PXG7_ARATH
ID PXG7_ARATH Reviewed; 210 AA.
AC B3H7A9; F4I4P7; Q8LE27; Q9LR37;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Probable peroxygenase 7;
DE Short=AtPXG7;
DE EC=1.11.2.3;
DE AltName: Full=Caleosin-7;
GN Name=PXG7; Synonyms=CLO7; OrderedLocusNames=At1g23240; ORFNames=F26F24.9;
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] (ISOFORM 3).
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 GENE FAMILY, AND NOMENCLATURE.
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 [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11431566; DOI=10.1126/science.1060972;
RA Mayfield J.A., Fiebig A., Johnstone S.E., Preuss D.;
RT "Gene families from the Arabidopsis thaliana pollen coat proteome.";
RL Science 292:2482-2485(2001).
CC -!- FUNCTION: Probable calcium-binding peroxygenase. May be involved in
CC pollination.
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: Secreted {ECO:0000269|PubMed:11431566}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=B3H7A9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B3H7A9-2; Sequence=VSP_042288, VSP_042289, VSP_042290;
CC Name=3;
CC IsoId=B3H7A9-3; Sequence=VSP_042287;
CC -!- TISSUE SPECIFICITY: Expressed in pollen coat.
CC {ECO:0000269|PubMed:11431566}.
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 (81-90) may be involved in targeting to
CC lipid bodies.
CC -!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87020.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005292; AAF87020.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30361.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30362.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30363.1; -; Genomic_DNA.
DR EMBL; AY085656; AAM62877.1; -; mRNA.
DR RefSeq; NP_001117339.1; NM_001123867.1. [B3H7A9-3]
DR RefSeq; NP_173738.2; NM_102173.4. [B3H7A9-1]
DR RefSeq; NP_973892.1; NM_202163.2. [B3H7A9-2]
DR AlphaFoldDB; B3H7A9; -.
DR STRING; 3702.AT1G23240.1; -.
DR iPTMnet; B3H7A9; -.
DR PaxDb; B3H7A9; -.
DR ProteomicsDB; 224805; -. [B3H7A9-1]
DR EnsemblPlants; AT1G23240.1; AT1G23240.1; AT1G23240. [B3H7A9-1]
DR EnsemblPlants; AT1G23240.2; AT1G23240.2; AT1G23240. [B3H7A9-2]
DR EnsemblPlants; AT1G23240.3; AT1G23240.3; AT1G23240. [B3H7A9-3]
DR GeneID; 838933; -.
DR Gramene; AT1G23240.1; AT1G23240.1; AT1G23240. [B3H7A9-1]
DR Gramene; AT1G23240.2; AT1G23240.2; AT1G23240. [B3H7A9-2]
DR Gramene; AT1G23240.3; AT1G23240.3; AT1G23240. [B3H7A9-3]
DR KEGG; ath:AT1G23240; -.
DR Araport; AT1G23240; -.
DR TAIR; locus:2028105; AT1G23240.
DR eggNOG; ENOG502QTJ2; Eukaryota.
DR InParanoid; B3H7A9; -.
DR OMA; NIKFGKH; -.
DR PhylomeDB; B3H7A9; -.
DR PRO; PR:B3H7A9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; B3H7A9; baseline and differential.
DR Genevisible; B3H7A9; AT.
DR GO; GO:0005576; C:extracellular region; 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:0016298; F:lipase activity; ISS:TAIR.
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 Alternative splicing; Calcium; Heme; Iron; Metal-binding; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Secreted.
FT CHAIN 1..210
FT /note="Probable peroxygenase 7"
FT /id="PRO_0000415557"
FT DOMAIN 25..60
FT /note="EF-hand"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 81..90
FT /note="Proline-knot"
FT BINDING 33
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 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81270"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_042287"
FT VAR_SEQ 1..19
FT /note="MSHQTVALASKAKSPKPKR -> MFFCFCFCESKKGLCMETYLWDYVVYVG
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042288"
FT VAR_SEQ 156..165
FT /note="LSDYGEWKIL -> FVVSELFQTN (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042289"
FT VAR_SEQ 166..210
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042290"
SQ SEQUENCE 210 AA; 23851 MW; 90F0899CDCD66445 CRC64;
MSHQTVALAS KAKSPKPKRG KLDKEKMTAL EKHVSFFDRN KDGTVYPWET YQGFRALGTG
RLLAAFVAIF INMGLSKKTR PGKGFSPLFP IDVKNSHLCM HGSDTDVYDD DGRFVESKFE
EIFNKHARTH KDALTAEEIQ KMLKTNRDPF DITGWLSDYG EWKILHTLAQ DKNGLLSEKS
VRAIYDGSLF HQLEKKRSSS SSRGKKQKLP
