VP53A_ARATH
ID VP53A_ARATH Reviewed; 828 AA.
AC Q0WQF4; F4I6I4; Q9C6Q3; Q9LPS3;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Vacuolar protein sorting-associated protein 53 A;
DE Short=AtVPS53;
DE AltName: Full=Protein HEAT-INTOLERANT 1;
GN Name=VPS53; Synonyms=HIT1; OrderedLocusNames=At1g50500;
GN ORFNames=F11F12.15, F17J6.4;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
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 [4]
RP FUNCTION, AND MUTAGENESIS OF SER-393.
RC STRAIN=cv. Columbia GL1;
RX DOI=10.1016/S0176-1617(00)80110-8;
RA Wu S.-J., Locy R.D., Shaw J.J., Cherry J.H., Singh N.K.;
RT "Mutation in Arabidopsis HIT1 locus causing heat and osmotic
RT hypersensitivity.";
RL J. Plant Physiol. 157:543-547(2000).
RN [5]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15235115; DOI=10.1104/pp.103.037747;
RA Lobstein E., Guyon A., Ferault M., Twell D., Pelletier G., Bonhomme S.;
RT "The putative Arabidopsis homolog of yeast vps52p is required for pollen
RT tube elongation, localizes to Golgi, and might be involved in vesicle
RT trafficking.";
RL Plant Physiol. 135:1480-1490(2004).
RN [6]
RP FUNCTION, MUTAGENESIS OF SER-393, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16408208; DOI=10.1007/s00425-005-0216-6;
RA Lee C.-F., Pu H.-Y., Wang L.-C., Sayler R.J., Yeh C.-H., Wu S.-J.;
RT "Mutation in a homolog of yeast Vps53p accounts for the heat and osmotic
RT hypersensitive phenotypes in Arabidopsis hit1-1 mutant.";
RL Planta 224:330-338(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18583349; DOI=10.1093/jxb/ern162;
RA Guermonprez H., Smertenko A., Crosnier M.-T., Durandet M., Vrielynck N.,
RA Guerche P., Hussey P.J., Satiat-Jeunemaitre B., Bonhomme S.;
RT "The POK/AtVPS52 protein localizes to several distinct post-Golgi
RT compartments in sporophytic and gametophytic cells.";
RL J. Exp. Bot. 59:3087-3098(2008).
RN [8]
RP FUNCTION, MUTAGENESIS OF SER-393, SUBCELLULAR LOCATION, SUBUNIT, AND
RP INTERACTION WITH VPS52 AND VPS54.
RC STRAIN=cv. Columbia;
RX PubMed=21398432; DOI=10.1093/jxb/err060;
RA Wang L.-C., Tsai M.-C., Chang K.-Y., Fan Y.-S., Yeh C.-H., Wu S.-J.;
RT "Involvement of the Arabidopsis HIT1/AtVPS53 tethering protein homologue in
RT the acclimation of the plasma membrane to heat stress.";
RL J. Exp. Bot. 62:3609-3620(2011).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF SER-393.
RC STRAIN=cv. Columbia;
RX PubMed=21758000; DOI=10.4161/psb.6.8.15842;
RA Wang L.-C., Chang K.-Y., Ke Y.-T., Huang H.-Y., Wu S.-J.;
RT "The Arabidopsis hit1-1 mutant has a plasma membrane profile distinct from
RT that of wild-type plants at optimal growing temperature.";
RL Plant Signal. Behav. 6:1205-1206(2011).
CC -!- FUNCTION: Acts as component of the GARP complex that is involved in
CC retrograde transport from early and late endosomes to the trans-Golgi
CC network (TGN). The GARP complex facilitates tethering as well as SNARE
CC complex assembly at the Golgi (By similarity). Required for vesicle
CC trafficking involved in plasma membrane protein composition. Probably
CC involved in pollen tube elongation and other polar growth. Confers
CC basal tolerance to long-term heat stress and osmotic stress, by
CC acclimation of the plasma membrane. {ECO:0000250,
CC ECO:0000269|PubMed:16408208, ECO:0000269|PubMed:18583349,
CC ECO:0000269|PubMed:21398432, ECO:0000269|PubMed:21758000,
CC ECO:0000269|Ref.4}.
CC -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC complex, composed by VPS52, VPS53 and VPS54. Interacts directly with
CC VPS52 and VPS54. {ECO:0000269|PubMed:21398432}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21398432}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:21398432}; Peripheral membrane
CC protein {ECO:0000269|PubMed:21398432}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000269|PubMed:21398432}; Peripheral membrane
CC protein {ECO:0000269|PubMed:21398432}. Endosome membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=Localized in the GARP
CC complex in the Golgi and post-Golgi compartments.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0WQF4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0WQF4-2; Sequence=VSP_053514;
CC -!- TISSUE SPECIFICITY: Present in pollen. Mostly expressed in vegetative
CC tissues, including leaves, siliques, and stems, and flower buds, and,
CC at lower levels, in roots and mature flowers.
CC {ECO:0000269|PubMed:15235115, ECO:0000269|PubMed:16408208}.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous. In hemizygous plants,
CC male-specific transmission defect. {ECO:0000269|PubMed:16408208,
CC ECO:0000269|PubMed:18583349}.
CC -!- SIMILARITY: Belongs to the VPS53 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87884.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51191.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC012561; AAF87884.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC079279; AAG51191.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32557.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32558.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60116.1; -; Genomic_DNA.
