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Vacuolar protein sorting-associated protein 52 A (AtVPS52) (ARE1-like protein POK) (Protein POKY POLLEN TUBE) (Protein T-DNA TRANSMISSION DEFECT 8)

 VP52A_ARATH             Reviewed;         707 AA.
Q94KD3; Q56WP0; Q68EC6; Q9FVV3;
22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-APR-2018, entry version 87.
RecName: Full=Vacuolar protein sorting-associated protein 52 A;
Short=AtVPS52;
AltName: Full=ARE1-like protein POK;
AltName: Full=Protein POKY POLLEN TUBE;
AltName: Full=Protein T-DNA TRANSMISSION DEFECT 8;
Name=VPS52; Synonyms=POK, TTD8; OrderedLocusNames=At1g71270;
ORFNames=F3I17.8;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE
FAMILY, AND NOMENCLATURE.
PubMed=15235115; DOI=10.1104/pp.103.037747;
Lobstein E., Guyon A., Ferault M., Twell D., Pelletier G.,
Bonhomme S.;
"The putative Arabidopsis homolog of yeast vps52p is required for
pollen tube elongation, localizes to Golgi, and might be involved in
vesicle trafficking.";
Plant Physiol. 135:1480-1490(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, SUBUNIT, AND DEVELOPMENTAL STAGE.
STRAIN=cv. Columbia, and cv. Wassilewskija;
PubMed=18583349; DOI=10.1093/jxb/ern162;
Guermonprez H., Smertenko A., Crosnier M.-T., Durandet M.,
Vrielynck N., Guerche P., Hussey P.J., Satiat-Jeunemaitre B.,
Bonhomme S.;
"The POK/AtVPS52 protein localizes to several distinct post-Golgi
compartments in sporophytic and gametophytic cells.";
J. Exp. Bot. 59:3087-3098(2008).
[7]
SUBCELLULAR LOCATION.
PubMed=19490533; DOI=10.1111/j.1600-0854.2009.00930.x;
Osterrieder A., Carvalho C.M., Latijnhouwers M., Johansen J.N.,
Stubbs C., Botchway S., Hawes C.;
"Fluorescence lifetime imaging of interactions between Golgi tethering
factors and small GTPases in plants.";
Traffic 10:1034-1046(2009).
[8]
SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH VPS53.
PubMed=21398432; DOI=10.1093/jxb/err060;
Wang L.-C., Tsai M.-C., Chang K.-Y., Fan Y.-S., Yeh C.-H., Wu S.-J.;
"Involvement of the Arabidopsis HIT1/AtVPS53 tethering protein
homologue in the acclimation of the plasma membrane to heat stress.";
J. Exp. Bot. 62:3609-3620(2011).
[9]
INTERACTION WITH VPS51.
STRAIN=cv. Columbia;
PubMed=24757006; DOI=10.1242/dev.099333;
Pahari S., Cormark R.D., Blackshaw M.T., Liu C., Erickson J.L.,
Schultz E.A.;
"Arabidopsis UNHINGED encodes a VPS51 homolog and reveals a role for
the GARP complex in leaf shape and vein patterning.";
Development 141:1894-1905(2014).
-!- FUNCTION: Acts as component of the GARP complex that is involved
in retrograde transport from early and late endosomes to the
trans-Golgi network (TGN). The GARP complex facilitates tethering
as well as SNARE complex assembly at the Golgi (By similarity).
Required for pollen tube elongation and other polar growth.
{ECO:0000250, ECO:0000269|PubMed:15235115,
ECO:0000269|PubMed:18583349}.
-!- SUBUNIT: Component of the Golgi-associated retrograde protein
(GARP) complex, composed by VPS52, VPS53 and VPS54. Interacts
directly with VPS53. Binds to VPS51 (PubMed:24757006).
