ATP1_ARATH
ID ATP1_ARATH Reviewed; 220 AA.
AC Q9LU63; Q8GZ70; Q8L944;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Probable pterin-4-alpha-carbinolamine dehydratase, chloroplastic {ECO:0000305};
DE EC=4.2.1.96 {ECO:0000305};
DE AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase {ECO:0000305};
DE AltName: Full=PCD/DCoH-like protein 1 {ECO:0000303|Ref.1};
DE AltName: Full=Protein AIRP2 TARGET PROTEIN 1 {ECO:0000303|PubMed:28626006};
DE AltName: Full=Protein SDIR1-INTERACTING PROTEIN 1 {ECO:0000303|PubMed:25616872};
DE Flags: Precursor;
GN Name=ATP1 {ECO:0000303|PubMed:28626006};
GN Synonyms=PDL1 {ECO:0000303|Ref.1}, SDIRIP1 {ECO:0000303|PubMed:25616872};
GN OrderedLocusNames=At5g51110 {ECO:0000312|Araport:AT5G51110};
GN ORFNames=MWD22.5 {ECO:0000312|EMBL:BAA97373.1};
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].
RA Plume A.M.;
RT "Functional characterisation of Arabidopsis DRGs: clues from the DRG2
RT interactor PDL1.";
RL Thesis (2002), University of Queensland, Australia.
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18245455; DOI=10.1104/pp.107.114090;
RA Naponelli V., Noiriel A., Ziemak M.J., Beverley S.M., Lye L.F., Plume A.M.,
RA Botella J.R., Loizeau K., Ravanel S., Rebeille F., de Crecy-Lagard V.,
RA Hanson A.D.;
RT "Phylogenomic and functional analysis of pterin-4a-carbinolamine
RT dehydratase family (COG2154) proteins in plants and microorganisms.";
RL Plant Physiol. 146:1515-1527(2008).
RN [9]
RP FUNCTION, INTERACTION WITH SDIR1, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=25616872; DOI=10.1105/tpc.114.134163;
RA Zhang H., Cui F., Wu Y., Lou L., Liu L., Tian M., Ning Y., Shu K., Tang S.,
RA Xie Q.;
RT "The RING finger ubiquitin E3 ligase SDIR1 targets SDIR1-INTERACTING
RT PROTEIN1 for degradation to modulate the salt stress response and ABA
RT signaling in Arabidopsis.";
RL Plant Cell 27:214-227(2015).
RN [10]
RP FUNCTION, INTERACTION WITH AIRP2, AND UBIQUITINATION.
RX PubMed=28626006; DOI=10.1104/pp.17.00467;
RA Oh T.R., Kim J.H., Cho S.K., Ryu M.Y., Yang S.W., Kim W.T.;
RT "AtAIRP2 E3 ligase affects ABA and high-salinity responses by stimulating
RT its ATP1/SDIRIP1 substrate turnover.";
RL Plant Physiol. 174:2515-2531(2017).
CC -!- FUNCTION: Involved in tetrahydrobiopterin biosynthesis (By similarity).
CC Interacts with and acts downstream of the E3 ubiquitin-protein ligase
CC SDIR1 in abscisic acid (ABA) and salt stress signaling. Regulates the
CC expression of the bZIP transcription factor ABI5, which mediates
CC responses to ABA during seed germination and salt stress. The SDIR1-
CC ATP1/SDIRIP1 complex plays an important role in ABA signaling through
CC the ubiquitination pathway (PubMed:25616872). Acts downstream of AIRP2
CC in regulation of ABA signaling during drought stress (PubMed:28626006).
