Biol. Cell 17:1228-1238(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP INDUCTION.
RX PubMed=16784798; DOI=10.1016/j.neurobiolaging.2006.05.009;
RA Riemenschneider M., Schoepfer-Wendels A., Friedrich P., Konta L.,
RA Laws S.M., Mueller J.C., Kurz A., Forstl H.;
RT "No association of vacuolar protein sorting 26 polymorphisms with
RT Alzheimer's disease.";
RL Neurobiol. Aging 28:883-884(2007).
RN [15]
RP INTERACTION WITH EHD1.
RX PubMed=17868075; DOI=10.1111/j.1600-0854.2007.00652.x;
RA Gokool S., Tattersall D., Seaman M.N.;
RT "EHD1 interacts with retromer to stabilize SNX1 tubules and facilitate
RT endosome-to-Golgi retrieval.";
RL Traffic 8:1873-1886(2007).
RN [16]
RP INTERACTION WITH SNX1; SNX2; SNX5 AND SNX6.
RX PubMed=19619496; DOI=10.1016/j.devcel.2009.04.016;
RA Wassmer T., Attar N., Harterink M., van Weering J.R., Traer C.J.,
RA Oakley J., Goud B., Stephens D.J., Verkade P., Korswagen H.C., Cullen P.J.;
RT "The retromer coat complex coordinates endosomal sorting and dynein-
RT mediated transport, with carrier recognition by the trans-Golgi network.";
RL Dev. Cell 17:110-122(2009).
RN [17]
RP INTERACTION WITH RAB7A.
RX PubMed=19531583; DOI=10.1242/jcs.048686;
RA Seaman M.N., Harbour M.E., Tattersall D., Read E., Bright N.;
RT "Membrane recruitment of the cargo-selective retromer subcomplex is
RT catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5.";
RL J. Cell Sci. 122:2371-2382(2009).
RN [18]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ECPAS.
RX PubMed=20682791; DOI=10.1074/jbc.m110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E.,
RA Rechsteiner M.;
RT "A protein interaction network for Ecm29 links the 26 S proteasome to
RT molecular motors and endosomal components.";
RL J. Biol. Chem. 285:31616-31633(2010).
RN [19]
RP FUNCTION, AND INTERACTION WITH WASHC5.
RX PubMed=20923837; DOI=10.1242/jcs.071472;
RA Harbour M.E., Breusegem S.Y., Antrobus R., Freeman C., Reid E.,
RA Seaman M.N.;
RT "The cargo-selective retromer complex is a recruiting hub for protein
RT complexes that regulate endosomal tubule dynamics.";
RL J. Cell Sci. 123:3703-3717(2010).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP FUNCTION.
RX PubMed=21602791; DOI=10.1038/ncb2252;
RA Temkin P., Lauffer B., Jager S., Cimermancic P., Krogan N.J.,
RA von Zastrow M.;
RT "SNX27 mediates retromer tubule entry and endosome-to-plasma membrane
RT trafficking of signalling receptors.";
RL Nat. Cell Biol. 13:715-721(2011).
RN [23]
RP INTERACTION WITH SNX3, AND FUNCTION OF THE SNX3-RETROMER.
RX PubMed=21725319; DOI=10.1038/ncb2281;
RA Harterink M., Port F., Lorenowicz M.J., McGough I.J., Silhankova M.,
RA Betist M.C., van Weering J.R., van Heesbeen R.G., Middelkoop T.C.,
RA Basler K., Cullen P.J., Korswagen H.C.;
RT "A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt
RT sorting receptor Wntless and is required for Wnt secretion.";
RL Nat. Cell Biol. 13:914-923(2011).
RN [24]
RP FUNCTION.
RX PubMed=22070227; DOI=10.1042/bj20111761;
RA Harbour M.E., Breusegem S.Y., Seaman M.N.;
RT "Recruitment of the endosomal WASH complex is mediated by the extended
RT 'tail' of Fam21 binding to the retromer protein Vps35.";
RL Biochem. J. 442:209-220(2012).
RN [25]
RP FUNCTION, AND INTERACTION WITH SORL1.