{ECO:0000269|PubMed:18583349, ECO:0000269|PubMed:21398432,
ECO:0000269|PubMed:24757006}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane; Peripheral membrane protein. Endosome membrane;
Peripheral membrane protein. Golgi apparatus membrane; Peripheral
membrane protein. Note=Localized in the GARP complex in the Golgi
and post-Golgi compartments.
-!- TISSUE SPECIFICITY: Mostly expressed in roots and flower buds,
and, at low levels, in seeds, whole inflorescence and mature
flowers. Also detected in pollen. Present in pollen, buds, leaves,
and roots (at protein level). {ECO:0000269|PubMed:15235115,
ECO:0000269|PubMed:18583349}.
-!- DEVELOPMENTAL STAGE: In seedlings, expressed in the root apex,
mostly in the elongation zone and emerging lateral root primordia,
in very young leaves and stipules. In flowers, detected from the
earliest stages of flower development, before meiosis and
gametogenesis and maintained later. As flower bud size reaches 1.6
to 1.7 mm, confined to male gametophytic tissues and female
sporophytic tissues, including ovules. At maturity, accumulates in
pollen grains within the anthers. At later postpollination stages,
expressed in developing seeds. Accumulates in intracellular
compartments in both sporophytic and gametophytic tissues (at
protein level). {ECO:0000269|PubMed:15235115,
ECO:0000269|PubMed:18583349}.
-!- DISRUPTION PHENOTYPE: Lethal when homozygous. In hemizygous
plants, male gametophytic mutants characterized by very short
pollen tubes. Male-specific transmission defect.
{ECO:0000269|PubMed:15235115, ECO:0000269|PubMed:18583349}.
-!- SIMILARITY: Belongs to the VPS52 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG51892.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAD94582.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; BK000522; DAA01355.1; -; mRNA.
EMBL; AC016162; AAG51892.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE35182.1; -; Genomic_DNA.
EMBL; AF367286; AAK56274.1; -; mRNA.
EMBL; BT004525; AAO42771.1; -; mRNA.
EMBL; AK221995; BAD94582.1; ALT_INIT; mRNA.
PIR; D96737; D96737.
RefSeq; NP_565015.1; NM_105796.3.
UniGene; At.23282; -.
ProteinModelPortal; Q94KD3; -.
SMR; Q94KD3; -.
BioGrid; 28688; 4.
STRING; 3702.AT1G71270.1; -.
PaxDb; Q94KD3; -.
PRIDE; Q94KD3; -.
EnsemblPlants; AT1G71270.1; AT1G71270.1; AT1G71270.
GeneID; 843468; -.
Gramene; AT1G71270.1; AT1G71270.1; AT1G71270.
KEGG; ath:AT1G71270; -.
Araport; AT1G71270; -.
TAIR; locus:2032343; AT1G71270.
eggNOG; KOG1961; Eukaryota.
eggNOG; ENOG410XNZ1; LUCA.
HOGENOM; HOG000020960; -.
InParanoid; Q94KD3; -.
KO; K20298; -.
OMA; YKFRKPM; -.
OrthoDB; EOG093603ZC; -.
PhylomeDB; Q94KD3; -.
PRO; PR:Q94KD3; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q94KD3; baseline and differential.
Genevisible; Q94KD3; AT.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0012505; C:endomembrane system; IDA:TAIR.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0000938; C:GARP complex; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; IBA:GO_Central.
GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
GO; GO:0019953; P:sexual reproduction; IMP:TAIR.
InterPro; IPR007258; Vps52.
PANTHER; PTHR14190; PTHR14190; 1.
Pfam; PF04129; Vps52; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Endosome; Golgi apparatus; Membrane;
Protein transport; Reference proteome; Transport.
CHAIN 1 707 Vacuolar protein sorting-associated
protein 52 A.
/FTId=PRO_0000424843.
COILED 181 203 {ECO:0000255}.
CONFLICT 179 179 D -> G (in Ref. 1; DAA01355).
{ECO:0000305}.
CONFLICT 583 583 T -> P (in Ref. 1; DAA01355).
{ECO:0000305}.
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


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