PDR2_ARATH
ID PDR2_ARATH Reviewed; 1179 AA.
AC Q9LT02;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable manganese-transporting ATPase PDR2;
DE EC=7.2.2.-;
DE AltName: Full=Protein MALE GAMETOGENESIS IMPAIRED ANTHERS;
DE AltName: Full=Protein PHOSPHATE DEFICIENCY RESPONSE 2;
GN Name=PDR2; Synonyms=MIA; OrderedLocusNames=At5g23630; ORFNames=MQM1.11;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 702-1179.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14996215; DOI=10.1111/j.1365-313x.2004.02005.x;
RA Ticconi C.A., Delatorre C.A., Lahner B., Salt D.E., Abel S.;
RT "Arabidopsis pdr2 reveals a phosphate-sensitive checkpoint in root
RT development.";
RL Plant J. 37:801-814(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16291648; DOI=10.1101/gad.357305;
RA Jakobsen M.K., Poulsen L.R., Schulz A., Fleurat-Lessard P., Moller A.,
RA Husted S., Schiott M., Amtmann A., Palmgren M.G.;
RT "Pollen development and fertilization in Arabidopsis is dependent on the
RT MALE GAMETOGENESIS IMPAIRED ANTHERS gene encoding a type V P-type ATPase.";
RL Genes Dev. 19:2757-2769(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF THR-699.
RX PubMed=19666499; DOI=10.1073/pnas.0901778106;
RA Ticconi C.A., Lucero R.D., Sakhonwasee S., Adamson A.W., Creff A.,
RA Nussaume L., Desnos T., Abel S.;
RT "ER-resident proteins PDR2 and LPR1 mediate the developmental response of
RT root meristems to phosphate availability.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14174-14179(2009).
CC -!- FUNCTION: Mediates manganese transport into the endoplasmic reticulum.
CC The ATPase activity is required for cellular manganese homeostasis (By
CC similarity). Plays an important role in pollen and root development
CC through its impact on protein secretion and transport processes.
CC Functions together with LPR1 and LPR2 in a common pathway that adjusts
CC root meristem activity to phosphate availability. Under phosphate
CC limitation, restricts SHR movement in root meristem and is required for
CC maintaining SCR expression in the root meristem stem-cell niche as well
CC as for proximal meristem activity. Can complement the yeast spf1
CC mutant. {ECO:0000250, ECO:0000269|PubMed:14996215,
CC ECO:0000269|PubMed:16291648, ECO:0000269|PubMed:19666499}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16291648, ECO:0000269|PubMed:19666499}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16291648,
CC ECO:0000269|PubMed:19666499}. Note=Found in secretory vesicles of the
CC tapetum and developing pollen grains.
CC -!- TISSUE SPECIFICITY: Highly expressed in root meristem. Expressed in
CC pavement cells of trichomes, stipules, stamens and pollen grains.
CC {ECO:0000269|PubMed:19666499}.
CC -!- DISRUPTION PHENOTYPE: Imbalances in cation homeostasis and severe
CC reduction in fertility. Increased inhibition of primary root growth in
CC low inorganic phosphate conditions. {ECO:0000269|PubMed:14996215,
CC ECO:0000269|PubMed:16291648, ECO:0000269|PubMed:19666499}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX831910; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB025633; BAA97238.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93192.1; -; Genomic_DNA.
DR EMBL; BX831910; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_197752.1; NM_122268.5.
DR AlphaFoldDB; Q9LT02; -.
DR SMR; Q9LT02; -.
DR BioGRID; 17703; 1.
DR STRING; 3702.AT5G23630.1; -.
DR TCDB; 3.A.3.10.22; the p-type atpase (p-atpase) superfamily.
DR MetOSite; Q9LT02; -.
DR PaxDb; Q9LT02; -.
DR PRIDE; Q9LT02; -.
DR ProteomicsDB; 251348; -.
DR EnsemblPlants; AT5G23630.1; AT5G23630.1; AT5G23630.
DR GeneID; 832428; -.
DR Gramene; AT5G23630.1; AT5G23630.1; AT5G23630.
DR KEGG; ath:AT5G23630; -.
DR Araport; AT5G23630; -.
DR TAIR; locus:2171686; AT5G23630.
DR eggNOG; KOG0209; Eukaryota.
DR HOGENOM; CLU_001828_4_1_1; -.
DR InParanoid; Q9LT02; -.
