VP202_ARATH
ID VP202_ARATH Reviewed; 216 AA.
AC Q9FY89;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Vacuolar protein sorting-associated protein 20 homolog 2;
DE Short=AtVPS20-2;
DE AltName: Full=Charged multivesicular body protein 6 homolog 2;
DE AltName: Full=ESCRT-III complex subunit VPS20 homolog 2;
GN Name=VPS20.2; Synonyms=CHMP6-2; OrderedLocusNames=At5g09260;
GN ORFNames=T2K12.4, T5E8.60;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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;
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 (SEP-2004) 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).
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 {ECO:0000250|UniProtKB:Q96FZ7, ECO:0000269|PubMed:20663085}.
CC -!- INTERACTION:
CC Q9FY89; Q8GXN6: VPS20.1; NbExp=4; IntAct=EBI-3865360, EBI-3865286;
CC Q9FY89; Q8VZC9: VPS25; NbExp=7; IntAct=EBI-3865360, EBI-3865350;
CC Q9FY89; O82197: VPS32.1; NbExp=3; IntAct=EBI-3865360, EBI-3865938;
CC Q9FY89; Q9SZE4: VPS32.2; NbExp=3; IntAct=EBI-3865360, EBI-3865953;
CC Q9FY89; Q9FF81: VPS36; NbExp=5; IntAct=EBI-3865360, EBI-3865302;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; AL391712; CAC05452.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91366.1; -; Genomic_DNA.
DR EMBL; BT010522; AAQ65145.1; -; mRNA.
DR EMBL; AK175654; BAD43417.1; -; mRNA.
DR RefSeq; NP_196488.1; NM_120962.3.
DR AlphaFoldDB; Q9FY89; -.
DR SMR; Q9FY89; -.
DR BioGRID; 16063; 10.
DR DIP; DIP-61573N; -.
DR IntAct; Q9FY89; 9.
DR STRING; 3702.AT5G09260.1; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR PaxDb; Q9FY89; -.
DR PRIDE; Q9FY89; -.
DR ProteomicsDB; 242666; -.
DR EnsemblPlants; AT5G09260.1; AT5G09260.1; AT5G09260.
DR GeneID; 830785; -.
DR Gramene; AT5G09260.1; AT5G09260.1; AT5G09260.
DR KEGG; ath:AT5G09260; -.
DR Araport; AT5G09260; -.
DR TAIR; locus:2184767; AT5G09260.
DR eggNOG; KOG2910; Eukaryota.
DR HOGENOM; CLU_086201_1_0_1; -.
DR InParanoid; Q9FY89; -.
DR OMA; GTIEFKL; -.
DR OrthoDB; 1287094at2759; -.
DR PhylomeDB; Q9FY89; -.
DR PRO; PR:Q9FY89; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FY89; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0000815; C:ESCRT III complex; ISS:TAIR.
DR GO; GO:0005770; C:late endosome; IDA:TAIR.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA: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 Coiled coil; Endosome; Lipoprotein; Membrane; Myristate; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..216
FT /note="Vacuolar protein sorting-associated protein 20
FT homolog 2"
FT /id="PRO_0000368203"
FT REGION 173..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..90
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 216 AA; 24609 MW; 710C1780459BDF72 CRC64;
MGNLFVKKPK ITEVDRAILS LKTQRRKLGQ YQQQLEKVIE AEKQAARDLI REKRKDRALL
ALKKKRTQEE LLKQVDQWLI NVEQQLADIE LTSKQKAVFE SLKQGNNAIK AIQSEVNLDD
VQKLMDDTAE AKAYQDELSA ILGEKLSAED EEEILAEFDN LESLLIVEDM PEVPTTELMP
EEPEKMDLPD VPTKAPVASN ETTSTKRKVL EEPLEA
