VPS29_ARATH
ID VPS29_ARATH Reviewed; 190 AA.
AC Q9STT2; Q3EAN1;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Vacuolar protein sorting-associated protein 29;
DE AltName: Full=Protein MAIGO 1 {ECO:0000303|PubMed:16926167};
DE AltName: Full=Vesicle protein sorting 29;
GN Name=VPS29; Synonyms=MAG1 {ECO:0000303|PubMed:16926167};
GN OrderedLocusNames=At3g47810; ORFNames=T23J7.140;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP COMPONENT OF THE RETROMER COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=16582012; DOI=10.1105/tpc.105.035907;
RA Oliviusson P., Heinzerling O., Hillmer S., Hinz G., Tse Y.C., Jiang L.,
RA Robinson D.G.;
RT "Plant retromer, localized to the prevacuolar compartment and microvesicles
RT in Arabidopsis, may interact with vacuolar sorting receptors.";
RL Plant Cell 18:1239-1252(2006).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=16926167; DOI=10.1093/pcp/pcj103;
RA Shimada T., Koumoto Y., Li L., Yamazaki M., Kondo M., Nishimura M.,
RA Hara-Nishimura I.;
RT "AtVPS29, a putative component of a retromer complex, is required for the
RT efficient sorting of seed storage proteins.";
RL Plant Cell Physiol. 47:1187-1194(2006).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, COMPONENT OF THE VPS26-VPS29-VPS35 RETROMER
RP SUBCOMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=17889650; DOI=10.1016/j.cell.2007.08.040;
RA Jaillais Y., Santambrogio M., Rozier F., Fobis-Loisy I., Miege C.,
RA Gaude T.;
RT "The retromer protein VPS29 links cell polarity and organ initiation in
RT plants.";
RL Cell 130:1057-1070(2007).
RN [8]
RP FUNCTION.
RX PubMed=19004783; DOI=10.1073/pnas.0808073105;
RA Kleine-Vehn J., Leitner J., Zwiewka M., Sauer M., Abas L., Luschnig C.,
RA Friml J.;
RT "Differential degradation of PIN2 auxin efflux carrier by retromer-
RT dependent vacuolar targeting.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17812-17817(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=21156856; DOI=10.1105/tpc.110.078451;
RA Pourcher M., Santambrogio M., Thazar N., Thierry A.M., Fobis-Loisy I.,
RA Miege C., Jaillais Y., Gaude T.;
RT "Analyses of sorting nexins reveal distinct retromer-subcomplex functions
RT in development and protein sorting in Arabidopsis thaliana.";
RL Plant Cell 22:3980-3991(2010).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=19796370; DOI=10.1111/j.1365-313x.2009.04034.x;
RA Niemes S., Langhans M., Viotti C., Scheuring D., San Wan Yan M., Jiang L.,
RA Hillmer S., Robinson D.G., Pimpl P.;
RT "Retromer recycles vacuolar sorting receptors from the trans-Golgi
RT network.";
RL Plant J. 61:107-121(2010).
CC -!- FUNCTION: Plays a role in vesicular protein sorting. Component of the
CC membrane-associated retromer complex which is essential in endosome-to-
CC Golgi retrograde transport. Required for the auxin-carrier protein PIN2
CC sorting to the lytic vacuolar pathway and the PIN1 recycling to the
CC plasma membrane. Also involved in the efficient sorting of seed storage
CC proteins globulin 12S and albumin 2S. The VPS29-VPS26-VPS35 subcomplex
CC may be involved in recycling of specific cargos from endosome to the
CC plasma membrane. {ECO:0000269|PubMed:17889650,
CC ECO:0000269|PubMed:19004783}.
