位置:首页 > 蛋白库 > VP321_ARATH
VP321_ARATH
ID   VP321_ARATH             Reviewed;         213 AA.
AC   O82197;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Vacuolar protein sorting-associated protein 32 homolog 1;
DE            Short=AtVPS32-1;
DE   AltName: Full=Charged multivesicular body protein 4 homolog 1;
DE   AltName: Full=ESCRT-III complex subunit VPS32 homolog 1;
GN   Name=VPS32.1; Synonyms=CHMP4-1, SNF7A {ECO:0000303|PubMed:22639582};
GN   OrderedLocusNames=At2g19830; ORFNames=F6F22.14;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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, 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   [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).
RN   [6]
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).
RN   [7]
RP   NOMENCLATURE, AND INTERACTION WITH BRO1.
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 BRO1.
RX   PubMed=26342016; DOI=10.1105/tpc.15.00393;
RA   Cardona-Lopez X., Cuyas L., Marin E., Rajulu C., Irigoyen M.L., Gil E.,
RA   Puga M.I., Bligny R., Nussaume L., Geldner N., Paz-Ares J., Rubio V.;
RT   "ESCRT-III-associated protein ALIX mediates high-affinity phosphate
RT   transporter trafficking to maintain phosphate homeostasis in Arabidopsis.";
RL   Plant Cell 27:2560-2581(2015).
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). Interacts
CC       with BRO1/ALIX (PubMed:22639582, PubMed:26342016).
CC       {ECO:0000250|UniProtKB:Q9H444, ECO:0000269|PubMed:20663085,
CC       ECO:0000269|PubMed:22639582, ECO:0000269|PubMed:26342016}.
CC   -!- INTERACTION:
CC       O82197; Q8GXN6: VPS20.1; NbExp=4; IntAct=EBI-3865938, EBI-3865286;
CC       O82197; Q9FY89: VPS20.2; NbExp=3; IntAct=EBI-3865938, EBI-3865360;
CC       O82197; Q9SZE4: VPS32.2; NbExp=4; IntAct=EBI-3865938, EBI-3865953;
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {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; AC005169; AAC62133.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61252.1; -; Genomic_DNA.
DR   EMBL; AY045911; AAK76585.1; -; mRNA.
DR   EMBL; AY079421; AAL85152.1; -; mRNA.
DR   PIR; F84581; F84581.
DR   RefSeq; NP_179573.1; NM_127541.5.
DR   AlphaFoldDB; O82197; -.
DR   SMR; O82197; -.
DR   BioGRID; 1857; 11.
DR   IntAct; O82197; 6.
DR   STRING; 3702.AT2G19830.1; -.
DR   TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR   MetOSite; O82197; -.
DR   PaxDb; O82197; -.
DR   PRIDE; O82197; -.
DR   ProteomicsDB; 242625; -.
DR   EnsemblPlants; AT2G19830.2; AT2G19830.2; AT2G19830.
DR   GeneID; 816502; -.
DR   Gramene; AT2G19830.2; AT2G19830.2; AT2G19830.
DR   KEGG; ath:AT2G19830; -.
DR   Araport; AT2G19830; -.
DR   TAIR; locus:2051970; AT2G19830.
DR   eggNOG; KOG1656; Eukaryota.
DR   HOGENOM; CLU_071097_2_0_1; -.
DR   InParanoid; O82197; -.
DR   OMA; EHKIQQE; -.
DR   OrthoDB; 1490465at2759; -.
DR   PhylomeDB; O82197; -.
DR   PRO; PR:O82197; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O82197; baseline and differential.
DR   Genevisible; O82197; AT.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0000815; C:ESCRT III complex; ISS:TAIR.
DR   GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
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; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..213
FT                   /note="Vacuolar protein sorting-associated protein 32
FT                   homolog 1"
FT                   /id="PRO_0000368200"
FT   REGION          180..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          11..42
FT                   /evidence="ECO:0000255"
FT   COILED          118..176
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   213 AA;  24014 MW;  FB7EBA169C56F1EC CRC64;
     MFMNRLFGKP KQETSTLQTL DKLNETLEML EKKENVLLKK ATGEVEKAKE FSRAKNKRAA
     IQCLKRKRLY EQQVEQLGNF QLRIHDQMIM LEGAKATTET VDALRTGASA MKAMQKATNI
     DDVDKTMDEI NEQTENMKQI QEALSAPFGA NDFDEDELEA ELDELEGAEL EEQLLQPVPI
     HVPQGNKPAR APAQKQPTAE EDELAALQAE MAL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024