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Database: UniProt
Entry: H2NTI5_PONAB
LinkDB: H2NTI5_PONAB
Original site: H2NTI5_PONAB 
ID   H2NTI5_PONAB            Unreviewed;       715 AA.
AC   H2NTI5; A0A2J8W7W4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=EPX isoform 1 {ECO:0000313|EMBL:PNJ65859.1};
DE   SubName: Full=Eosinophil peroxidase {ECO:0000313|Ensembl:ENSPPYP00000009255.2};
GN   Name=EPX {ECO:0000313|Ensembl:ENSPPYP00000009255.2};
GN   ORFNames=CR201_G0012117 {ECO:0000313|EMBL:PNJ65859.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000009255.2, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000009255.2, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ65859.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ65859.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000009255.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
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DR   EMBL; NDHI03003397; PNJ65859.1; -; Genomic_DNA.
DR   STRING; 9601.ENSPPYP00000009255; -.
DR   Ensembl; ENSPPYT00000009629.2; ENSPPYP00000009255.2; ENSPPYG00000008237.2.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00940000156009; -.
DR   HOGENOM; CLU_006087_1_1_1; -.
DR   OMA; PRWNGDK; -.
DR   OrthoDB; 4560at2759; -.
DR   TreeFam; TF314316; -.
DR   Proteomes; UP000001595; Chromosome 17.
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:Ensembl.
DR   GO; GO:0002215; P:defense response to nematode; IEA:Ensembl.
DR   GO; GO:0072677; P:eosinophil migration; IEA:Ensembl.
DR   GO; GO:0032693; P:negative regulation of interleukin-10 production; IEA:Ensembl.
DR   GO; GO:0032714; P:negative regulation of interleukin-5 production; IEA:Ensembl.
DR   GO; GO:0010936; P:negative regulation of macrophage cytokine production; IEA:Ensembl.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd09824; myeloperoxidase_like; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   PANTHER; PTHR11475:SF63; EOSINOPHIL PEROXIDASE; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..715
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041117983"
FT   BINDING         474
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ   SEQUENCE   715 AA;  81028 MW;  453F385E2CCAFF2E CRC64;
     MHLLPALAGV LATLVLAQPC EGTDPAFPGA VETSVLRDCI AEAKLLVDAA YNWTQKSIKQ
     RLRSGSASPM DLLSYFKQPV AATRTVVRAA DYMHVALGLL EEKLQPQRSR PFNVTDVLTE
     PQLRLLSQAS GCALRDQAER CSNKYRTITG RCNNKRRPLL GASNQALARW LPAEYEDGLS
     LPFGWTPGRR RNGFLLPLVR AVSNQIVRFP NERLTSDRGR ALMFMQWGQF IDHDLDFSPE
     SPARVAFTAG VDCERTCAQL PPCFPIKIPP NDPRIKNQLD CIPFFRSAPS CPQNKNRVRN
     QINALTSFVD ASMVYGSEVS LSLRLRNRTN YLGLLAINQR FQDNGRALLP FDNLHDDPCL
     LTNRSARIPC FLAGDTRSTE TPKLAAMHTL FMREHNRLAT ELRRLNPRWN GDKLYNEARK
     IMGAMVQIIT YRDFLPLVLG KARARRTLGP YRGYCSNVDP RVANVFTLAF RFGHTMLQPF
     MFRLDSQYRA SAPNSHVPLS SAFFASWRIV YEGGIDPILR GLMATPAKLN RQDAMLVDEL
     RDRLFRQVRR IGLDLAALNM QRSRDHGLPG YNAWRRFCGL SQPRNLAQLS RVLKNQDLAR
     KFLNLYGTPD NIDIWIGAIA EPLLPGARVG PLLACLFENQ FRRARDGDRF WWQKRGVFTK
     RQRKALSRIS LSRIICDNTG IATVSRDIFR ANIYPRGFVS CSRIPRLNLS AWQGK
//
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