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DnaJ homolog subfamily C GRV2 (Protein GRAVITROPISM DEFECTIVE 2) (Protein GREEN FLUORESCENT SEED 2) (Protein KATAMARI2)

 GRV2_ARATH              Reviewed;        2554 AA.
F4IVL6; B3H5B3; O81018;
06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
23-MAY-2018, entry version 53.
RecName: Full=DnaJ homolog subfamily C GRV2;
AltName: Full=Protein GRAVITROPISM DEFECTIVE 2;
AltName: Full=Protein GREEN FLUORESCENT SEED 2;
AltName: Full=Protein KATAMARI2;
Name=GRV2; Synonyms=GFS2, KAM2; OrderedLocusNames=At2g26890;
ORFNames=F12C20.7;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[2]
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).
[3]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=15466218; DOI=10.1104/pp.104.050583;
Silady R.A., Kato T., Lukowitz W., Sieber P., Tasaka M.,
Somerville C.R.;
"The gravitropism defective 2 mutants of Arabidopsis are deficient in
a protein implicated in endocytosis in Caenorhabditis elegans.";
Plant Physiol. 136:3095-3103(2004).
[4]
FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND SUBCELLULAR
LOCATION.
PubMed=17259264; DOI=10.1105/tpc.106.046631;
Tamura K., Takahashi H., Kunieda T., Fuji K., Shimada T.,
Hara-Nishimura I.;
"Arabidopsis KAM2/GRV2 is required for proper endosome formation and
functions in vacuolar sorting and determination of the embryo growth
axis.";
Plant Cell 19:320-332(2007).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17293568; DOI=10.1105/tpc.106.045997;
Fuji K., Shimada T., Takahashi H., Tamura K., Koumoto Y., Utsumi S.,
Nishizawa K., Maruyama N., Hara-Nishimura I.;
"Arabidopsis vacuolar sorting mutants (green fluorescent seed) can be
identified efficiently by secretion of vacuole-targeted green
fluorescent protein in their seeds.";
Plant Cell 19:597-609(2007).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17971043; DOI=10.1111/j.1365-313X.2007.03314.x;
Silady R.A., Ehrhardt D.W., Jackson K., Faulkner C., Oparka K.,
Somerville C.R.;
"The GRV2/RME-8 protein of Arabidopsis functions in the late endocytic
pathway and is required for vacuolar membrane flow.";
Plant J. 53:29-41(2008).
[7]
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: Required for endosome formation, vacuolar protein
sorting and determination of the embryo growth axis. Necessary for
the transport of proteins into protein storage vacuoles (PSVs).
Participates in vesicle trafficking from the endosome to the
central vacuole. Involved in the regulation of shoot phototropism
and gravitropism, probably through the positioning of specialized
amyloplasts (statoliths) in endodermal cells.
{ECO:0000269|PubMed:15466218, ECO:0000269|PubMed:17259264,
ECO:0000269|PubMed:17293568, ECO:0000269|PubMed:17971043}.
-!- SUBCELLULAR LOCATION: Endosome membrane
{ECO:0000269|PubMed:17259264, ECO:0000269|PubMed:17971043};
Peripheral membrane protein {ECO:0000269|PubMed:17259264}.
-!- TISSUE SPECIFICITY: Constitutively expressed in roots, hypocotyls,
leaves (e.g. vascular tissues), stems, flowers (e.g. petals and
stigmas), siliques and pollen. {ECO:0000269|PubMed:15466218,
ECO:0000269|PubMed:17971043}.
-!- DEVELOPMENTAL STAGE: Expressed at the early to middle stages of
seed maturation. {ECO:0000269|PubMed:17259264}.
-!- DISRUPTION PHENOTYPE: Reduced shoot phototropism and gravitropism,
and impaired embryo growth axis (e.g. between the late torpedo-
shaped embryo stage and the walking stick-shaped embryo stage).
Abnormal amyloplasts position and sedimentation in endodermal
cells. Defect in the organization of endomembranes characterized
by aggregated endomembrane structures accompanied by a missorting
of storage proteins. {ECO:0000269|PubMed:15466218,
ECO:0000269|PubMed:17259264, ECO:0000269|PubMed:17293568}.
-!- MISCELLANEOUS: 'Katamari' means 'aggregate' in Japanese.
-!- SEQUENCE CAUTION:
Sequence=AAC32237.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC005168; AAC32237.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002685; AEC07904.1; -; Genomic_DNA.
PIR; T02646; T02646.
RefSeq; NP_180257.3; NM_128246.5.
UniGene; At.12880; -.
