VP322_ARATH
ID VP322_ARATH Reviewed; 219 AA.
AC Q9SZE4; Q3E9U7; Q8L9C3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Vacuolar protein sorting-associated protein 32 homolog 2;
DE Short=AtVPS32-2;
DE AltName: Full=Charged multivesicular body protein 4 homolog 2;
DE AltName: Full=ESCRT-III complex subunit VPS32 homolog 2;
GN Name=VPS32.2;
GN Synonyms=CHMP4-2, SNF7.1 {ECO:0000303|PubMed:24812106},
GN SNF7B {ECO:0000303|PubMed:22639582}; OrderedLocusNames=At4g29160;
GN ORFNames=F19B15.190;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] (ISOFORM 1).
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] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=17090720; DOI=10.1242/dev.02654;
RA Spitzer C., Schellmann S., Sabovljevic A., Shahriari M., Keshavaiah C.,
RA Bechtold N., Herzog M., Mueller S., Hanisch F.-G., Huelskamp M.;
RT "The Arabidopsis elch mutant reveals functions of an ESCRT component in
RT cytokinesis.";
RL Development 133:4679-4689(2006).
RN [6]
RP IDENTIFICATION.
RX PubMed=16488176; DOI=10.1016/j.tplants.2006.01.008;
RA Winter V., Hauser M.-T.;
RT "Exploring the ESCRTing machinery in eukaryotes.";
RL Trends Plant Sci. 11:115-123(2006).
RN [7]
RP INTERACTION WITH SKD1.
RC STRAIN=cv. Columbia;
RX PubMed=20663085; DOI=10.1111/j.1365-313x.2010.04310.x;
RA Shahriari M., Keshavaiah C., Scheuring D., Sabovljevic A., Pimpl P.,
RA Haeusler R.E., Huelskamp M., Schellmann S.;
RT "The AAA-type ATPase AtSKD1 contributes to vacuolar maintenance of
RT Arabidopsis thaliana.";
RL Plant J. 64:71-85(2010).
RN [8]
RP NOMENCLATURE, AND INTERACTION WITH BRO1.
RX PubMed=22639582; DOI=10.3389/fpls.2011.00020;
RA Richardson L.G., Howard A.S., Khuu N., Gidda S.K., McCartney A.,
RA Morphy B.J., Mullen R.T.;
RT "Protein-protein interaction network and subcellular localization of the
RT Arabidopsis thaliana ESCRT machinery.";
RL Front. Plant Sci. 2:20-20(2011).
RN [9]
RP INTERACTION WITH SKD1, AND REVIEW ON ESCRT-III.
RX PubMed=24812106; DOI=10.1104/pp.114.238378;
RA Cai Y., Zhuang X., Gao C., Wang X., Jiang L.;
RT "The Arabidopsis endosomal sorting complex required for transport III
RT regulates internal vesicle formation of the prevacuolar compartment and is
RT required for plant development.";
RL Plant Physiol. 165:1328-1343(2014).
RN [10]
RP INTERACTION WITH BRO1.
RX PubMed=26342016; DOI=10.1105/tpc.15.00393;
RA Cardona-Lopez X., Cuyas L., Marin E., Rajulu C., Irigoyen M.L., Gil E.,
RA Puga M.I., Bligny R., Nussaume L., Geldner N., Paz-Ares J., Rubio V.;
RT "ESCRT-III-associated protein ALIX mediates high-affinity phosphate
RT transporter trafficking to maintain phosphate homeostasis in Arabidopsis.";
RL Plant Cell 27:2560-2581(2015).
CC -!- FUNCTION: Component of the ESCRT-III complex, which is required for
CC multivesicular bodies (MVBs) formation and sorting of endosomal cargo
CC proteins into MVBs. The ESCRT-III complex is probably involved in the
CC concentration of MVB cargo (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the endosomal sorting required for transport
CC complex III (ESCRT-III), composed at least of VPS2, VPS20, VPS24 and
CC VPS32 (By similarity). Interacts with SKD1 (PubMed:20663085
CC PubMed:24812106). Interacts with BRO1/ALIX (PubMed:22639582,
CC PubMed:26342016). {ECO:0000250|UniProtKB:Q9H444,
CC ECO:0000269|PubMed:20663085, ECO:0000269|PubMed:22639582,
CC ECO:0000269|PubMed:24812106, ECO:0000269|PubMed:26342016}.
