GRV2_ARATH
ID GRV2_ARATH Reviewed; 2554 AA.
AC F4IVL6; B3H5B3; O81018;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=DnaJ homolog subfamily C GRV2;
DE AltName: Full=Protein GRAVITROPISM DEFECTIVE 2;
DE AltName: Full=Protein GREEN FLUORESCENT SEED 2;
DE AltName: Full=Protein KATAMARI2;
GN Name=GRV2; Synonyms=GFS2, KAM2; OrderedLocusNames=At2g26890;
GN ORFNames=F12C20.7;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=15466218; DOI=10.1104/pp.104.050583;
RA Silady R.A., Kato T., Lukowitz W., Sieber P., Tasaka M., Somerville C.R.;
RT "The gravitropism defective 2 mutants of Arabidopsis are deficient in a
RT protein implicated in endocytosis in Caenorhabditis elegans.";
RL Plant Physiol. 136:3095-3103(2004).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17259264; DOI=10.1105/tpc.106.046631;
RA Tamura K., Takahashi H., Kunieda T., Fuji K., Shimada T.,
RA Hara-Nishimura I.;
RT "Arabidopsis KAM2/GRV2 is required for proper endosome formation and
RT functions in vacuolar sorting and determination of the embryo growth
RT axis.";
RL Plant Cell 19:320-332(2007).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17293568; DOI=10.1105/tpc.106.045997;
RA Fuji K., Shimada T., Takahashi H., Tamura K., Koumoto Y., Utsumi S.,
RA Nishizawa K., Maruyama N., Hara-Nishimura I.;
RT "Arabidopsis vacuolar sorting mutants (green fluorescent seed) can be
RT identified efficiently by secretion of vacuole-targeted green fluorescent
RT protein in their seeds.";
RL Plant Cell 19:597-609(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17971043; DOI=10.1111/j.1365-313x.2007.03314.x;
RA Silady R.A., Ehrhardt D.W., Jackson K., Faulkner C., Oparka K.,
RA Somerville C.R.;
RT "The GRV2/RME-8 protein of Arabidopsis functions in the late endocytic
RT pathway and is required for vacuolar membrane flow.";
RL Plant J. 53:29-41(2008).
RN [7]
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: Required for endosome formation, vacuolar protein sorting and
CC determination of the embryo growth axis. Necessary for the transport of
CC proteins into protein storage vacuoles (PSVs). Participates in vesicle
CC trafficking from the endosome to the central vacuole. Involved in the
CC regulation of shoot phototropism and gravitropism, probably through the
CC positioning of specialized amyloplasts (statoliths) in endodermal
CC cells. {ECO:0000269|PubMed:15466218, ECO:0000269|PubMed:17259264,
CC ECO:0000269|PubMed:17293568, ECO:0000269|PubMed:17971043}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:17259264,
CC ECO:0000269|PubMed:17971043}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17259264}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in roots, hypocotyls,
CC leaves (e.g. vascular tissues), stems, flowers (e.g. petals and
CC stigmas), siliques and pollen. {ECO:0000269|PubMed:15466218,
CC ECO:0000269|PubMed:17971043}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the early to middle stages of seed
CC maturation. {ECO:0000269|PubMed:17259264}.
CC -!- DISRUPTION PHENOTYPE: Reduced shoot phototropism and gravitropism, and
CC impaired embryo growth axis (e.g. between the late torpedo-shaped
CC embryo stage and the walking stick-shaped embryo stage). Abnormal
CC amyloplasts position and sedimentation in endodermal cells. Defect in
CC the organization of endomembranes characterized by aggregated
CC endomembrane structures accompanied by a missorting of storage
CC proteins. {ECO:0000269|PubMed:15466218, ECO:0000269|PubMed:17259264,
CC ECO:0000269|PubMed:17293568}.
CC -!- MISCELLANEOUS: 'Katamari' means 'aggregate' in Japanese.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC32237.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005168; AAC32237.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07904.1; -; Genomic_DNA.
DR PIR; T02646; T02646.
DR RefSeq; NP_180257.3; NM_128246.5.
DR AlphaFoldDB; F4IVL6; -.
DR BioGRID; 2582; 1.
DR STRING; 3702.AT2G26890.1; -.
DR iPTMnet; F4IVL6; -.
DR PaxDb; F4IVL6; -.
DR PRIDE; F4IVL6; -.
DR ProteomicsDB; 222277; -.
DR EnsemblPlants; AT2G26890.1; AT2G26890.1; AT2G26890.
DR GeneID; 817230; -.
DR Gramene; AT2G26890.1; AT2G26890.1; AT2G26890.
DR KEGG; ath:AT2G26890; -.
DR Araport; AT2G26890; -.
DR TAIR; locus:2039543; AT2G26890.
DR eggNOG; KOG1789; Eukaryota.
DR HOGENOM; CLU_001238_1_0_1; -.
DR InParanoid; F4IVL6; -.
DR OMA; EITNQWL; -.
DR OrthoDB; 11434at2759; -.
DR PRO; PR:F4IVL6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IVL6; baseline and differential.
DR Genevisible; F4IVL6; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0005770; C:late endosome; IDA:TAIR.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0009660; P:amyloplast organization; IMP:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0000578; P:embryonic axis specification; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:TAIR.
DR GO; GO:0007032; P:endosome organization; IMP:TAIR.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:UniProtKB.
DR GO; GO:0009959; P:negative gravitropism; IMP:TAIR.
DR GO; GO:0009638; P:phototropism; IMP:UniProtKB.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:2000641; P:regulation of early endosome to late endosome transport; IEA:InterPro.
DR GO; GO:0042594; P:response to starvation; IMP:TAIR.
DR GO; GO:0007033; P:vacuole organization; IMP:TAIR.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR044978; GRV2/DNAJC13.
DR InterPro; IPR045802; GRV2/DNAJC13_N.
DR InterPro; IPR025640; GYF_2.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR36983; PTHR36983; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF14237; GYF_2; 1.
DR Pfam; PF19432; RME-8_N; 3.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Developmental protein; Endosome; Membrane;
KW Protein transport; Reference proteome; Stress response; Transport.
FT CHAIN 1..2554
FT /note="DnaJ homolog subfamily C GRV2"
FT /id="PRO_0000420922"
FT DOMAIN 1524..1606
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 746..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1960..1994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2339..2366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 925..951
FT /evidence="ECO:0000255"
FT COILED 1518..1546
FT /evidence="ECO:0000255"
FT COMPBIAS 1960..1980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2352..2366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ 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
