VP601_ARATH
ID VP601_ARATH Reviewed; 235 AA.
AC Q9LPN5; Q9CAF3;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Vacuolar protein sorting-associated protein 60.1 {ECO:0000305};
GN Name=VPS60-1 {ECO:0000305}; Synonyms=VPS60A {ECO:0000303|PubMed:22639582};
GN OrderedLocusNames=At3g10640 {ECO:0000312|Araport:AT3G10640};
GN ORFNames=F13M14.7 {ECO:0000312|EMBL:AAG51378.1},
GN F18K10.26 {ECO:0000312|EMBL:AAF76370.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, AND REVIEW.
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 [6]
RP INTERACTION WITH SKD1 AND LIP5, AND SUBCELLULAR LOCATION.
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 [7]
RP GENE FAMILY, AND NOMENCLATURE.
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 [8]
RP INTERACTION WITH VPS2.2.
RX PubMed=22010978; DOI=10.1021/pr200845n;
RA Ibl V., Csaszar E., Schlager N., Neubert S., Spitzer C., Hauser M.T.;
RT "Interactome of the plant-specific ESCRT-III component AtVPS2.2 in
RT Arabidopsis thaliana.";
RL J. Proteome Res. 11:397-411(2012).
CC -!- FUNCTION: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III) which is
CC involved in multivesicular bodies (MVBs) formation and sorting of
CC endosomal cargo proteins into MVBs. {ECO:0000305|PubMed:16488176}.
CC -!- SUBUNIT: Interacts with SKD1/VPS4 AND LIP5 (PubMed:20663085). Interacts
CC with VPS2.2 (PubMed:22010978). {ECO:0000269|PubMed:20663085,
CC ECO:0000269|PubMed:22010978}.
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC {ECO:0000269|PubMed:20663085}; Peripheral membrane protein
CC {ECO:0000305}. Note=Localized in multivesicular body when associated
CC with SKD1. {ECO:0000269|PubMed:20663085}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist. {ECO:0000305};
CC Name=1;
CC IsoId=Q9LPN5-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51378.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC011560; AAG51378.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC013428; AAF76370.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74937.1; -; Genomic_DNA.
DR EMBL; BT005859; AAO64794.1; -; mRNA.
DR EMBL; AK228223; BAF00173.1; -; mRNA.
DR RefSeq; NP_187675.2; NM_111900.5. [Q9LPN5-1]
DR AlphaFoldDB; Q9LPN5; -.
DR SMR; Q9LPN5; -.
DR IntAct; Q9LPN5; 259.
DR STRING; 3702.AT3G10640.1; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR PaxDb; Q9LPN5; -.
DR PRIDE; Q9LPN5; -.
DR ProteomicsDB; 242447; -. [Q9LPN5-1]
DR EnsemblPlants; AT3G10640.1; AT3G10640.1; AT3G10640. [Q9LPN5-1]
DR GeneID; 820233; -.
DR Gramene; AT3G10640.1; AT3G10640.1; AT3G10640. [Q9LPN5-1]
DR KEGG; ath:AT3G10640; -.
DR Araport; AT3G10640; -.
DR TAIR; locus:2075800; AT3G10640.
DR eggNOG; KOG1655; Eukaryota.
DR HOGENOM; CLU_079409_0_0_1; -.
DR InParanoid; Q9LPN5; -.
DR OMA; KNMVKQR; -.
DR PhylomeDB; Q9LPN5; -.
DR PRO; PR:Q9LPN5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LPN5; baseline and differential.
DR GO; GO:0005771; C:multivesicular body; IDA:UniProtKB.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
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; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..235
FT /note="Vacuolar protein sorting-associated protein 60.1"
FT /id="PRO_0000440685"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 99..148
FT /evidence="ECO:0000255"
SQ SEQUENCE 235 AA; 26170 MW; C875290A3B86AF8E CRC64;
MRRVFGAKKN TEPPPSIQDA SDRINKRGDS VEDKIKKLDV ELCKYKEQLK KTRPGPAQEA
VKARAMRVLK QKKMYEGQRD MLYNQTFNLD QVSFAAEGLK DAQQTMTALK SANKELKGMM
KTVKIQDIDN LQDEMMDLMD VSSEIQESLG RSYNIPDGLD EDDLMGELDA LEADMGNETE
ADGMPSYLQP DTETDYDSEL NLPAAPTGHN GAPHGRAQAE DEFGLPAVPR ASLRG
