VP35A_ARATH
ID VP35A_ARATH Reviewed; 787 AA.
AC Q7X659; Q0WMP3;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Vacuolar protein sorting-associated protein 35A;
DE AltName: Full=Protein ZIG SUPPRESSOR 3;
DE AltName: Full=Vesicle protein sorting 35A;
GN Name=VPS35A; Synonyms=ZIP3; OrderedLocusNames=At2g17790; ORFNames=T17A5.7;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] OF 591-787.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 SUBCELLULAR LOCATION.
RX PubMed=18222962; DOI=10.1093/pcp/pcn006;
RA Yamazaki M., Shimada T., Takahashi H., Tamura K., Kondo M., Nishimura M.,
RA Hara-Nishimura I.;
RT "Arabidopsis VPS35, a retromer component, is required for vacuolar protein
RT sorting and involved in plant growth and leaf senescence.";
RL Plant Cell Physiol. 49:142-156(2008).
RN [7]
RP FUNCTION.
RX PubMed=20086190; DOI=10.1105/tpc.109.069294;
RA Hashiguchi Y., Niihama M., Takahashi T., Saito C., Nakano A., Tasaka M.,
RA Morita M.T.;
RT "Loss-of-function mutations of retromer large subunit genes suppress the
RT phenotype of an Arabidopsis zig mutant that lacks Qb-SNARE VTI11.";
RL Plant Cell 22:159-172(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP FUNCTION, INTERACTION WITH RABG3F, AND SUBCELLULAR LOCATION.
RX PubMed=23362252; DOI=10.1074/jbc.m112.440503;
RA Zelazny E., Santambrogio M., Pourcher M., Chambrier P., Berne-Dedieu A.,
RA Fobis-Loisy I., Miege C., Jaillais Y., Gaude T.;
RT "Mechanisms governing the endosomal membrane recruitment of the core
RT retromer in Arabidopsis.";
RL J. Biol. Chem. 288:8815-8825(2013).
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. Also involved in the efficient sorting of
CC seed storage proteins (Probable). Binds alone to endosomal membranes
CC and is required for recruitment of VPS26 and VPS29 to membrane
CC (PubMed:23362252). The VPS29-VPS26-VPS35 subcomplex may be involved in
CC recycling of specific cargos from endosome to the plasma membrane
CC (PubMed:20086190). {ECO:0000269|PubMed:20086190,
CC ECO:0000269|PubMed:23362252, ECO:0000305|PubMed:23362252}.
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) (Probable). Interacts with RABG3F (PubMed:23362252).
CC {ECO:0000269|PubMed:23362252, ECO:0000305|PubMed:23362252}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane
CC {ECO:0000269|PubMed:23362252}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Prevacuolar compartment
CC membrane; Peripheral membrane protein; Cytoplasmic side. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS35 family. {ECO:0000305}.
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DR EMBL; CP002685; AEC06688.1; -; Genomic_DNA.
DR EMBL; BT008553; AAP40380.1; -; mRNA.
DR EMBL; BT008664; AAP40476.1; -; mRNA.
DR EMBL; AK229772; BAF01607.1; -; mRNA.
DR RefSeq; NP_179370.2; NM_127333.5.
DR AlphaFoldDB; Q7X659; -.
DR SMR; Q7X659; -.
DR BioGRID; 1646; 3.
DR IntAct; Q7X659; 2.
DR STRING; 3702.AT2G17790.1; -.
DR iPTMnet; Q7X659; -.
DR PaxDb; Q7X659; -.
DR PRIDE; Q7X659; -.
DR ProteomicsDB; 242749; -.
DR EnsemblPlants; AT2G17790.1; AT2G17790.1; AT2G17790.
DR GeneID; 816289; -.
DR Gramene; AT2G17790.1; AT2G17790.1; AT2G17790.
DR KEGG; ath:AT2G17790; -.
DR Araport; AT2G17790; -.
DR TAIR; locus:2827896; AT2G17790.
DR eggNOG; KOG1107; Eukaryota.
DR HOGENOM; CLU_005836_1_0_1; -.
DR InParanoid; Q7X659; -.
DR OMA; WWVVENP; -.
DR OrthoDB; 316875at2759; -.
DR PhylomeDB; Q7X659; -.
DR PRO; PR:Q7X659; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7X659; baseline and differential.
DR Genevisible; Q7X659; AT.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0030904; C:retromer complex; IBA:GO_Central.
DR GO; GO:0030906; C:retromer, cargo-selective complex; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR Gene3D; 1.25.40.660; -; 1.
DR InterPro; IPR005378; Vps35.
DR InterPro; IPR042491; Vps35_C.
DR PANTHER; PTHR11099; PTHR11099; 1.
DR Pfam; PF03635; Vps35; 1.
DR PIRSF; PIRSF009375; Retromer_Vps35; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endosome; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..787
FT /note="Vacuolar protein sorting-associated protein 35A"
FT /id="PRO_0000414724"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 787 AA; 89493 MW; EB4A591B9AA90687 CRC64;
MIADGSEDEE KWLAAGAAAF KQNAFYMQRA IDSNNLKDAL KYSAQMLSEL RTSKLSPHKY
YDLYMRAFDE LRKLEIFFME ETRRGCSVIE LYELVQHAGN ILPRLYLLCT AGSVYIKTKE
APAKEILKDL VEMCRGIQHP LRGLFLRSYL AQISRDKLPD IGSEYEGDAD TVIDAVEFVL
LNFTEMNKLW VRMQHQGPAR EKERREKERG ELRDLVGKNL HVLSQLEGVD LDMYRDTVLP
RVLEQIVNCR DEIAQYYLID CIIQVFPDEY HLQTLDVLLG ACPQLQASVD IMTVLSRLME
RLSNYAALNA EVLPYFLQVE AFSKLNNAIG KVIEAQEDMP ILSAVTLYSS LLKFTLHVHP
DRLDYADQVL GSCVKQLSGK GKIDDTRATK ELVSLLSAPL EKYNDVVTAL KLTNYPLVVE
YLDTETKRIM ATVIVRSIMK NNTLITTAEK VEALFELIKG IINDLDEPQG LEVDEDDFQE
EQNSVALLIH MLYNDDPEEM FKIVNVLKKH FLTGGPKRLK FTIPPLVVST LKLIRRLPVE
GDNPFGKEAS VTATKIFQFL NQIIEALPNV PSPDLAFRLY LQCAEAADKC DEEPIAYEFF
TQAYILYEEE ISDSKAQVTA LQLIIGTLQR MQVFGVENRD TLTHKATGYA AKLLKKPDQC
RAVYACSHLF WLEDRETIQD GERVLLCLKR ALKIANSAQQ VANTARGSTG SVTLFIEILN
KYLYFYEKGV PQITVESVES LIKLIKNEES MPSDPSAESF FATTLEFMEF QKQKEGAIGE
RYQAIKV