RX PubMed=22279231; DOI=10.1523/jneurosci.2272-11.2012;
RA Fjorback A.W., Seaman M., Gustafsen C., Mehmedbasic A., Gokool S., Wu C.,
RA Militz D., Schmidt V., Madsen P., Nyengaard J.R., Willnow T.E.,
RA Christensen E.I., Mobley W.B., Nykjaer A., Andersen O.M.;
RT "Retromer binds the FANSHY sorting motif in SorLA to regulate amyloid
RT precursor protein sorting and processing.";
RL J. Neurosci. 32:1467-1480(2012).
RN [26]
RP SUBCELLULAR LOCATION.
RX PubMed=22431521; DOI=10.1128/mcb.06726-11;
RA Mamo A., Jules F., Dumaresq-Doiron K., Costantino S., Lefrancois S.;
RT "The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal
RT sorting.";
RL Mol. Cell. Biol. 32:1855-1866(2012).
RN [27]
RP INTERACTION WITH SNX27, AND FUNCTION OF THE SNX27-RETROMER.
RX PubMed=23563491; DOI=10.1038/ncb2721;
RA Steinberg F., Gallon M., Winfield M., Thomas E.C., Bell A.J., Heesom K.J.,
RA Tavare J.M., Cullen P.J.;
RT "A global analysis of SNX27-retromer assembly and cargo specificity reveals
RT a function in glucose and metal ion transport.";
RL Nat. Cell Biol. 15:461-471(2013).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [29]
RP INTERACTION WITH RAB7A.
RX PubMed=24344282; DOI=10.1073/pnas.1316482111;
RA Harrison M.S., Hung C.S., Liu T.T., Christiano R., Walther T.C., Burd C.G.;
RT "A mechanism for retromer endosomal coat complex assembly with cargo.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:267-272(2014).
RN [30]
RP INTERACTION WITH VPS35.
RX PubMed=28892079; DOI=10.1038/ncb3610;
RA McNally K.E., Faulkner R., Steinberg F., Gallon M., Ghai R., Pim D.,
RA Langton P., Pearson N., Danson C.M., Naegele H., Morris L.L., Singla A.,
RA Overlee B.L., Heesom K.J., Sessions R., Banks L., Collins B.M., Berger I.,
RA Billadeau D.D., Burstein E., Cullen P.J.;
RT "Retriever is a multiprotein complex for retromer-independent endosomal
RT cargo recycling.";
RL Nat. Cell Biol. 19:1214-1225(2017).
RN [31]
RP INTERACTION WITH SNX3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=30213940; DOI=10.1038/s41467-018-06114-3;
RA McGough I.J., de Groot R.E.A., Jellett A.P., Betist M.C., Varandas K.C.,
RA Danson C.M., Heesom K.J., Korswagen H.C., Cullen P.J.;
RT "SNX3-retromer requires an evolutionary conserved MON2:DOPEY2:ATP9A complex
RT to mediate Wntless sorting and Wnt secretion.";
RL Nat. Commun. 9:3737-3737(2018).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBCELLULAR LOCATION, INTERACTION
RP WITH VPS35, AND MUTAGENESIS OF 236-ILE-MET-237.
RX PubMed=16732284; DOI=10.1038/nsmb1103;
RA Shi H., Rojas R., Bonifacino J.S., Hurley J.H.;
RT "The retromer subunit Vps26 has an arrestin fold and binds Vps35 through
RT its C-terminal domain.";
RL Nat. Struct. Mol. Biol. 13:540-548(2006).
CC -!- FUNCTION: Acts as component of the retromer cargo-selective complex
CC (CSC). The CSC is believed to be the core functional component of
CC retromer or respective retromer complex variants acting to prevent
CC missorting of selected transmembrane cargo proteins into the lysosomal
CC degradation pathway. The recruitment of the CSC to the endosomal
CC membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates
CC retrograde transport of cargo proteins from endosomes to the trans-
CC Golgi network (TGN) and is involved in endosome-to-plasma membrane
CC transport for cargo protein recycling. The SNX3-retromer mediates the
CC retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR
CC retromer pathway. The SNX27-retromer is believed to be involved in
CC endosome-to-plasma membrane trafficking and recycling of a broad
CC spectrum of cargo proteins (Probable). The CSC seems to act as
CC recruitment hub for other proteins, such as the WASH complex and TBC1D5
CC (Probable). Required for retrograde transport of lysosomal enzyme
CC receptor IGF2R (PubMed:15078902, PubMed:15078903). Required to regulate
CC transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA)
CC (PubMed:15247922). Required for the endosomal localization of WASHC2A
CC (indicative for the WASH complex) (PubMed:22070227). Required for the
CC endosomal localization of TBC1D5 (PubMed:20923837). Mediates retromer
CC cargo recognition of SORL1 and is involved in trafficking of SORL1
CC implicated in sorting and processing of APP (PubMed:22279231). Involved
CC in retromer-independent lysosomal sorting of F2R (PubMed:16407403).
