VPS25_ARATH
ID VPS25_ARATH Reviewed; 179 AA.
AC Q8VZC9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Vacuolar protein sorting-associated protein 25;
DE Short=AtVPS25;
DE AltName: Full=ESCRT-II complex subunit VPS25;
GN Name=VPS25; OrderedLocusNames=At4g19003; ORFNames=F13C5;
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].
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;
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 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).
CC -!- FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex
CC required for transport II), which is required for multivesicular body
CC (MVB) formation and sorting of endosomal cargo proteins into MVBs. The
CC ESCRT-II complex is probably involved in the recruitment of the ESCRT-
CC III complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the ESCRT-II complex (endosomal sorting complex
CC required for transport II), composed of VPS22, VPS25 and VPS36.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q8VZC9; Q8GXN6: VPS20.1; NbExp=4; IntAct=EBI-3865350, EBI-3865286;
CC Q8VZC9; Q9FY89: VPS20.2; NbExp=7; IntAct=EBI-3865350, EBI-3865360;
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS25 family. {ECO:0000305}.
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DR EMBL; AL161549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE84122.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84123.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67992.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67993.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67994.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67995.1; -; Genomic_DNA.
DR EMBL; AY065055; AAL57689.1; -; mRNA.
DR EMBL; AY093752; AAM10376.1; -; mRNA.
DR EMBL; AK317105; BAH19794.1; -; mRNA.
DR RefSeq; NP_001319990.1; NM_001341314.1.
DR RefSeq; NP_001319991.1; NM_001341313.1.
DR RefSeq; NP_001329780.1; NM_001341316.1.
DR RefSeq; NP_001329781.1; NM_001341315.1.
DR RefSeq; NP_680720.1; NM_148354.4.
DR RefSeq; NP_974570.1; NM_202841.2.
DR AlphaFoldDB; Q8VZC9; -.
DR SMR; Q8VZC9; -.
DR BioGRID; 12930; 6.
DR DIP; DIP-61574N; -.
DR IntAct; Q8VZC9; 5.
DR STRING; 3702.AT4G19003.2; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR PaxDb; Q8VZC9; -.
DR PRIDE; Q8VZC9; -.
DR ProteomicsDB; 242671; -.
DR DNASU; 827637; -.
DR EnsemblPlants; AT4G19003.1; AT4G19003.1; AT4G19003.
DR EnsemblPlants; AT4G19003.2; AT4G19003.2; AT4G19003.
DR EnsemblPlants; AT4G19003.3; AT4G19003.3; AT4G19003.
DR EnsemblPlants; AT4G19003.4; AT4G19003.4; AT4G19003.
DR EnsemblPlants; AT4G19003.5; AT4G19003.5; AT4G19003.
DR EnsemblPlants; AT4G19003.6; AT4G19003.6; AT4G19003.
DR GeneID; 827637; -.
DR Gramene; AT4G19003.1; AT4G19003.1; AT4G19003.
DR Gramene; AT4G19003.2; AT4G19003.2; AT4G19003.
DR Gramene; AT4G19003.3; AT4G19003.3; AT4G19003.
DR Gramene; AT4G19003.4; AT4G19003.4; AT4G19003.
DR Gramene; AT4G19003.5; AT4G19003.5; AT4G19003.
DR Gramene; AT4G19003.6; AT4G19003.6; AT4G19003.
DR KEGG; ath:AT4G19003; -.
DR Araport; AT4G19003; -.
DR TAIR; locus:504955551; AT4G19003.
DR eggNOG; KOG4068; Eukaryota.
DR HOGENOM; CLU_087657_1_2_1; -.
DR InParanoid; Q8VZC9; -.
DR OMA; SQEFHGM; -.
DR OrthoDB; 1094121at2759; -.
DR PhylomeDB; Q8VZC9; -.
DR PRO; PR:Q8VZC9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VZC9; baseline and differential.
DR GO; GO:0000814; C:ESCRT II complex; ISS:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.10.570; -; 1.
DR InterPro; IPR008570; ESCRT-II_cplx_Vps25-sub.
DR InterPro; IPR014041; ESCRT-II_cplx_Vps25-sub_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13149; PTHR13149; 1.
DR Pfam; PF05871; ESCRT-II; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 1: Evidence at protein level;
KW Endosome; Protein transport; Reference proteome; Transport.
FT CHAIN 1..179
FT /note="Vacuolar protein sorting-associated protein 25"
FT /id="PRO_0000368193"
SQ SEQUENCE 179 AA; 20682 MW; 34FCFEA07F95AC39 CRC64;
MQKLADFKLP QFFNYPPYFT LQPVRDTREK QIQLWKELIL DYCKSQKIFL IGVEEDFPLF
SNSAIDRSLS HEARETFLSA IVGEGRAEWL DKGHRKCLIL WHRIQDWADI VLQFVRDNGL
EDSVMTVEEI RSGTESLGTE LQGIDRTILM RALKLLENKG KLALFKGTSA DDEGVKFSV
