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Chaperone protein dnaJ 15 (AtDjB15) (AtJ15) (Protein ALTERED RESPONSE TO GRAVITY) (AtARG1)

 DNJ15_ARATH             Reviewed;         410 AA.
Q9ZSY2;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 117.
RecName: Full=Chaperone protein dnaJ 15;
Short=AtDjB15;
Short=AtJ15;
AltName: Full=Protein ALTERED RESPONSE TO GRAVITY;
Short=AtARG1;
Name=ATJ15; Synonyms=ARG1, B15; OrderedLocusNames=At1g68370;
ORFNames=T2E12.8;
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, TISSUE SPECIFICITY, AND
DISRUPTION PHENOTYPE.
PubMed=9927707; DOI=10.1073/pnas.96.3.1140;
Sedbrook J.C., Chen R., Masson P.H.;
"ARG1 (Altered Response to Gravity) encodes a novel DnaJ-like protein
which potentially interacts with the cytoskeleton.";
Proc. Natl. Acad. Sci. U.S.A. 96:1140-1145(1999).
[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;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11599562; DOI=10.1379/1466-1268(2001)006<0209:TJDPOA>2.0.CO;2;
Miernyk J.A.;
"The J-domain proteins of Arabidopsis thaliana: an unexpectedly large
and diverse family of chaperones.";
Cell Stress Chaperones 6:209-218(2001).
[5]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=14507996; DOI=10.1105/tpc.015560;
Boonsirichai K., Sedbrook J.C., Chen R., Gilroy S., Masson P.H.;
"ALTERED RESPONSE TO GRAVITY is a peripheral membrane protein that
modulates gravity-induced cytoplasmic alkalinization and lateral auxin
transport in plant statocytes.";
Plant Cell 15:2612-2625(2003).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
-!- FUNCTION: Have a continuous role in plant development probably in
the structural organization of compartments (By similarity). Seems
to be involved in early gravitropic signal transduction within the
gravity-perceiving cells (statocytes), where it influences pH
changes and auxin distribution. Probably affects the localization
and/or activity of auxin efflux carrier components (PIN proteins)
or other proteins involved in lateral auxin transport.
{ECO:0000250, ECO:0000269|PubMed:14507996,
ECO:0000269|PubMed:9927707}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:14507996}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:14507996}; Peripheral membrane protein
{ECO:0000269|PubMed:14507996}. Golgi apparatus membrane
{ECO:0000269|PubMed:14507996}; Peripheral membrane protein
{ECO:0000269|PubMed:14507996}. Note=Found in endoplasmic
reticulum, Golgi, vesicles near the plasma membrane and around
cell plate, and bound to the plasma membrane. Probably interacts
with integral membrane proteins. Also interacts with cytoskeleton.
-!- TISSUE SPECIFICITY: Expressed at high levels in root cap, root tip
meristematic region and elongation zones, and at lower levels in
mature part of roots (at protein level). Constitutively expressed
in seedlings, etiolated or not, roots, rosette leaves, cauline
leaves, stems, flowers, siliques and pollen.
{ECO:0000269|PubMed:14507996, ECO:0000269|PubMed:9927707}.
-!- DISRUPTION PHENOTYPE: Roots and hypocotyls reorient slowly upon
gravistimulation. Plants are normal for phototropism and for
responses to hormones such as auxin, abscisic acid, gibberellins
and ethylene. They also accumulate starch like the wild-type. In
response to gravistimulation arg1-2 lacks cytoplasmic pH changes
in columella cells and has a bad repartition of auxin that
accumulates in root tips instead of forming a gradient.
{ECO:0000269|PubMed:14507996, ECO:0000269|PubMed:9927707}.
-!- SIMILARITY: Belongs to the DnaJ family. B/II subfamily.
{ECO:0000305}.
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EMBL; AF089810; AAD13758.1; -; mRNA.
EMBL; AC015986; AAF26045.1; -; Genomic_DNA.
EMBL; CP002684; AEE34786.1; -; Genomic_DNA.
PIR; E96707; E96707.
RefSeq; NP_177004.1; NM_105508.4.
UniGene; At.11013; -.
ProteinModelPortal; Q9ZSY2; -.
SMR; Q9ZSY2; -.
STRING; 3702.AT1G68370.1; -.
iPTMnet; Q9ZSY2; -.
PaxDb; Q9ZSY2; -.
EnsemblPlants; AT1G68370.1; AT1G68370.1; AT1G68370.
GeneID; 843166; -.
Gramene; AT1G68370.1; AT1G68370.1; AT1G68370.
KEGG; ath:AT1G68370; -.
Araport; AT1G68370; -.
TAIR; locus:2202334; AT1G68370.
eggNOG; KOG0713; Eukaryota.
eggNOG; COG0484; LUCA.
HOGENOM; HOG000241767; -.
InParanoid; Q9ZSY2; -.
OMA; VYGDNWI; -.
OrthoDB; EOG09360CN1; -.
PhylomeDB; Q9ZSY2; -.
PRO; PR:Q9ZSY2; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9ZSY2; baseline and differential.
Genevisible; Q9ZSY2; AT.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0008092; F:cytoskeletal protein binding; TAS:TAIR.
GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR036869; DnaJ_dom_sf.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
Pfam; PF00226; DnaJ; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF46565; SSF46565; 1.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
1: Evidence at protein level;
Chaperone; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Endoplasmic reticulum; Golgi apparatus; Membrane; Reference proteome.
CHAIN 1 410 Chaperone protein dnaJ 15.
/FTId=PRO_0000071083.
DOMAIN 17 82 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
COILED 284 344 {ECO:0000255}.
SEQUENCE 410 AA; 45484 MW; 4B54EA9AE42331A0 CRC64;
MSAKKLEGSS APANRRDPYE VLCVSKDAND QEIKSAYRKL ALKYHPDKNA NNPDASELFK
EVAFSYSILS DPEKRRHYDN AGFEALDADG MDMEIDLSNL GTVNTMFAAL FSKLGVPIKT
TVSANVLEEA MNGTVTVRPL PIGTSVSGKV EKQCAHFFGV TISEQQAESG VVVRVTSTAQ
SKFKLLYFEQ DSSGGYGLAL QEEREKTGKV TSAGMYFLHF QVYRMDTTVN ALAAAKDPES
AFFKRLEGLQ PCEVSELKAG THIFAVYGDN FFKTASYTIE ALCAKTYEDT TEKLKEIEAQ
ILRKRNELRQ FETEYRKALA RFQEVTNRYT QEKQTVDELL KQRDTIHSTF SVVKTPSGNN
LSNGSSSKAQ GDESKGDGDS AGEEGGTENR DKSKRKWFNL NLKGSDKKLG


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