VP52A_ARATH
ID VP52A_ARATH Reviewed; 707 AA.
AC Q94KD3; Q56WP0; Q68EC6; Q9FVV3;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Vacuolar protein sorting-associated protein 52 A;
DE Short=AtVPS52;
DE AltName: Full=ARE1-like protein POK;
DE AltName: Full=Protein POKY POLLEN TUBE;
DE AltName: Full=Protein T-DNA TRANSMISSION DEFECT 8;
GN Name=VPS52; Synonyms=POK, TTD8; OrderedLocusNames=At1g71270;
GN ORFNames=F3I17.8;
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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY, AND
RP 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 [2]
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 [3]
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 [4]
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 [5]
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP SUBUNIT, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19490533; DOI=10.1111/j.1600-0854.2009.00930.x;
RA Osterrieder A., Carvalho C.M., Latijnhouwers M., Johansen J.N., Stubbs C.,
RA Botchway S., Hawes C.;
RT "Fluorescence lifetime imaging of interactions between Golgi tethering
RT factors and small GTPases in plants.";
RL Traffic 10:1034-1046(2009).
RN [8]
RP SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH VPS53.
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 INTERACTION WITH VPS51.
RC STRAIN=cv. Columbia;
RX PubMed=24757006; DOI=10.1242/dev.099333;
RA Pahari S., Cormark R.D., Blackshaw M.T., Liu C., Erickson J.L.,
RA Schultz E.A.;
RT "Arabidopsis UNHINGED encodes a VPS51 homolog and reveals a role for the
RT GARP complex in leaf shape and vein patterning.";
RL Development 141:1894-1905(2014).
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 pollen tube
CC elongation and other polar growth. {ECO:0000250,
CC ECO:0000269|PubMed:15235115, ECO:0000269|PubMed:18583349}.
CC -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC complex, composed by VPS52, VPS53 and VPS54. Interacts directly with
CC VPS53. Binds to VPS51 (PubMed:24757006). {ECO:0000269|PubMed:18583349,
CC ECO:0000269|PubMed:21398432, ECO:0000269|PubMed:24757006}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane;
CC Peripheral membrane protein. Endosome membrane; Peripheral membrane
CC protein. Golgi apparatus membrane; Peripheral membrane protein.
CC Note=Localized in the GARP complex in the Golgi and post-Golgi
CC compartments.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and flower buds, and, at
CC low levels, in seeds, whole inflorescence and mature flowers. Also
CC detected in pollen. Present in pollen, buds, leaves, and roots (at
CC protein level). {ECO:0000269|PubMed:15235115,
CC ECO:0000269|PubMed:18583349}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, expressed in the root apex, mostly
CC in the elongation zone and emerging lateral root primordia, in very
CC young leaves and stipules. In flowers, detected from the earliest
CC stages of flower development, before meiosis and gametogenesis and
CC maintained later. As flower bud size reaches 1.6 to 1.7 mm, confined to
CC male gametophytic tissues and female sporophytic tissues, including
CC ovules. At maturity, accumulates in pollen grains within the anthers.
CC At later postpollination stages, expressed in developing seeds.
CC Accumulates in intracellular compartments in both sporophytic and
CC gametophytic tissues (at protein level). {ECO:0000269|PubMed:15235115,
CC ECO:0000269|PubMed:18583349}.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous. In hemizygous plants,
CC male gametophytic mutants characterized by very short pollen tubes.
CC Male-specific transmission defect. {ECO:0000269|PubMed:15235115,
CC ECO:0000269|PubMed:18583349}.
CC -!- SIMILARITY: Belongs to the VPS52 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51892.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD94582.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BK000522; DAA01355.1; -; mRNA.
DR EMBL; AC016162; AAG51892.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35182.1; -; Genomic_DNA.
DR EMBL; AF367286; AAK56274.1; -; mRNA.
DR EMBL; BT004525; AAO42771.1; -; mRNA.
DR EMBL; AK221995; BAD94582.1; ALT_INIT; mRNA.
DR PIR; D96737; D96737.
DR RefSeq; NP_565015.1; NM_105796.3.
DR AlphaFoldDB; Q94KD3; -.
DR SMR; Q94KD3; -.
DR BioGRID; 28688; 4.
DR STRING; 3702.AT1G71270.1; -.
DR PaxDb; Q94KD3; -.
DR PRIDE; Q94KD3; -.
DR ProteomicsDB; 242646; -.
DR EnsemblPlants; AT1G71270.1; AT1G71270.1; AT1G71270.
DR GeneID; 843468; -.
DR Gramene; AT1G71270.1; AT1G71270.1; AT1G71270.
DR KEGG; ath:AT1G71270; -.
DR Araport; AT1G71270; -.
DR TAIR; locus:2032343; AT1G71270.
DR eggNOG; KOG1961; Eukaryota.
DR HOGENOM; CLU_010797_0_1_1; -.
DR InParanoid; Q94KD3; -.
DR OMA; IHVVMVE; -.
DR OrthoDB; 158568at2759; -.
DR PhylomeDB; Q94KD3; -.
DR PRO; PR:Q94KD3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94KD3; baseline and differential.
DR Genevisible; Q94KD3; AT.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000938; C:GARP complex; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0019953; P:sexual reproduction; IMP:TAIR.
DR InterPro; IPR007258; Vps52.
DR PANTHER; PTHR14190; PTHR14190; 1.
DR Pfam; PF04129; Vps52; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endosome; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..707
FT /note="Vacuolar protein sorting-associated protein 52 A"
FT /id="PRO_0000424843"
FT COILED 181..203
FT /evidence="ECO:0000255"
FT CONFLICT 179
FT /note="D -> G (in Ref. 1; DAA01355)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="T -> P (in Ref. 1; DAA01355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 80938 MW; 030C26D60A9A2E9F CRC64;
MSDISIDALG QTMGDFSNHE KLGFDLGAFV GDLAFEEDSG SEDISLEGLQ QELEECESDE
VVANILSSGD KLREYAKGVE NNLRKVELDS IEDYIKESDN LVSLHDQIRD CDSILSQMET
LLSGFQEEIG SISSDIKILQ EKSMDMGLRL KNRRVAESKL AKFVEDIIVP PKMIDVIVDG
EVNEEYMKTL EILSKKLKFV EADQAVKSSK ALKDVEPELE KLRQKAISKV YDFIVQKLIA
LRKPKTNIQI LQQSVLLKYK YIISFLKEHG KEVFMDVRAA YIDTMNKVLS AHFRAYIQAL
EKLQLDIATA YDLIGVETRT TGLFSRAREP LKNRSAVFAL GDRIKIIKDI DQPALIPHIA
EASSLKYPYE VLFRSLHKLL MDTATSEYMF CDDFFGEESI FYEIFAGPFS VIDEHFNPVL
SNCFDAIGLM LMIRIIHHHQ LIMSRRRIPC LDSYLDKVNI SLWPRFKMVF DSHLSSLRDA
NIKTLWEDDV HPHYVMRRYA EFTASFIHLN VEYGDGQLDI NLERLRMAVD GLILKLAKLF
PRPKQQIVFL INNYDMTIAV LKEAGPEGGK IQMHFEEMLK SNTSLFVEEL LVEHFSDLIK
FVKNRASEDS SLNPERSITI AEVEPLVKDF GSRWKTAIEL MDKDIITSFS NFLCGMDILR
AALTQLLLYY TRLTDCIKKI DGGSALNRDL VSIQSIMYEI RKYSKTF