CC -!- SUBUNIT: Component of the retromer complex which consists of VPS29
CC (MAG1), VPS26 (VPS26A or VPS26B), VPS35 (VPS35A or VPS35B or VPS35C),
CC VPS5/17 (SNX1 or SNX2A or SNX2B). Component of a retromer subcomplex
CC consisting of VPS29 (MAG1), VPS26 (VPS26A or VPS26B), VPS35 (VPS35A or
CC VPS35B or VPS35C).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side. Prevacuolar compartment membrane; Peripheral
CC membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi
CC network membrane; Peripheral membrane protein; Cytoplasmic side.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype. Reduced primary root length and
CC fewer secondary roots. Abnormal cotyledon shape, number and
CC positioning. Accumulation of storage proteins globulin 12S and albumin
CC 2S in dry seeds. {ECO:0000269|PubMed:16926167,
CC ECO:0000269|PubMed:17889650}.
CC -!- SIMILARITY: Belongs to the VPS29 family. {ECO:0000305}.
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DR EMBL; AL049746; CAB41864.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78331.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78332.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78333.1; -; Genomic_DNA.
DR EMBL; BT002774; AAO22602.1; -; mRNA.
DR EMBL; BT004347; AAO42341.1; -; mRNA.
DR EMBL; AK317472; BAH20137.1; -; mRNA.
DR PIR; T07720; T07720.
DR RefSeq; NP_190365.3; NM_114649.4.
DR RefSeq; NP_974399.2; NM_202670.3.
DR RefSeq; NP_974400.1; NM_202671.3.
DR AlphaFoldDB; Q9STT2; -.
DR SMR; Q9STT2; -.
DR BioGRID; 9255; 5.
DR IntAct; Q9STT2; 6.
DR STRING; 3702.AT3G47810.2; -.
DR PaxDb; Q9STT2; -.
DR PRIDE; Q9STT2; -.
DR ProteomicsDB; 242738; -.
DR EnsemblPlants; AT3G47810.1; AT3G47810.1; AT3G47810.
DR EnsemblPlants; AT3G47810.2; AT3G47810.2; AT3G47810.
DR EnsemblPlants; AT3G47810.3; AT3G47810.3; AT3G47810.
DR GeneID; 823935; -.
DR Gramene; AT3G47810.1; AT3G47810.1; AT3G47810.
DR Gramene; AT3G47810.2; AT3G47810.2; AT3G47810.
DR Gramene; AT3G47810.3; AT3G47810.3; AT3G47810.
DR KEGG; ath:AT3G47810; -.
DR Araport; AT3G47810; -.
DR TAIR; locus:2100362; AT3G47810.
DR eggNOG; KOG3325; Eukaryota.
DR HOGENOM; CLU_063749_0_1_1; -.
DR InParanoid; Q9STT2; -.
DR OMA; IVVYVYE; -.
DR OrthoDB; 1233814at2759; -.
DR PhylomeDB; Q9STT2; -.
DR PRO; PR:Q9STT2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STT2; baseline and differential.
DR Genevisible; Q9STT2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005771; C:multivesicular body; IDA:TAIR.
DR GO; GO:0030904; C:retromer complex; IDA:TAIR.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:TAIR.
DR GO; GO:0001881; P:receptor recycling; IDA:TAIR.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0007034; P:vacuolar transport; IMP:TAIR.
DR CDD; cd07394; MPP_Vps29; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR InterPro; IPR028661; Vps29.
DR PANTHER; PTHR11124; PTHR11124; 1.
DR Pfam; PF12850; Metallophos_2; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR00040; yfcE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endosome; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..190
FT /note="Vacuolar protein sorting-associated protein 29"
FT /id="PRO_0000414723"
SQ SEQUENCE 190 AA; 20968 MW; C749EB2FE34095E5 CRC64;
MVLVLALGDL HVPHRAADLP PKFKSMLVPG KIQHIICTGN LCIKEIHDYL KTICPDLHIV
RGEFDEDARY PENKTLTIGQ FKLGLCHGHQ VIPWGDLDSL AMLQRQLGVD ILVTGHTHQF
TAYKHEGGVV INPGSATGAY SSINQDVNPS FVLMDIDGFR AVVYVYELID GEVKVDKIEF
KKPPTTSSGP