CC Involved in recycling of ADRB2 (PubMed:21602791). Enhances the affinity
CC of SNX27 for PDZ-binding motifs in cargo proteins (By similarity).
CC {ECO:0000250|UniProtKB:P40336, ECO:0000269|PubMed:15078902,
CC ECO:0000269|PubMed:15078903, ECO:0000269|PubMed:15247922,
CC ECO:0000269|PubMed:16407403, ECO:0000269|PubMed:22070227,
CC ECO:0000269|PubMed:22279231, ECO:0000303|PubMed:20923837,
CC ECO:0000303|PubMed:21602791, ECO:0000303|PubMed:21725319,
CC ECO:0000303|PubMed:23563491, ECO:0000305}.
CC -!- SUBUNIT: Component of the heterotrimeric retromer cargo-selective
CC complex (CSC), also described as vacuolar protein sorting subcomplex
CC (VPS), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35
CC (PubMed:11102511, PubMed:28892079). The CSC has a highly elongated
CC structure with VPS26 and VPS29 binding independently at opposite distal
CC ends of VPS35 as central platform (By similarity). The CSC is believed
CC to associate with variable sorting nexins to form functionally distinct
CC retromer complex variants. The originally described retromer complex
CC (also called SNX-BAR retromer) is a pentamer containing the CSC and a
CC heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2
CC and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC
CC and SNX-BAR subcomplexes associate with low affinity. The CSC
CC associates with SNX3 to form a SNX3-retromer complex. The CSC
CC associates with SNX27, the WASH complex and the SNX-BAR subcomplex to
CC form the SNX27-retromer complex (Probable). Interacts with VPS29,
CC VPS35, SNX1, SNX2, SNX5, SNX6, SNX3, SNX27, RAB7A, ECPAS, EHD1, WASHC5,
CC SORL1 (PubMed:11102511, PubMed:16190980, PubMed:19619496,
CC PubMed:17868075, PubMed:19531583, PubMed:20682791, PubMed:20923837,
CC PubMed:21725319, PubMed:22279231, PubMed:24344282, PubMed:16732284,
CC PubMed:28892079, PubMed:30213940). {ECO:0000250|UniProtKB:P40336,
CC ECO:0000269|PubMed:11102511, ECO:0000269|PubMed:16190980,
CC ECO:0000269|PubMed:16732284, ECO:0000269|PubMed:17868075,
CC ECO:0000269|PubMed:19531583, ECO:0000269|PubMed:20682791,
CC ECO:0000269|PubMed:20923837, ECO:0000269|PubMed:21725319,
CC ECO:0000269|PubMed:22279231, ECO:0000269|PubMed:23563491,
CC ECO:0000269|PubMed:24344282, ECO:0000269|PubMed:28892079,
CC ECO:0000303|PubMed:19619496, ECO:0000303|PubMed:21602791,
CC ECO:0000303|PubMed:21725319}.
CC -!- INTERACTION:
CC O75436; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-1043891, EBI-10288852;
CC O75436; P19404: NDUFV2; NbExp=3; IntAct=EBI-1043891, EBI-713665;
CC O75436; Q9UBQ0: VPS29; NbExp=9; IntAct=EBI-1043891, EBI-718596;
CC O75436; Q96QK1: VPS35; NbExp=23; IntAct=EBI-1043891, EBI-1054634;
CC O75436; O43309: ZSCAN12; NbExp=3; IntAct=EBI-1043891, EBI-1210440;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15078903}. Endosome
CC membrane {ECO:0000269|PubMed:22431521}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P40336}. Early endosome
CC {ECO:0000269|PubMed:15078903, ECO:0000269|PubMed:16190980,
CC ECO:0000269|PubMed:16732284, ECO:0000269|PubMed:20682791}.