CC -!- INTERACTION:
CC Q9SZE4; Q0WTY4: VPS2.2; NbExp=3; IntAct=EBI-3865953, EBI-3865323;
CC Q9SZE4; Q9FY89: VPS20.2; NbExp=3; IntAct=EBI-3865953, EBI-3865360;
CC Q9SZE4; O82197: VPS32.1; NbExp=4; IntAct=EBI-3865953, EBI-3865938;
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SZE4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SZE4-2; Sequence=VSP_036804;
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM66053.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL078470; CAB43930.1; -; Genomic_DNA.
DR EMBL; AL161574; CAB79674.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85593.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85594.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85595.1; -; Genomic_DNA.
DR EMBL; AY042853; AAK68793.1; -; mRNA.
DR EMBL; AY072490; AAL66905.1; -; mRNA.
DR EMBL; AY088519; AAM66053.1; ALT_INIT; mRNA.
DR PIR; T08971; T08971.
DR RefSeq; NP_001078468.1; NM_001084999.2. [Q9SZE4-1]
DR RefSeq; NP_194645.1; NM_119060.5. [Q9SZE4-1]
DR RefSeq; NP_974635.1; NM_202906.1. [Q9SZE4-2]
DR AlphaFoldDB; Q9SZE4; -.
DR SMR; Q9SZE4; -.
DR BioGRID; 14324; 19.
DR IntAct; Q9SZE4; 13.
DR STRING; 3702.AT4G29160.3; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR MetOSite; Q9SZE4; -.
DR PaxDb; Q9SZE4; -.
DR PRIDE; Q9SZE4; -.
DR ProteomicsDB; 242645; -. [Q9SZE4-1]
DR EnsemblPlants; AT4G29160.1; AT4G29160.1; AT4G29160. [Q9SZE4-1]
DR EnsemblPlants; AT4G29160.2; AT4G29160.2; AT4G29160. [Q9SZE4-2]
DR EnsemblPlants; AT4G29160.3; AT4G29160.3; AT4G29160. [Q9SZE4-1]
DR GeneID; 829037; -.
DR Gramene; AT4G29160.1; AT4G29160.1; AT4G29160. [Q9SZE4-1]
DR Gramene; AT4G29160.2; AT4G29160.2; AT4G29160. [Q9SZE4-2]
DR Gramene; AT4G29160.3; AT4G29160.3; AT4G29160. [Q9SZE4-1]
DR KEGG; ath:AT4G29160; -.
DR Araport; AT4G29160; -.
DR TAIR; locus:2119956; AT4G29160.
DR eggNOG; KOG1656; Eukaryota.
DR InParanoid; Q9SZE4; -.
DR OMA; QHMDVDQ; -.
DR PhylomeDB; Q9SZE4; -.
DR PRO; PR:Q9SZE4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZE4; baseline and differential.
DR Genevisible; Q9SZE4; AT.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0000815; C:ESCRT III complex; ISS:TAIR.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0070676; P:intralumenal vesicle formation; IDA:TAIR.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Endosome; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..219
FT /note="Vacuolar protein sorting-associated protein 32
FT homolog 2"
FT /id="PRO_0000368201"
FT REGION 168..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 10..41
FT /evidence="ECO:0000255"
FT COILED 117..176
FT /evidence="ECO:0000255"
FT COMPBIAS 181..195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036804"
SQ SEQUENCE 219 AA; 24333 MW; 711E9EEB70450D6B CRC64;
MMNRLFGKPK QEANALQTLD KLNETLEMLE KKEKVLLKKA GAEVEKAKEY SRAKNKRAAI
QCLKRKRLYE GQVEQLGNFQ LRIHDQMIML EGAKATTETV DALRSGASAM KAMQKATNID
DVDKTMDEIN EQTENMKQIQ EALATPMGAA ADFDEDELAA ELDELESEEL ESQLLQPATT
APPLPSVPVP AGRQPARPVP QKRTAEEEEL AALQAEMAL
