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P2C75_ARATH
ID   P2C75_ARATH             Reviewed;         416 AA.
AC   Q9FLI3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Probable protein phosphatase 2C 75;
DE            Short=AtPP2C75;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein ABA-HYPERSENSITIVE GERMINATION 1;
DE   AltName: Full=Protein phosphatase 2C AHG1;
DE            Short=PP2C AHG1;
GN   Name=AHG1; OrderedLocusNames=At5g51760; ORFNames=MIO24.11;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
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, DEVELOPMENTAL STAGE, INDUCTION BY ABA, AND DISRUPTION PHENOTYPE.
RX   PubMed=17461784; DOI=10.1111/j.1365-313x.2007.03107.x;
RA   Nishimura N., Yoshida T., Kitahata N., Asami T., Shinozaki K., Hirayama T.;
RT   "ABA-Hypersensitive Germination1 encodes a protein phosphatase 2C, an
RT   essential component of abscisic acid signaling in Arabidopsis seed.";
RL   Plant J. 50:935-949(2007).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19021904; DOI=10.1186/1471-2164-9-550;
RA   Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.;
RT   "Genome-wide and expression analysis of protein phosphatase 2C in rice and
RT   Arabidopsis.";
RL   BMC Genomics 9:550-550(2008).
CC   -!- FUNCTION: Negative regulator of abscisic acid (ABA) responses during
CC       seed germination. {ECO:0000269|PubMed:17461784}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC   -!- INTERACTION:
CC       Q9FLI3; Q9ATB4: ADA2B; NbExp=3; IntAct=EBI-2363348, EBI-979237;
CC       Q9FLI3; O80931: AS1; NbExp=3; IntAct=EBI-2363348, EBI-763232;
CC       Q9FLI3; Q17TI5: BRX; NbExp=3; IntAct=EBI-2363348, EBI-4426649;
CC       Q9FLI3; A0SVK0: DOG1; NbExp=3; IntAct=EBI-2363348, EBI-25512274;
CC       Q9FLI3; Q8RXD6: HUB1; NbExp=3; IntAct=EBI-2363348, EBI-2012188;
CC       Q9FLI3; Q9SJW5: LBD14; NbExp=3; IntAct=EBI-2363348, EBI-25522919;
CC       Q9FLI3; Q38845: PP2AA1; NbExp=3; IntAct=EBI-2363348, EBI-1645478;
CC       Q9FLI3; Q93ZY2: ROPGEF1; NbExp=2; IntAct=EBI-2363348, EBI-4425188;
CC       Q9FLI3; Q39192: SRK2D; NbExp=2; IntAct=EBI-2363348, EBI-2363308;
CC       Q9FLI3; Q39193: SRK2I; NbExp=2; IntAct=EBI-2363348, EBI-2620383;
CC       Q9FLI3; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-2363348, EBI-4426144;
CC       Q9FLI3; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-2363348, EBI-15192297;
CC       Q9FLI3; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-2363348, EBI-4426557;
CC       Q9FLI3; Q5CCK4: VAL2; NbExp=5; IntAct=EBI-2363348, EBI-15193683;
CC   -!- DEVELOPMENTAL STAGE: During germination, expressed in the embryo,
CC       vascular bundles and the root cap. In 6-day-old seedlings, expression
CC       in seed coat/endosperm disappears is detected only at the bases of the
CC       lateral root buds. Expressed in developing an mature siliques from 10
CC       to 16 days after flowering (DAF). {ECO:0000269|PubMed:17461784}.
CC   -!- INDUCTION: By ABA. {ECO:0000269|PubMed:17461784}.
CC   -!- DISRUPTION PHENOTYPE: Hypersensitivity to ABA, salt and sucrose during
CC       seed germination. {ECO:0000269|PubMed:17461784}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; AB010074; BAB11245.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96123.1; -; Genomic_DNA.
DR   RefSeq; NP_199989.1; NM_124555.3.
DR   AlphaFoldDB; Q9FLI3; -.
DR   SMR; Q9FLI3; -.
DR   BioGRID; 20495; 28.
DR   DIP; DIP-48990N; -.
DR   IntAct; Q9FLI3; 16.
DR   STRING; 3702.AT5G51760.1; -.
DR   iPTMnet; Q9FLI3; -.
DR   PaxDb; Q9FLI3; -.
DR   PRIDE; Q9FLI3; -.
DR   ProteomicsDB; 250918; -.
DR   EnsemblPlants; AT5G51760.1; AT5G51760.1; AT5G51760.
DR   GeneID; 835250; -.
DR   Gramene; AT5G51760.1; AT5G51760.1; AT5G51760.
DR   KEGG; ath:AT5G51760; -.
DR   Araport; AT5G51760; -.
DR   TAIR; locus:2165371; AT5G51760.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_20_4_1; -.
DR   InParanoid; Q9FLI3; -.
DR   OrthoDB; 1044139at2759; -.
DR   PhylomeDB; Q9FLI3; -.
DR   PRO; PR:Q9FLI3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FLI3; baseline and differential.
DR   Genevisible; Q9FLI3; AT.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR   GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..416
FT                   /note="Probable protein phosphatase 2C 75"
FT                   /id="PRO_0000367995"
FT   DOMAIN          108..411
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          32..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         402
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  46043 MW;  7272F86C929FF020 CRC64;
     MTEIYRTIST GRGDDVSPTK CRERRRRRIE MRRQAAVFGE PSSSRNRDRT DMEVYSSFDV
     PLRKQARRSE IGGLPADIGG FLAPPAASSC QKSEAPVWKG EETEDEPLYG IVSVMGRSRK
     MEDSVTVKPN LCKPEVNRQR PVHFFAVYDG HGGSQVSTLC STTMHTFVKE ELEQNLEEEE
     EGSENDVVER KWRGVMKRSF KRMDEMATST CVCGTSVPLC NCDPREAAIS GSTAVTAVLT
     HDHIIVANTG DSRAVLCRNG MAIPLSNDHK PDRPDERARI EAAGGRVLVV DGARVEGILA
     TSRAIGDRYL KPMVAWEPEV TFMRRESGDE CLVLASDGLW DVLSSQLACD IARFCLREET
     PSSLDLNRMA QEDDNDGEQN PSRSVLAATL LTRLALGRQS SDNISVVVID LKNSSQ
 
 
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