PXG5_ARATH
ID PXG5_ARATH Reviewed; 192 AA.
AC Q9CAB8; Q0WQP7; Q8L911;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable peroxygenase 5;
DE Short=AtPXG5;
DE EC=1.11.2.3;
DE AltName: Full=Caleosin-5;
GN Name=PXG5; Synonyms=CLO4, CLO5; OrderedLocusNames=At1g70680;
GN ORFNames=F5A18.14;
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].
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 [4]
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 [5]
RP GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11197322; DOI=10.1023/a:1026564411918;
RA Naested H., Frandsen G.I., Jauh G.Y., Hernandez-Pinzon I., Nielsen H.B.,
RA Murphy D.J., Rogers J.C., Mundy J.;
RT "Caleosins: Ca2+-binding proteins associated with lipid bodies.";
RL Plant Mol. Biol. 44:463-476(2000).
RN [6]
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).
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).
CC {ECO:0000250}.
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; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet. Microsome membrane {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, shoots and flowers.
CC {ECO:0000269|PubMed:11197322, ECO:0000269|PubMed:19467604}.
CC -!- INDUCTION: Not regulated by abscisic acid, desiccation and osmotic
CC stress. {ECO:0000269|PubMed:11197322, ECO:0000269|PubMed:19467604}.
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 (71-80) may be involved in targeting to
CC lipid bodies.
CC -!- SIMILARITY: Belongs to the caleosin 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; AC011663; AAG52337.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35099.1; -; Genomic_DNA.
DR EMBL; AY088690; AAM67011.1; -; mRNA.
DR EMBL; AK228644; BAF00552.1; -; mRNA.
DR PIR; B96731; B96731.
DR RefSeq; NP_564996.1; NM_105736.2.
DR AlphaFoldDB; Q9CAB8; -.
DR STRING; 3702.AT1G70680.1; -.
DR SwissPalm; Q9CAB8; -.
DR PaxDb; Q9CAB8; -.
DR PRIDE; Q9CAB8; -.
DR ProteomicsDB; 224804; -.
DR EnsemblPlants; AT1G70680.1; AT1G70680.1; AT1G70680.
DR GeneID; 843405; -.
DR Gramene; AT1G70680.1; AT1G70680.1; AT1G70680.
DR KEGG; ath:AT1G70680; -.
DR Araport; AT1G70680; -.
DR TAIR; locus:2033625; AT1G70680.
DR eggNOG; ENOG502QTJ2; Eukaryota.
DR HOGENOM; CLU_062049_2_1_1; -.
DR InParanoid; Q9CAB8; -.
DR OMA; SHELKAM; -.
DR OrthoDB; 1423799at2759; -.
DR PhylomeDB; Q9CAB8; -.
DR PRO; PR:Q9CAB8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAB8; baseline and differential.
DR Genevisible; Q9CAB8; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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 2: Evidence at transcript level;
KW Calcium; Endoplasmic reticulum; Heme; Iron; Lipid droplet; Membrane;
KW Metal-binding; Microsome; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..192
FT /note="Probable peroxygenase 5"
FT /id="PRO_0000415556"
FT DOMAIN 15..50
FT /note="EF-hand"
FT MOTIF 71..80
FT /note="Proline-knot"
FT BINDING 23
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 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81270"
FT CONFLICT 98
FT /note="Y -> H (in Ref. 4; BAF00552)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="I -> T (in Ref. 3; AAM67011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21519 MW; 9982C7ECAD677776 CRC64;
MASSISAAEV KVVPEEYNFL QKHVAFFDRN KDGIVYPSET FQGFRAIGCG YLLSTFAAVF
INISLSSKTR PGKGFSFSFP IEVKNVRLGI HSSDSGVYDK DGRFVASKFE EIFAKHAHTH
RDALTSKELK ELLKANREPN DCKGGILAFG EWKVLYNLCK DKSGLLHKEI VRAVYDGSLF
EQLEKQRSSK TP
