DNJ15_ARATH
ID DNJ15_ARATH Reviewed; 410 AA.
AC Q9ZSY2;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Chaperone protein dnaJ 15;
DE Short=AtDjB15;
DE Short=AtJ15;
DE AltName: Full=Protein ALTERED RESPONSE TO GRAVITY;
DE Short=AtARG1;
GN Name=ATJ15; Synonyms=ARG1, B15; OrderedLocusNames=At1g68370;
GN ORFNames=T2E12.8;
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, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=9927707; DOI=10.1073/pnas.96.3.1140;
RA Sedbrook J.C., Chen R., Masson P.H.;
RT "ARG1 (Altered Response to Gravity) encodes a novel DnaJ-like protein which
RT potentially interacts with the cytoskeleton.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1140-1145(1999).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11599562; DOI=10.1379/1466-1268(2001)006<0209:tjdpoa>2.0.co;2;
RA Miernyk J.A.;
RT "The J-domain proteins of Arabidopsis thaliana: an unexpectedly large and
RT diverse family of chaperones.";
RL Cell Stress Chaperones 6:209-218(2001).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=14507996; DOI=10.1105/tpc.015560;
RA Boonsirichai K., Sedbrook J.C., Chen R., Gilroy S., Masson P.H.;
RT "ALTERED RESPONSE TO GRAVITY is a peripheral membrane protein that
RT modulates gravity-induced cytoplasmic alkalinization and lateral auxin
RT transport in plant statocytes.";
RL Plant Cell 15:2612-2625(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Plays a continuous role in plant development probably in the
CC structural organization of compartments (By similarity). Seems to be
CC involved in early gravitropic signal transduction within the gravity-
CC perceiving cells (statocytes), where it influences pH changes and auxin
CC distribution. Probably affects the localization and/or activity of
CC auxin efflux carrier components (PIN proteins) or other proteins
CC involved in lateral auxin transport. {ECO:0000250,
CC ECO:0000269|PubMed:14507996, ECO:0000269|PubMed:9927707}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14507996}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14507996}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14507996}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:14507996}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14507996}. Note=Found in endoplasmic reticulum,
CC Golgi, vesicles near the plasma membrane and around cell plate, and
CC bound to the plasma membrane. Probably interacts with integral membrane
CC proteins. Also interacts with cytoskeleton.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in root cap, root tip
CC meristematic region and elongation zones, and at lower levels in mature
CC part of roots (at protein level). Constitutively expressed in
CC seedlings, etiolated or not, roots, rosette leaves, cauline leaves,
CC stems, flowers, siliques and pollen. {ECO:0000269|PubMed:14507996,
CC ECO:0000269|PubMed:9927707}.
CC -!- DISRUPTION PHENOTYPE: Roots and hypocotyls reorient slowly upon
CC gravistimulation. Plants are normal for phototropism and for responses
CC to hormones such as auxin, abscisic acid, gibberellins and ethylene.
CC They also accumulate starch like the wild-type. In response to
CC gravistimulation arg1-2 lacks cytoplasmic pH changes in columella cells
CC and has a bad repartition of auxin that accumulates in root tips
CC instead of forming a gradient. {ECO:0000269|PubMed:14507996,
CC ECO:0000269|PubMed:9927707}.
CC -!- SIMILARITY: Belongs to the DnaJ family. B/II subfamily. {ECO:0000305}.
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DR EMBL; AF089810; AAD13758.1; -; mRNA.
DR EMBL; AC015986; AAF26045.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34786.1; -; Genomic_DNA.
DR PIR; E96707; E96707.
DR RefSeq; NP_177004.1; NM_105508.4.
DR AlphaFoldDB; Q9ZSY2; -.
DR SMR; Q9ZSY2; -.
DR STRING; 3702.AT1G68370.1; -.
DR iPTMnet; Q9ZSY2; -.
DR PaxDb; Q9ZSY2; -.
DR PRIDE; Q9ZSY2; -.
DR ProteomicsDB; 222080; -.
DR EnsemblPlants; AT1G68370.1; AT1G68370.1; AT1G68370.
DR GeneID; 843166; -.
DR Gramene; AT1G68370.1; AT1G68370.1; AT1G68370.
DR KEGG; ath:AT1G68370; -.
DR Araport; AT1G68370; -.
DR TAIR; locus:2202334; AT1G68370.
DR eggNOG; KOG0713; Eukaryota.
DR HOGENOM; CLU_031086_0_0_1; -.
DR InParanoid; Q9ZSY2; -.
DR OMA; VAIICKS; -.
DR OrthoDB; 924703at2759; -.
DR PhylomeDB; Q9ZSY2; -.
DR PRO; PR:Q9ZSY2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZSY2; baseline and differential.
DR Genevisible; Q9ZSY2; AT.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008092; F:cytoskeletal protein binding; TAS:TAIR.
DR GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW Golgi apparatus; Membrane; Reference proteome.
FT CHAIN 1..410
FT /note="Chaperone protein dnaJ 15"
FT /id="PRO_0000071083"
FT DOMAIN 17..82
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 351..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 284..344
FT /evidence="ECO:0000255"
FT COMPBIAS 351..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ 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
