VP281_ARATH
ID VP281_ARATH Reviewed; 209 AA.
AC O65421;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Vacuolar protein sorting-associated protein 28 homolog 1;
GN Name=VPS28-1; OrderedLocusNames=At4g21560; ORFNames=F17L22.20, F18E5.180;
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 IDENTIFICATION, NOMENCLATURE, AND INTERACTION WITH ELC.
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 [5]
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-I complex (endosomal sorting complex
CC required for transport I), a regulator of vesicular trafficking
CC process. Required for the sorting of endocytic ubiquitinated cargos
CC into multivesicular bodies (MVBs). Mediates the association to the
CC ESCRT-0 complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the endosomal sorting required for transport
CC complex I (ESCRT-I), composed of ELC, VPS28 and VPS37. Interacts with
CC ELC. {ECO:0000269|PubMed:17090720}.
CC -!- INTERACTION:
CC O65421; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-3865310, EBI-4426557;
CC O65421; Q0WTY4: VPS2.2; NbExp=4; IntAct=EBI-3865310, EBI-3865323;
CC O65421; Q9SCP9: VPS37-1; NbExp=3; IntAct=EBI-3865310, EBI-3865264;
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS28 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00642, ECO:0000255|PROSITE-ProRule:PRU00645}.
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DR EMBL; AL022603; CAA18720.1; -; Genomic_DNA.
DR EMBL; AL035527; CAB36800.1; -; Genomic_DNA.
DR EMBL; AL161555; CAB81263.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84469.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84470.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84471.1; -; Genomic_DNA.
DR EMBL; AY136475; AAM97140.1; -; mRNA.
DR EMBL; BT006261; AAP13369.1; -; mRNA.
DR PIR; T05164; T05164.
DR RefSeq; NP_001320024.1; NM_001341499.1.
DR RefSeq; NP_193887.1; NM_118276.4.
DR RefSeq; NP_974585.1; NM_202856.3.
DR AlphaFoldDB; O65421; -.
DR SMR; O65421; -.
DR BioGRID; 13530; 8.
DR IntAct; O65421; 6.
DR STRING; 3702.AT4G21560.3; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR PaxDb; O65421; -.
DR PRIDE; O65421; -.
DR ProteomicsDB; 242682; -.
DR EnsemblPlants; AT4G21560.1; AT4G21560.1; AT4G21560.
DR EnsemblPlants; AT4G21560.2; AT4G21560.2; AT4G21560.
DR EnsemblPlants; AT4G21560.3; AT4G21560.3; AT4G21560.
DR GeneID; 828241; -.
DR Gramene; AT4G21560.1; AT4G21560.1; AT4G21560.
DR Gramene; AT4G21560.2; AT4G21560.2; AT4G21560.
DR Gramene; AT4G21560.3; AT4G21560.3; AT4G21560.
DR KEGG; ath:AT4G21560; -.
DR Araport; AT4G21560; -.
DR TAIR; locus:2119662; AT4G21560.
DR eggNOG; KOG3284; Eukaryota.
DR HOGENOM; CLU_076417_1_0_1; -.
DR InParanoid; O65421; -.
DR OMA; NAREREX; -.
DR OrthoDB; 1281819at2759; -.
DR PhylomeDB; O65421; -.
DR PRO; PR:O65421; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65421; baseline and differential.
DR Genevisible; O65421; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0000813; C:ESCRT I complex; ISS:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0044877; F:protein-containing complex binding; 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; 1.20.120.1130; -; 1.
DR Gene3D; 1.20.1440.200; -; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR007143; Vps28.
DR InterPro; IPR017899; VPS28_C.
DR InterPro; IPR037206; VPS28_C_sf.
DR InterPro; IPR017898; VPS28_N.
DR InterPro; IPR038358; VPS28_N_sf.
DR PANTHER; PTHR12937; PTHR12937; 1.
DR Pfam; PF03997; VPS28; 1.
DR PIRSF; PIRSF017535; VPS28; 1.
DR SUPFAM; SSF140111; SSF140111; 1.
DR SUPFAM; SSF140427; SSF140427; 1.
DR PROSITE; PS51310; VPS28_C; 1.
DR PROSITE; PS51313; VPS28_N; 1.
PE 1: Evidence at protein level;
KW Endosome; Protein transport; Reference proteome; Transport.
FT CHAIN 1..209
FT /note="Vacuolar protein sorting-associated protein 28
FT homolog 1"
FT /id="PRO_0000120956"
FT DOMAIN 1..99
FT /note="VPS28 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00645"
FT DOMAIN 109..205
FT /note="VPS28 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00642"
SQ SEQUENCE 209 AA; 23494 MW; 8A8BB4B415D9786B CRC64;
MEVKLWNDKR EREMYENFAE LYAIIKATEK LEKAYIRDLI SPSEYETECQ KLIVHFKTLS
ASLKDMVPNI ERFAETYKMD CSAAVYRLVT SGVPATVEHR AAASASTSSS ASVVAECVQN
FITSMDSLKL NMVAVDQVYP LLSDLSASLN KLSILPPDFE GKIKMKEWLL RLSKMGASDE
LTEQQARQLH FDLESSYNSF MAALPNAGN