UniGene; At.67106; -.
SMR; F4IVL6; -.
BioGrid; 2582; 1.
STRING; 3702.AT2G26890.1; -.
iPTMnet; F4IVL6; -.
PaxDb; F4IVL6; -.
PRIDE; F4IVL6; -.
EnsemblPlants; AT2G26890.1; AT2G26890.1; AT2G26890.
GeneID; 817230; -.
Gramene; AT2G26890.1; AT2G26890.1; AT2G26890.
KEGG; ath:AT2G26890; -.
Araport; AT2G26890; -.
TAIR; locus:2039543; AT2G26890.
eggNOG; KOG1789; Eukaryota.
eggNOG; ENOG410XRI2; LUCA.
HOGENOM; HOG000243604; -.
InParanoid; F4IVL6; -.
KO; K09533; -.
OMA; GMLERCT; -.
OrthoDB; EOG0936001Z; -.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:F4IVL6; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; F4IVL6; baseline and differential.
Genevisible; F4IVL6; AT.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
GO; GO:0005770; C:late endosome; IDA:TAIR.
GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0009660; P:amyloplast organization; IMP:TAIR.
GO; GO:0051301; P:cell division; IMP:TAIR.
GO; GO:0045022; P:early endosome to late endosome transport; IBA:GO_Central.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0000578; P:embryonic axis specification; IMP:UniProtKB.
GO; GO:0006897; P:endocytosis; ISS:TAIR.
GO; GO:0007032; P:endosome organization; IMP:TAIR.
GO; GO:0045324; P:late endosome to vacuole transport; IMP:UniProtKB.
GO; GO:0009959; P:negative gravitropism; IMP:TAIR.
GO; GO:0009638; P:phototropism; IMP:UniProtKB.
GO; GO:0006623; P:protein targeting to vacuole; IMP:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
GO; GO:0042594; P:response to starvation; IMP:TAIR.
GO; GO:0007033; P:vacuole organization; IMP:TAIR.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR025640; DUF4339.
InterPro; IPR036869; J_dom_sf.
Pfam; PF00226; DnaJ; 1.
Pfam; PF14237; DUF4339; 1.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF48371; SSF48371; 5.
PROSITE; PS50076; DNAJ_2; 1.
1: Evidence at protein level;
Chaperone; Coiled coil; Complete proteome; Developmental protein;
Endosome; Membrane; Protein transport; Reference proteome;
Stress response; Transport.
CHAIN 1 2554 DnaJ homolog subfamily C GRV2.
/FTId=PRO_0000420922.
DOMAIN 1524 1606 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
COILED 925 951 {ECO:0000255}.
COILED 1518 1546 {ECO:0000255}.
COMPBIAS 427 430 Poly-Ala.
COMPBIAS 1055 1061 Poly-Gly.
COMPBIAS 2548 2551 Poly-Pro.
SEQUENCE 2554 AA; 279073 MW; 2282C39AC62AEA7D CRC64;
MDSVSRGAVA STTGGAVEEP EYLARYLVVK HSWRGRYKRI LCISSGGIVT LDPNTLAVTN
SYDTGSNFDG ASPLVGRDEN TESVGGEFTV NVRTDGKGKF KAMKFSSRCR ASILTELYRL
RWNQIRPVAE FQVLHLRRRN AEWVPYKLKI TFVGLELVDS KSGNSRWILD FRDMGSPAII
LLSDAYRTKS ADSAGFVLCP MYGRKSKAFR AAPGTTNSSI VASLAKTAKS MVGVFLSVDD