CC Note=Localizes to tubular profiles adjacent to endosomes
CC (PubMed:15078903). Predominantly found in early not late endosomes (By
CC similarity). {ECO:0000250|UniProtKB:P40336}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75436-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75436-2; Sequence=VSP_044910;
CC -!- INDUCTION: Down-regulated in Alzheimer disease. No polymorphism or
CC variant is however associated with Alzheimer disease for VPS26A.
CC {ECO:0000269|PubMed:16315276, ECO:0000269|PubMed:16784798}.
CC -!- SIMILARITY: Belongs to the VPS26 family. {ECO:0000305}.
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DR EMBL; AF175266; AAF89954.1; -; mRNA.
DR EMBL; AF054179; AAC39912.1; -; mRNA.
DR EMBL; AK022992; BAB14351.1; -; mRNA.
DR EMBL; AK315496; BAG37880.1; -; mRNA.
DR EMBL; AL596223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL442635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54313.1; -; Genomic_DNA.
DR EMBL; BC022505; AAH22505.1; -; mRNA.
DR EMBL; BQ048905; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS41536.1; -. [O75436-2]
DR CCDS; CCDS7286.1; -. [O75436-1]
DR RefSeq; NP_001030337.1; NM_001035260.2. [O75436-2]
DR RefSeq; NP_001305875.1; NM_001318946.1.
DR RefSeq; NP_004887.2; NM_004896.4. [O75436-1]
DR PDB; 2FAU; X-ray; 2.10 A; A=1-327.
DR PDB; 5F0J; X-ray; 2.70 A; B=2-326.
DR PDB; 5F0L; X-ray; 3.20 A; B=1-317.
DR PDB; 5F0M; X-ray; 3.10 A; B=1-321.
DR PDB; 5F0P; X-ray; 2.78 A; B=1-321.
DR PDB; 7BLO; EM; 9.50 A; F/J=8-301.
DR PDBsum; 2FAU; -.
DR PDBsum; 5F0J; -.
DR PDBsum; 5F0L; -.
DR PDBsum; 5F0M; -.
DR PDBsum; 5F0P; -.
DR PDBsum; 7BLO; -.
DR AlphaFoldDB; O75436; -.
DR SMR; O75436; -.
DR BioGRID; 114930; 181.
DR CORUM; O75436; -.
DR DIP; DIP-29075N; -.
DR IntAct; O75436; 61.
DR MINT; O75436; -.
DR STRING; 9606.ENSP00000362480; -.
DR TCDB; 9.A.3.1.1; the sorting nexin27 (snx27)-retromer assembly apparatus (retromeraa) family.
DR GlyGen; O75436; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75436; -.
DR MetOSite; O75436; -.
DR PhosphoSitePlus; O75436; -.
DR SwissPalm; O75436; -.
DR BioMuta; VPS26A; -.
DR EPD; O75436; -.
DR jPOST; O75436; -.
DR MassIVE; O75436; -.
DR MaxQB; O75436; -.
DR PaxDb; O75436; -.
DR PeptideAtlas; O75436; -.
DR PRIDE; O75436; -.
DR ProteomicsDB; 2454; -.
DR ProteomicsDB; 50002; -. [O75436-1]
DR Antibodypedia; 28695; 224 antibodies from 36 providers.
DR DNASU; 9559; -.
DR Ensembl; ENST00000263559.11; ENSP00000263559.6; ENSG00000122958.15. [O75436-1]
DR Ensembl; ENST00000373382.5; ENSP00000362480.1; ENSG00000122958.15. [O75436-1]
DR Ensembl; ENST00000395098.5; ENSP00000378532.1; ENSG00000122958.15. [O75436-2]
DR GeneID; 9559; -.
DR KEGG; hsa:9559; -.
DR MANE-Select; ENST00000263559.11; ENSP00000263559.6; NM_004896.5; NP_004887.2.
DR UCSC; uc001jpb.4; human. [O75436-1]
DR CTD; 9559; -.
DR DisGeNET; 9559; -.
DR GeneCards; VPS26A; -.
