Entry sw:PER68_ARATH

ID   PER68_ARATH             Reviewed;         325 AA.
AC   Q9LVL1;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   30-NOV-2016, entry version 118.
DE   RecName: Full=Peroxidase 68;
DE            Short=Atperox P68;
DE            EC=1.11.1.7;
DE   Flags: Precursor;
GN   Name=PER68; Synonyms=P68; OrderedLocusNames=At5g58400;
GN   ORFNames=MCK7.27;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
RA   Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA   Shibata K., Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=12034502; DOI=10.1016/S0378-1119(02)00465-1;
RA   Tognolli M., Penel C., Greppin H., Simon P.;
RT   "Analysis and expression of the class III peroxidase large gene family
RT   in Arabidopsis thaliana.";
RL   Gene 288:129-138(2002).
CC   -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
CC       biosynthesis and degradation of lignin, suberization, auxin
CC       catabolism, response to environmental stresses such as wounding,
CC       pathogen attack and oxidative stress. These functions might be
CC       dependent on each isozyme/isoform in each plant tissue.
CC   -!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl
CC       radical of the donor + 2 H(2)O.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
CC       subunit. {ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00297};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-
CC       ProRule:PRU00297}.
CC   -!- MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Classical plant
CC       (class III) peroxidase subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00297}.
DR   EMBL; AB019228; BAA96931.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97048.1; -; Genomic_DNA.
DR   EMBL; AK118274; BAC42892.1; -; mRNA.
DR   EMBL; BT008527; AAP40354.1; -; mRNA.
DR   RefSeq; NP_200648.1; NM_125226.4.
DR   UniGene; At.29282; -.
DR   ProteinModelPortal; Q9LVL1; -.
DR   SMR; Q9LVL1; -.
DR   STRING; 3702.AT5G58400.1; -.
DR   PeroxiBase; 234; AtPrx68.
DR   PaxDb; Q9LVL1; -.
DR   PRIDE; Q9LVL1; -.
DR   EnsemblPlants; AT5G58400.1; AT5G58400.1; AT5G58400.
DR   GeneID; 835953; -.
DR   Gramene; AT5G58400.1; AT5G58400.1; AT5G58400.
DR   KEGG; ath:AT5G58400; -.
DR   TAIR; AT5G58400; -.
DR   HOGENOM; HOG000237557; -.
DR   InParanoid; Q9LVL1; -.
DR   KO; K00430; -.
DR   OMA; MECYEQS; -.
DR   OrthoDB; EOG09360G9Q; -.
DR   PhylomeDB; Q9LVL1; -.
DR   BioCyc; ARA:AT5G58400-MONOMER; -.
DR   PRO; PR:Q9LVL1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; Q9LVL1; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00693; secretory_peroxidase; 1.
DR   InterPro; IPR010255; Haem_peroxidase.
DR   InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR   InterPro; IPR000823; Peroxidase_pln.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   InterPro; IPR033905; Secretory_peroxidase.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00458; PEROXIDASE.
DR   PRINTS; PR00461; PLPEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Complete proteome; Disulfide bond; Glycoprotein; Heme;
KW   Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   CHAIN        29    325       Peroxidase 68.
FT                                /FTId=PRO_0000023733.
FT   ACT_SITE     70     70       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00297, ECO:0000255|PROSITE-
FT                                ProRule:PRU10012}.
FT   METAL        71     71       Calcium 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00297}.
FT   METAL        74     74       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT   METAL        76     76       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT   METAL        78     78       Calcium 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00297}.
FT   METAL        80     80       Calcium 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00297}.
FT   METAL       198    198       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT   METAL       199    199       Calcium 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00297}.
FT   METAL       245    245       Calcium 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00297}.
FT   METAL       248    248       Calcium 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00297}.
FT   METAL       253    253       Calcium 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00297}.
FT   BINDING     168    168       Substrate; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT   SITE         66     66       Transition state stabilizer.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT   MOD_RES      29     29       Pyrrolidone carboxylic acid.
FT                                {ECO:0000250|UniProtKB:Q42578,
FT                                ECO:0000255|PROSITE-ProRule:PRU00297}.
FT   CARBOHYD     99     99       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    214    214       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     39    119       {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT   DISULFID     72     77       {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT   DISULFID    125    321       {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT   DISULFID    205    230       {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        61     72       ipat:PEROXIDASE_2 [T]
FT   MYHIT       190    200       ipat:PEROXIDASE_1 [T]
FT   MYHIT        29    325       iprf:PEROXIDASE_4 [T]
FT   MYHIT        46    289       ipfam:peroxidase [T]
SQ   SEQUENCE   325 AA;  35627 MW;  52CD84C9D11019B5 CRC64;
     MECYEQSRQR AAFVVLLFIV MLGSQAQAQL RTDFYSDSCP SLLPTVRRVV QREVAKERRI
     AASLLRLFFH DCFVNGCDAS ILLDDTRSFL GEKTAGPNNN SVRGYEVIDA IKSRVERLCP
     GVVSCADILA ITARDSVLLM GGRGWSVKLG RRDSITASFS TANSGVLPPP TSTLDNLINL
     FRANGLSPRD MVALSGAHTI GQARCVTFRS RIYNSTNIDL SFALSRRRSC PAATGSGDNN
     AAILDLRTPE KFDGSYFMQL VNHRGLLTSD QVLFNGGSTD SIVVSYSRSV QAFYRDFVAA
     MIKMGDISPL TGSNGQIRRS CRRPN
//