DR OMA; RFAPKQK; -.
DR OrthoDB; 172453at2759; -.
DR PhylomeDB; Q9LT02; -.
DR PRO; PR:Q9LT02; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LT02; baseline and differential.
DR Genevisible; Q9LT02; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006875; P:cellular metal ion homeostasis; IMP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
DR GO; GO:0010073; P:meristem maintenance; IMP:TAIR.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0010152; P:pollen maturation; IMP:TAIR.
DR GO; GO:0048867; P:stem cell fate determination; IMP:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006544; P-type_TPase_V.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endoplasmic reticulum; Magnesium; Manganese; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1179
FT /note="Probable manganese-transporting ATPase PDR2"
FT /id="PRO_0000046420"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..50
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..218
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..435
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 948..967
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 968..979
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..997
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 998..1013
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1014..1034
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1035..1059
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1060..1079
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1080..1092
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1093..1110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1111..1128
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1129..1148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1149..1179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 833..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 491
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 812
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 816
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 699
FT /note="T->I: In pdr2-1; increased inhibition of primary
FT root growth in low inorganic phosphate conditions."
FT /evidence="ECO:0000269|PubMed:19666499"
FT CONFLICT 935
FT /note="D -> N (in Ref. 3; BX831910)"
FT /evidence="ECO:0000305"
FT CONFLICT 995
FT /note="S -> F (in Ref. 3; BX831910)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1179 AA; 131115 MW; 4A3E82D2222A4D78 CRC64;
MSSFRVGGKV VEKVDLCRKK QLVWRLDVWP FAILYTVWLT TIVPSIDFSD ACIALGGLSA
FHILVLLFTT WSVDFKCFVQ FSKVNSIDQA DACKVTPAKF SGSKEVVPLH FRSQMTDSAS
SGDMEEIFFD FRKQRFIYSK ELGAFSKLPY PTKETFGHYL KCTGHGTEAK IATATEKWGR
NVFDYPQPTF QKLMKENCME PFFVFQVFCV GLWCLDEFWY YSVFTLFMLF MFESTMAKSR
LKTLTDLRSV RVDSQTVMVY RSGKWVKLLG TDLLPGDVVS IGRPSTQTGG EDKTVPADML
LLVGSAIVNE AILTGESTPQ WKVPIVGQRS DEKLSIKRNK NHVLFGGTKI LQHSPDKSFS
LKTPDGGCLA VVLRTGFETS QGKLMRTILF STERVTANSW ESGLFILFLV VFAVIAAGYV
LVKGLEDPTR SKYKLLLGCS LIITSVIPPE LPMELSIAVN TSLLALVRRG IFCTEPFRIP
FAGKVDLCCF DKTGTLTSDD MEFRGVGGLS NCEEAETDMS KVPVRTLEIL ASCHALVFVE
NKLVGDPLEK AALKGIDWSY KADEKALPRR GNGNSVQIMQ RYHFASHLKR MSVIVRIQEE
YLAFVKGAPE TIQERLVDVP AQYIETYKRY TRQGSRVLAL AYKRLPDMMV SEARDMDRDA
VESDLTFAGF AVFNCPIRPD SAPVLLELKN SSHDLVMITG DQALTACHVA GQVHIVSNPV
LILGRSGSGN EYKWVSPDEK EIIPYSEKEI ETLAETHDLC IGGDSIEMLQ ATSAVLRVIP
FVKVFARVAP QQKELILTTF KAVGRGTLMC GDGTNDVGAL KQAHVGVALL NNKLPLSPSD
SSKDDKSKSK KSKLPLEPAS KTITQNGEGS SKGKIPPQNR HLTAAELQRQ KLKKIMDDLN
NDEGDGRSAP LVKLGDASMA SPFTAKHASV APVTDIIRQG RSTLVTTLQM FKILGLNCLA
TAYVLSVMYL DGVKLGDVQA TISGVLTAAF FLFISHARPL QTLSAERPHP SVFSVYLFLS
LIGQFAVHLT FLVYSVKEAE KHMPEECIEP DASFHPNLVN TVSYMVSMML QVATFAVNYM
GHPFNQSIRE NKPFFYALIA GAGFFTVIAS DLFRDLNDSL KLVPLPQGLR DKLLIWASLM
FIICYSWERL LRWAFPGKIS SWKHKQRAVT ANLEKKKKV