DR HGNC; HGNC:12711; VPS26A.
DR HPA; ENSG00000122958; Low tissue specificity.
DR MIM; 605506; gene.
DR neXtProt; NX_O75436; -.
DR OpenTargets; ENSG00000122958; -.
DR PharmGKB; PA37326; -.
DR VEuPathDB; HostDB:ENSG00000122958; -.
DR eggNOG; KOG3063; Eukaryota.
DR GeneTree; ENSGT00950000183064; -.
DR HOGENOM; CLU_031077_0_0_1; -.
DR InParanoid; O75436; -.
DR OMA; FKQHGKR; -.
DR OrthoDB; 987411at2759; -.
DR PhylomeDB; O75436; -.
DR TreeFam; TF300907; -.
DR PathwayCommons; O75436; -.
DR Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking.
DR SignaLink; O75436; -.
DR BioGRID-ORCS; 9559; 78 hits in 1043 CRISPR screens.
DR ChiTaRS; VPS26A; human.
DR EvolutionaryTrace; O75436; -.
DR GeneWiki; VPS26A; -.
DR GenomeRNAi; 9559; -.
DR Pharos; O75436; Tbio.
DR PRO; PR:O75436; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O75436; protein.
DR Bgee; ENSG00000122958; Expressed in parietal pleura and 209 other tissues.
DR ExpressionAtlas; O75436; baseline and differential.
DR Genevisible; O75436; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:HPA.
DR GO; GO:0030904; C:retromer complex; IDA:UniProtKB.
DR GO; GO:0030906; C:retromer, cargo-selective complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097422; C:tubular endosome; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR Gene3D; 2.60.40.640; -; 2.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR028934; Vps26-related.
DR PANTHER; PTHR12233; PTHR12233; 1.
DR Pfam; PF03643; Vps26; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Endosome; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..327
FT /note="Vacuolar protein sorting-associated protein 26A"
FT /id="PRO_0000073007"
FT REGION 306..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 243..327
FT /note="GESIPIRLFLAGYDPTPTMRDVNKKFSVRYFLNLVLVDEEDRRYFKQQEIIL
FT WRKAPEKLRKQRTNFHQRFESPESQASAEQPEM -> GDNFMEKSS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044910"
FT MUTAGEN 235..236
FT /note="IM->DD: Abolishes interaction with VPS35 and
FT endosomal subcellular location."
FT CONFLICT 75
FT /note="Q -> R (in Ref. 3; BAB14351)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="K -> Q (in Ref. 6; BQ048905)"
FT /evidence="ECO:0000305"
FT CONFLICT 285..286
FT /note="RY -> SS (in Ref. 1; AAF89954 and 2; AAC39912)"
FT /evidence="ECO:0000305"
FT TURN 7..11
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:2FAU"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2FAU"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5F0J"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 48..60
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 68..78
FT /evidence="ECO:0007829|PDB:2FAU"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5F0J"
FT STRAND 85..96
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 124..136
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:2FAU"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 190..200
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 204..218
FT /evidence="ECO:0007829|PDB:2FAU"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 224..234
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:2FAU"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 268..280
FT /evidence="ECO:0007829|PDB:2FAU"
FT STRAND 285..295
FT /evidence="ECO:0007829|PDB:2FAU"
FT CONFLICT O75436-2:243
FT /note="G -> R (in Ref. 6; BQ048905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 38170 MW; BD3B2EAA6CFCBFA9 CRC64;
MSFLGGFFGP ICEIDIVLND GETRKMAEMK TEDGKVEKHY LFYDGESVSG KVNLAFKQPG
KRLEHQGIRI EFVGQIELFN DKSNTHEFVN LVKELALPGE LTQSRSYDFE FMQVEKPYES
YIGANVRLRY FLKVTIVRRL TDLVKEYDLI VHQLATYPDV NNSIKMEVGI EDCLHIEFEY
NKSKYHLKDV IVGKIYFLLV RIKIQHMELQ LIKKEITGIG PSTTTETETI AKYEIMDGAP
VKGESIPIRL FLAGYDPTPT MRDVNKKFSV RYFLNLVLVD EEDRRYFKQQ EIILWRKAPE
KLRKQRTNFH QRFESPESQA SAEQPEM
