VP221_ARATH
ID VP221_ARATH Reviewed; 250 AA.
AC Q5M759; Q9SZ43;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Vacuolar protein sorting-associated protein 22 homolog 1;
DE Short=AtVPS22-1;
DE AltName: Full=ESCRT-II complex subunit VPS22 homolog 1;
GN Name=VP22-1; OrderedLocusNames=At4g27040; ORFNames=F10M23.380;
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].
RX PubMed=15805490; DOI=10.1101/gr.3176505;
RA Ayele M., Haas B.J., Kumar N., Wu H., Xiao Y., Van Aken S., Utterback T.R.,
RA Wortman J.R., White O.R., Town C.D.;
RT "Whole genome shotgun sequencing of Brassica oleracea and its application
RT to gene discovery and annotation in Arabidopsis.";
RL Genome Res. 15:487-495(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) 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).
CC -!- FUNCTION: Component of the endosomal sorting complex required for
CC transport II (ESCRT-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 endosomal sorting complex required for
CC transport II (ESCRT-II), composed of VPS22, VPS25 and VPS36.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36550.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79559.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035440; CAB36550.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161566; CAB79559.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85287.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85288.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85289.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85290.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66725.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66726.1; -; Genomic_DNA.
DR EMBL; AY299265; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT020389; AAV91335.1; -; mRNA.
DR EMBL; BT020552; AAW70398.1; -; mRNA.
DR PIR; T04827; T04827.
DR RefSeq; NP_001119065.1; NM_001125593.1.
DR RefSeq; NP_001119066.1; NM_001125594.1.
DR RefSeq; NP_001119067.1; NM_001125595.2.
DR RefSeq; NP_001328603.1; NM_001341835.1.
DR RefSeq; NP_001328604.1; NM_001341834.1.
DR RefSeq; NP_194434.2; NM_118838.5.
DR AlphaFoldDB; Q5M759; -.
DR SMR; Q5M759; -.
DR BioGRID; 14099; 6.
DR IntAct; Q5M759; 5.
DR STRING; 3702.AT4G27040.2; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR PaxDb; Q5M759; -.
DR PRIDE; Q5M759; -.
DR ProteomicsDB; 242623; -.
DR DNASU; 828812; -.
DR EnsemblPlants; AT4G27040.1; AT4G27040.1; AT4G27040.
DR EnsemblPlants; AT4G27040.2; AT4G27040.2; AT4G27040.
DR EnsemblPlants; AT4G27040.3; AT4G27040.3; AT4G27040.
DR EnsemblPlants; AT4G27040.4; AT4G27040.4; AT4G27040.
DR EnsemblPlants; AT4G27040.5; AT4G27040.5; AT4G27040.
DR EnsemblPlants; AT4G27040.6; AT4G27040.6; AT4G27040.
DR GeneID; 828812; -.
DR Gramene; AT4G27040.1; AT4G27040.1; AT4G27040.
DR Gramene; AT4G27040.2; AT4G27040.2; AT4G27040.
DR Gramene; AT4G27040.3; AT4G27040.3; AT4G27040.
DR Gramene; AT4G27040.4; AT4G27040.4; AT4G27040.
DR Gramene; AT4G27040.5; AT4G27040.5; AT4G27040.
DR Gramene; AT4G27040.6; AT4G27040.6; AT4G27040.
DR KEGG; ath:AT4G27040; -.
DR Araport; AT4G27040; -.
DR TAIR; locus:2116357; AT4G27040.
DR eggNOG; KOG3341; Eukaryota.
DR HOGENOM; CLU_070147_2_0_1; -.
DR InParanoid; Q5M759; -.
DR OMA; SNTEQGC; -.
DR OrthoDB; 869548at2759; -.
DR PRO; PR:Q5M759; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5M759; baseline and differential.
DR Genevisible; Q5M759; AT.
DR GO; GO:0000814; C:ESCRT II complex; ISS:TAIR.
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; -; 2.
DR InterPro; IPR016689; ESCRT-2_cplx_Snf8.
DR InterPro; IPR040608; Snf8/Vps36.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12806; PTHR12806; 1.
DR Pfam; PF04157; EAP30; 1.
DR PIRSF; PIRSF017215; ESCRT2_Vps22; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 2: Evidence at transcript level;
KW Coiled coil; Endosome; Protein transport; Reference proteome; Transport.
FT CHAIN 1..250
FT /note="Vacuolar protein sorting-associated protein 22
FT homolog 1"
FT /id="PRO_0000368191"
FT COILED 35..55
FT /evidence="ECO:0000255"
FT CONFLICT 17
FT /note="R -> G (in Ref. 4; AAV91335/AAW70398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 250 AA; 28310 MW; 0BED008163F0C744 CRC64;
MRRRPGIGGL QKAAAARDQY RLLGENVAKL RTDMMKEQLS TFRSQLEEFA RKHKNDIRKN
PAFRAQFHEM CANIGVDPLA SNKGFWAELL GIGDFYYELG VQIIEVCMLT RSHNGGLISL
QELCNHLRQR RKKDREAVTE DDCLRAISKL KVLGSGFEVI TIGKKKLVRS VPTELNKDHN
QILELAQGQG FVIVEEVQRR LSWTSGRVID ALETLLEEGL AMIDNGHKDG KCRYWFPCVS
SVYSSIGSDT
