位置:首页 > 蛋白库 > LPPE2_ARATH
LPPE2_ARATH
ID   LPPE2_ARATH             Reviewed;         286 AA.
AC   Q6NQL6; Q9FJZ4;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Lipid phosphate phosphatase epsilon 2, chloroplastic;
DE            Short=AtLPPE2;
DE            EC=3.1.3.-;
DE   AltName: Full=Phosphatidic acid phosphatase epsilon 2;
DE   AltName: Full=Plastidic phosphatidic acid phosphatase epsilon 2;
DE   Flags: Precursor;
GN   Name=LPPE2; OrderedLocusNames=At5g66450; ORFNames=K1F13.10;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=17652095; DOI=10.1074/jbc.m704385200;
RA   Nakamura Y., Tsuchiya M., Ohta H.;
RT   "Plastidic phosphatidic acid phosphatases identified in a distinct
RT   subfamily of lipid phosphate phosphatases with prokaryotic origin.";
RL   J. Biol. Chem. 282:29013-29021(2007).
CC   -!- FUNCTION: Exhibits phosphatidate phosphatase (PAP) activity in vitro.
CC       May play a secondary role as PAP in plastids.
CC       {ECO:0000269|PubMed:17652095}.
CC   -!- ACTIVITY REGULATION: Inhibited by Mg(2+).
CC       {ECO:0000269|PubMed:17652095}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:17652095};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC       {ECO:0000305|PubMed:17652095}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:17652095}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NQL6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NQL6-2; Sequence=VSP_053604;
CC   -!- TISSUE SPECIFICITY: Expressed in root tips, root branch points,
CC       cotyledons and leaves. {ECO:0000269|PubMed:17652095}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|PubMed:17652095}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB013389; BAB10921.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED98215.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED98216.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70312.1; -; Genomic_DNA.
DR   EMBL; BT010436; AAQ62437.1; -; mRNA.
DR   EMBL; AK175761; BAD43524.1; -; mRNA.
DR   RefSeq; NP_001078807.1; NM_001085338.1. [Q6NQL6-2]
DR   RefSeq; NP_001331934.1; NM_001345762.1. [Q6NQL6-1]
DR   RefSeq; NP_201446.2; NM_126043.3. [Q6NQL6-1]
DR   AlphaFoldDB; Q6NQL6; -.
DR   BioGRID; 22019; 1.
DR   STRING; 3702.AT5G66450.1; -.
DR   PaxDb; Q6NQL6; -.
DR   PRIDE; Q6NQL6; -.
DR   EnsemblPlants; AT5G66450.1; AT5G66450.1; AT5G66450. [Q6NQL6-1]
DR   EnsemblPlants; AT5G66450.2; AT5G66450.2; AT5G66450. [Q6NQL6-2]
DR   EnsemblPlants; AT5G66450.4; AT5G66450.4; AT5G66450. [Q6NQL6-1]
DR   GeneID; 836777; -.
DR   Gramene; AT5G66450.1; AT5G66450.1; AT5G66450. [Q6NQL6-1]
DR   Gramene; AT5G66450.2; AT5G66450.2; AT5G66450. [Q6NQL6-2]
DR   Gramene; AT5G66450.4; AT5G66450.4; AT5G66450. [Q6NQL6-1]
DR   KEGG; ath:AT5G66450; -.
DR   Araport; AT5G66450; -.
DR   TAIR; locus:2154875; AT5G66450.
DR   eggNOG; KOG3146; Eukaryota.
DR   HOGENOM; CLU_087422_1_0_1; -.
DR   InParanoid; Q6NQL6; -.
DR   PhylomeDB; Q6NQL6; -.
DR   BRENDA; 3.1.3.4; 399.
DR   PRO; PR:Q6NQL6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q6NQL6; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0047874; F:dolichyldiphosphatase activity; IBA:GO_Central.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:TAIR.
DR   GO; GO:0006651; P:diacylglycerol biosynthetic process; IDA:TAIR.
DR   GO; GO:0008610; P:lipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   CDD; cd03382; PAP2_dolichyldiphosphatase; 1.
DR   InterPro; IPR039667; Dolichyldiphosphatase_PAP2.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chloroplast; Hydrolase; Membrane; Plastid;
KW   Plastid inner membrane; Reference proteome; Transit peptide; Transmembrane;
KW   Transmembrane helix.
FT   TRANSIT         1..60
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           61..286
FT                   /note="Lipid phosphate phosphatase epsilon 2,
FT                   chloroplastic"
FT                   /id="PRO_0000425228"
FT   TRANSMEM        133..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..59
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_053604"
SQ   SEQUENCE   286 AA;  31530 MW;  993360644F510B33 CRC64;
     MAASSSSLLL LHKPTYNFHF AASSVPTYIN SARFRISSSI FPLDRRRRRR IWSVSGFKSM
     ADLVKTNARR DGEDRFQALE QEAFISNSSS ELQNELVSDA GDGIEAIANR LSKWIVAALF
     GSVLLLRHDG AALWAVIGSV SNSVLSVALK RILNQERPVA TLRSDPGMPS SHAQSISFIS
     VFSVFSVMEW LGTNVLSLFL SGFILALGSY FTWLRVSQKL HTTSQVVVGA IVGSVYSTLW
     YVTWNSLVLE AFTSTFSVQI ALFLVAAASA LGFAVYVLLN WFKDDR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024