GPPL3_ARATH
ID GPPL3_ARATH Reviewed; 245 AA.
AC Q8RYE9; Q56YT8; Q93Z44;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein At2g33255;
DE EC=3.1.3.-;
GN OrderedLocusNames=At2g33255; ORFNames=F25I18.1, F4P9.2;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-245.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RYE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RYE9-2; Sequence=VSP_057946;
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. DOG/GPP
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93834.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC002332; AAM14804.1; -; Genomic_DNA.
DR EMBL; AC002334; AAM14806.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08806.1; -; Genomic_DNA.
DR EMBL; AY058145; AAL25561.1; -; mRNA.
DR EMBL; AY093716; AAM10340.1; -; mRNA.
DR EMBL; AK221233; BAD93834.1; ALT_INIT; mRNA.
DR RefSeq; NP_850204.2; NM_179873.3. [Q8RYE9-1]
DR AlphaFoldDB; Q8RYE9; -.
DR SMR; Q8RYE9; -.
DR STRING; 3702.AT2G33255.1; -.
DR PaxDb; Q8RYE9; -.
DR PRIDE; Q8RYE9; -.
DR ProteomicsDB; 220640; -. [Q8RYE9-1]
DR EnsemblPlants; AT2G33255.1; AT2G33255.1; AT2G33255. [Q8RYE9-1]
DR GeneID; 817888; -.
DR Gramene; AT2G33255.1; AT2G33255.1; AT2G33255. [Q8RYE9-1]
DR KEGG; ath:AT2G33255; -.
DR Araport; AT2G33255; -.
DR TAIR; locus:505006285; AT2G33255.
DR eggNOG; ENOG502QR7R; Eukaryota.
DR HOGENOM; CLU_045011_11_2_1; -.
DR InParanoid; Q8RYE9; -.
DR OMA; CALYCPE; -.
DR OrthoDB; 1153965at2759; -.
DR PhylomeDB; Q8RYE9; -.
DR PRO; PR:Q8RYE9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RYE9; baseline and differential.
DR Genevisible; Q8RYE9; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..245
FT /note="Haloacid dehalogenase-like hydrolase domain-
FT containing protein At2g33255"
FT /id="PRO_0000424322"
FT ACT_SITE 39
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 41
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_057946"
FT INIT_MET Q8RYE9-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES Q8RYE9-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 245 AA; 27497 MW; 20FF6D71A29B025E CRC64;
MTFLLSRTFI SLTLRPSCSI SMANLTTNAK TRLRGVVFDM DGTLTVPVID FAAMYRAVLG
EDAYKRIKAE SPSGIDILHH IESWSPDKQQ KAYEIIADYE KQGIDKLQIM PGTAELCGFL
DSKKIKRGLI TRNVQKAIDI FHQRFEVIFS PALGREFRPY KPNPDPLLHI CSTWDIQPNE
VMMVGDSLKD DIACGKRAGA FTCLLDETGR YGPDDFSVSG LQPDFKVDSL SKIQNLLETN
FDLNP