CC {ECO:0000250|UniProtKB:P61457, ECO:0000269|PubMed:25616872,
CC ECO:0000269|PubMed:28626006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin =
CC (6R)-L-erythro-6,7-dihydrobiopterin + H2O; Xref=Rhea:RHEA:11920,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15642, ChEBI:CHEBI:43120; EC=4.2.1.96;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with SDIR1 (PubMed:25616872). Interacts with AIRP2
CC (PubMed:28626006). {ECO:0000269|PubMed:25616872,
CC ECO:0000269|PubMed:28626006}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18245455, ECO:0000269|PubMed:25616872}. Cell
CC membrane {ECO:0000269|PubMed:25616872}; Peripheral membrane protein
CC {ECO:0000269|PubMed:25616872}. Nucleus {ECO:0000269|PubMed:25616872}.
CC -!- PTM: Ubiquitinated by SDIR1. Ubiquitination leads to its subsequent
CC degradation, thus controlling abscisic acid (ABA) signaling
CC (PubMed:25616872). Ubiquitinated by AIRP2. Ubiquitination leads to its
CC subsequent degradation, thus controlling abscisic acid (ABA) signaling
CC during drought stress (PubMed:25616872). {ECO:0000269|PubMed:25616872}.
CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AY536640; AAS45833.1; -; mRNA.
DR EMBL; AB023044; BAA97373.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96036.1; -; Genomic_DNA.
DR EMBL; AK117179; BAC41856.1; -; mRNA.
DR EMBL; AY052253; AAK97723.1; -; mRNA.
DR EMBL; AY143825; AAN28764.1; -; mRNA.
DR EMBL; BT003720; AAO39948.1; -; mRNA.
DR EMBL; AK226425; BAE98569.1; -; mRNA.
DR EMBL; AY088643; AAM66965.1; -; mRNA.
DR RefSeq; NP_199924.1; NM_124490.5.
DR AlphaFoldDB; Q9LU63; -.
DR SMR; Q9LU63; -.
DR IntAct; Q9LU63; 14.
DR STRING; 3702.AT5G51110.1; -.
DR PaxDb; Q9LU63; -.
DR PRIDE; Q9LU63; -.
DR ProteomicsDB; 241061; -.
DR EnsemblPlants; AT5G51110.1; AT5G51110.1; AT5G51110.
DR GeneID; 835185; -.
DR Gramene; AT5G51110.1; AT5G51110.1; AT5G51110.
DR KEGG; ath:AT5G51110; -.
DR Araport; AT5G51110; -.
DR TAIR; locus:2176182; AT5G51110.
DR eggNOG; ENOG502QSK7; Eukaryota.
DR InParanoid; Q9LU63; -.
DR OrthoDB; 1588292at2759; -.
DR PhylomeDB; Q9LU63; -.
DR PRO; PR:Q9LU63; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LU63; baseline and differential.
DR GO; GO:0071944; C:cell periphery; IDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0110102; P:ribulose bisphosphate carboxylase complex assembly; IMP:TAIR.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1360.20; -; 1.
DR InterPro; IPR036428; PCD_sf.
DR InterPro; IPR001533; Pterin_deHydtase.
DR PANTHER; PTHR12599; PTHR12599; 1.
DR Pfam; PF01329; Pterin_4a; 1.
DR SUPFAM; SSF55248; SSF55248; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chloroplast; Lyase; Membrane; Nucleus; Plastid;
KW Reference proteome; Tetrahydrobiopterin biosynthesis; Transit peptide;
KW Ubl conjugation.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..220
FT /note="Probable pterin-4-alpha-carbinolamine dehydratase,
FT chloroplastic"
FT /id="PRO_0000443385"
FT CONFLICT 148
FT /note="R -> K (in Ref. 7; AAM66965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 220 AA; 23897 MW; E99E5C7A4B39CECC CRC64;
MAATSSSPPC NISASSLLLR QPSRSILKVF GLLPPVSRNN RKLGRLTVTR SNLAQDFLGD
FGARDPYPEE IASQFGDKVL GCQSTEHKIL IPNASVLSLS QLQCSPVSSS QPPLSGDDAR
TLLHKVLGWS IVDNEAGGLK IRCMWKVRDF GCGVELINRI HKVAEASGHY PSLHLESPTQ
VRAELFTSSI GGLSMNDFIM AAKIDDIKTS DLSPRKRAWA