SQLLTVSEYM TRRAKEAVGA EETPNGWWSV TRLRSAAHGT LNMPGLSLAI GPKGGLGEHG
DAVALQLILT KASLVERRID NYEVVIVRPL SSVSSLVRFA EEPQMFAIEF SDGCPVLVYA
SISRDNLLAA ILDTLQTEGH CPIPVLPRLT MPGHRIDPPC GRVSLISGPQ HLVADLETCS
LHLKHLAAAA KDAVAEGGSV PGCRARLWRR IREFNACIPY TGVPANSEVP EVTLMALITM
LPSTPNLPVD APPLPPPSPK AAATVIGFVT CLRRLLSSRS AASHIMSFPA AVNRIMGLLR
NGSEGVAAEA AGLIASLIGG WSADLSTAPD SRGEKHATIM HTKSVLFAQQ GYVTILVNRL
KPMSVSPLFS MAIVEVFEAM VCDPHGETTQ YTVFVELLRQ IAALRRRLFA LFAHPAESVR
ETIAVIMRTI AEEDAIAAES MRDAALRDGA LLRHLLNAFS LPASERREVS RQLVALWADS
YQPALDLLSR VLPPGLVAYL HTRPDDVVDD TDQEGSSTNR RQKRLLQQRR GRIAKGMGAQ
DIPLPPGNNV EAGDAAKHMS ANASVPDNFQ RRAADSSSEA SNPQASAFPG VDSTIAGVSQ
NGYPAFASVT TNANGHEQPE TNASDVVGSD PNLYGIQNSV LPAPAQVIVE STAVGSGKLL
LNWREFWRAF GLDHNRADLI WNERTRQELI EALKAEVHNL DVEKERTEDI SPGDVEATTG
QEIIPRISWN YSEFSVSYRS LSKEVCVGQY YLRLLLESGN AGKAQDFPLR DPVAFFRALY
HRFQCDADMG LTIDGAVPDE LGSSGDWCDM SRLDGFGGGG GASVRELCAR AMAIVYEQHY
NTIGPFEGTA HITALIDRTN DRALRHRLLL LLKALVKVLL NVEGCVVVGG CVLAVDLLTV
VHENSERTPI PLQSNLIAAT AFMEPPKEWM YIDKGGAEVG PVEKDVIRSL WSKKDIDWTT
KCRALGMSDW KKLRDIRELR WAVAVRVPVL TPSQVGDAAL SILHSMVSAH SDLDDAGEIV
TPTPRVKRIL SSTRCLPHIA QALLSGEPVI VEAGAALLKD VVTRNSKAMI RLYSTGAFYF
ALAYPGSNLY SIAQLFSVTH VHQAFHGGEE ATVSSSLPLA KRSVLGGLLP ESLLYVLERS
GPAAFAAGMV SDSDTPEIIW THKMRAENLI CQVLQHLGDY PQKLSQHCHS LYDYAPMPPV
TYPELRDEMW CHRYYLRNLC DEIQFPNWPI VEHVEFLQSL LVMWREELTR KPMDLSEGEA
CKILEISLNN VSSDDLNRTA SVELNEEISN ISKQIQNLDE EKLKRQYRKL AMRYHPDKNP
EGREKFLAVQ KAYECLQATM QGLQGPQPWR LLLLLKAQCI LYRRYGHVLR PFKYAGYPML
LDAVTVDKDD NNFLSNDRSP LLVAASELVS LTCAASSLNG EELVRDGGVQ LLSTLLSRCM
CVVQPTTSQH EPAAIIVTNV MRTLSVISQF ESARAGFLEL PSLIEDIVHC TELERVPAAV
DAALQSIAKV SVFPELQHGL LKAGALWYIL PLLLQYDSTA EESNSVESHG VGVSIQIAKN
EHALQASQAL SRLTGLCADE SLTPYNATAA DVLKALLTPK LASLLKDEVA KDLLSKLNTN
LETPEIIWNS ATRSELLNFV DEQRACQCPD GSYDLKNAQS FSYDALSKEV FVGNVYLKVY
NDQPDSEISE PESFCNALID FISSLVHTEL PSVSEDQNLI EDRNSSNDTP ELQSSVAEPS
LIEEHSDHQP SSEGMKNEEC FLIDHLQLGL TALQNLLTKY PDLASVFSSK ERLLPLFECF
SVAIASKTDI PKLCLNVLSR LTAYAPCLET MVSDGSSLLL LLQMLHSAPS FREGALHVLY
ALASTPELAW AAAKHGGVVY ILELLLPLQK EIPLQQRAAA ASLLGKLVAQ PMHGPRVAIT
LVRFLPDGLV SIIRDGPGEA VVHALERTTE TPELVWTPAM AASLSAQIAT MASDIYREQQ
KGSVIEWDVP EQSAGQQEMR DEPQVGGIYV RRFLKDPKFP LRNPKRFLEG LLDQYLSAMA
ATHYEQHPVD PELPLLLSAA LVSLLRVHPA LADHIGHLGY VPKLVAAVAY EGRRETMSSG
EVKAEEIGSD GVNESTDPSS LPGQTPQERV RLSCLRVLHQ LAASTTCAEA MAATSAGNAQ
VVPLLMKAIG WLGGSILALE TLKRVVVAGN RARDALVAQG LKVGLIEVLL GLLDWRTGGR
YGLSSHMKWN ESEASIGRVL AVEVLHGFAT EGAHCSKVRE ILDASEVWSA YKDQKHDLFL
PSNTQSAAGV AGFIENSSNS LTYALTAPPP PSHP


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