DR EMBL; AK228745; BAF00645.1; -; mRNA.
DR PIR; E96541; E96541.
DR RefSeq; NP_001185188.1; NM_001198259.1. [Q0WQF4-2]
DR RefSeq; NP_001322424.1; NM_001333440.1. [Q0WQF4-1]
DR RefSeq; NP_564573.3; NM_103933.6. [Q0WQF4-1]
DR AlphaFoldDB; Q0WQF4; -.
DR SMR; Q0WQF4; -.
DR BioGRID; 26697; 3.
DR STRING; 3702.AT1G50500.2; -.
DR iPTMnet; Q0WQF4; -.
DR PaxDb; Q0WQF4; -.
DR PRIDE; Q0WQF4; -.
DR EnsemblPlants; AT1G50500.1; AT1G50500.1; AT1G50500. [Q0WQF4-1]
DR EnsemblPlants; AT1G50500.2; AT1G50500.2; AT1G50500. [Q0WQF4-2]
DR EnsemblPlants; AT1G50500.3; AT1G50500.3; AT1G50500. [Q0WQF4-1]
DR GeneID; 841472; -.
DR Gramene; AT1G50500.1; AT1G50500.1; AT1G50500. [Q0WQF4-1]
DR Gramene; AT1G50500.2; AT1G50500.2; AT1G50500. [Q0WQF4-2]
DR Gramene; AT1G50500.3; AT1G50500.3; AT1G50500. [Q0WQF4-1]
DR KEGG; ath:AT1G50500; -.
DR Araport; AT1G50500; -.
DR TAIR; locus:2015826; AT1G50500.
DR eggNOG; KOG2180; Eukaryota.
DR HOGENOM; CLU_007339_0_0_1; -.
DR OrthoDB; 1379600at2759; -.
DR PhylomeDB; Q0WQF4; -.
DR PRO; PR:Q0WQF4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WQF4; baseline and differential.
DR Genevisible; Q0WQF4; AT.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000938; C:GARP complex; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0007009; P:plasma membrane organization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS:TAIR.
DR Gene3D; 1.10.357.110; -; 1.
DR InterPro; IPR039766; Vps53.
DR InterPro; IPR038260; Vps53_C_sf.
DR InterPro; IPR007234; Vps53_N.
DR PANTHER; PTHR12820; PTHR12820; 1.
DR Pfam; PF04100; Vps53_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Endosome; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..828
FT /note="Vacuolar protein sorting-associated protein 53 A"
FT /id="PRO_0000424845"
FT COILED 53..152
FT /evidence="ECO:0000255"
FT VAR_SEQ 15
FT /note="P -> PTVSAYVTAFTMIFKCVFSF (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053514"
FT MUTAGEN 393
FT /note="S->Y: In hit1-1; reduced tolerance to both heat and
FT water stress, lethal at 37 degrees Celsius. Altered vesicle
FT trafficking leading in changes in the plasma membrane
FT components. Less stable plasma membrane under heat stress
FT conditions, leading to heat intolerance; this sensitivity
FT to heat depends more of the duration than of the intensity
FT of the stress."
FT /evidence="ECO:0000269|PubMed:16408208,
FT ECO:0000269|PubMed:21398432, ECO:0000269|PubMed:21758000,
FT ECO:0000269|Ref.4"
SQ SEQUENCE 828 AA; 92530 MW; 2E33D943FEABE5F1 CRC64;
MDKSSALEYI NQMFPTEASL TGVEPLMQKI QGEIRRVDAS ILSAVRQQSN SGTKAKEDLA
DATRAVEELS HKIQEIKSKA EQSEAMVQEI CRDIKKLDFA KKNITTTITA LHRLTMLVSA
VEQLQVMASK RQYKEAAAQL EAVNQLCNHF EAYRDVPKIT ELREKLNNIK QILKSHVFSD
FSSLGTGKET EETNLLQKLS DSCLVVDALE PSVREELVNN FCSRELTSYE QIFEGAELAK
LDKTERRYAW IKRRIRTNEE IWKIFPASWH VPYRLCIQFC KQTRKQVESI LVNMKEKPVV
AILLLALQST VEFEKELEKK FGGGVPTKDI EDDIEEIGTW EDNSQNISKI RKKYEKKFAA
SQETEENGFQ QEKTGNKDLS VTGAGFNFRG MISSCFEPHL TPYIELEEKT LMDDLEKIVQ
EESWDVEDGS QNNVLSSSTQ LFSNIKKSLK RCNTLSKNQT LFNLFKVFQR VLKAYATKLF
FKLPKGGTGI VAAATGMDGQ IKVSERDERV ICYIVNSAEY CHKTSGELAE NVSEIIDPHY
ADGVDMSEVQ DEFSAVITKA LVTLVLGLET KFDTEMAVMT RVPWSTLESV GDQSGYVNGI
NTVLSGSIPV LGKLLTPVYF QFFLDKLASS LGPRFYANIF RCKQLSETGA QQMLLDTQAV
KSILLEIPSL ARQTSTAASY SKFVSREMSR AEALLKVILS PIDSVADTYR ALFPEGTPME
FQRILELKGL KKADQQSILD DFNKHGPGFT QQSVAAAMPQ PMPTPPAPPL AITNPATAAG
FIANSEDVLT RAAALGRGAA STGFKKFIAL TEAAKDRKDG PLRRLFNA
