PXG4_ARATH
ID PXG4_ARATH Reviewed; 195 AA.
AC Q9CAB7; Q8L9R2;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable peroxygenase 4;
DE Short=AtPXG4;
DE EC=1.11.2.3;
DE AltName: Full=Caleosin-4;
GN Name=PXG4; Synonyms=CLO4; OrderedLocusNames=At1g70670; ORFNames=F5A18.15;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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].
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 [5]
RP INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=19467604; DOI=10.1016/j.plaphy.2009.04.005;
RA Partridge M., Murphy D.J.;
RT "Roles of a membrane-bound caleosin and putative peroxygenase in biotic and
RT abiotic stress responses in Arabidopsis.";
RL Plant Physiol. Biochem. 47:796-806(2009).
RN [6]
RP FUNCTION, INDUCTION, CALCIUM-BINDING, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21471120; DOI=10.1093/pcp/pcr039;
RA Kim Y.Y., Jung K.W., Yoo K.S., Jeung J.U., Shin J.S.;
RT "A stress-responsive caleosin-like protein, AtCLO4, acts as a negative
RT regulator of ABA responses in Arabidopsis.";
RL Plant Cell Physiol. 52:874-884(2011).
CC -!- FUNCTION: Calcium-binding peroxygenase involved in the degradation of
CC storage lipid in oil bodies. May be involved in the interaction between
CC oil bodies and vacuoles during seed germination (By similarity). Acts
CC as a negative regulator of abscisic acid responses in non-seed tissues.
CC {ECO:0000250, ECO:0000269|PubMed:21471120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, shoots, flowers
CC and germinated seeds. Barely detected in dry seeds prior to
CC germination. Preferentially expressed in vascular bundles and in guard
CC cells. {ECO:0000269|PubMed:19467604, ECO:0000269|PubMed:21471120}.
CC -!- INDUCTION: Down-regulated by abscisic acid and high salt. Not induced
CC by salt stress or desiccation. {ECO:0000269|PubMed:19467604,
CC ECO:0000269|PubMed:21471120}.
CC -!- DOMAIN: Transmembrane regions are predicted by sequence analysis tools,
CC but these regions probably constitute hydrophobic domains associated to
CC phospholipids.
CC -!- DOMAIN: The proline-knot motif (70-79) may be involved in targeting to
CC lipid bodies.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but increased sensitivity
CC to exogenous abscisic acid and osmotic stresses. Increased drought
CC tolerance. {ECO:0000269|PubMed:21471120}.
CC -!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
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DR EMBL; AC011663; AAG52340.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35098.1; -; Genomic_DNA.
DR EMBL; AY056102; AAL06990.1; -; mRNA.
DR EMBL; AY143815; AAN28754.1; -; mRNA.
DR EMBL; AY088279; AAM65818.1; -; mRNA.
DR PIR; A96731; A96731.
DR RefSeq; NP_564995.1; NM_105735.3.
DR AlphaFoldDB; Q9CAB7; -.
DR STRING; 3702.AT1G70670.1; -.
DR PaxDb; Q9CAB7; -.
DR PRIDE; Q9CAB7; -.
DR ProteomicsDB; 226133; -.
DR EnsemblPlants; AT1G70670.1; AT1G70670.1; AT1G70670.
DR GeneID; 843404; -.
DR Gramene; AT1G70670.1; AT1G70670.1; AT1G70670.
DR KEGG; ath:AT1G70670; -.
DR Araport; AT1G70670; -.
DR TAIR; locus:2033632; AT1G70670.
DR eggNOG; ENOG502QTJ2; Eukaryota.
DR HOGENOM; CLU_062049_2_1_1; -.
DR InParanoid; Q9CAB7; -.
DR OMA; GQRNIND; -.
DR OrthoDB; 1423799at2759; -.
DR PhylomeDB; Q9CAB7; -.
DR BRENDA; 1.11.2.3; 399.
DR PRO; PR:Q9CAB7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAB7; baseline and differential.
DR Genevisible; Q9CAB7; AT.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0102070; F:18-hydroxyoleate peroxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:1990137; F:plant seed peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009819; P:drought recovery; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR InterPro; IPR007736; Caleosin-related.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR PANTHER; PTHR31495; PTHR31495; 1.
DR Pfam; PF05042; Caleosin; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 1: Evidence at protein level;
KW Calcium; Heme; Iron; Lipid droplet; Metal-binding; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..195
FT /note="Probable peroxygenase 4"
FT /id="PRO_0000415555"
FT DOMAIN 14..49
FT /note="EF-hand"
FT MOTIF 70..79
FT /note="Proline-knot"
FT BINDING 22
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81270"
FT CONFLICT 95
FT /note="G -> C (in Ref. 4; AAM65818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 195 AA; 22092 MW; BEF8CDD5D0623C96 CRC64;
MASSISTGVK FVPEEDNFLQ RHVAFFDRNK DGIVYPSETF QGFRAIGCGY LLSAVASVFI
NIGLSSKTRP GKGFSIWFPI EVKNIHLAKH GSDSGVYDKD GRFVASKFEE IFTKHAHTHR
DALTNEELKQ LLKANKEPND RKGWLAGYTE WKVLHYLCKD KNGLLHKDTV RAAYDGSLFE
KLEKQRSSKT SKKHP
