ID A0A2Y9JVE6_ENHLU Unreviewed; 732 AA.
AC A0A2Y9JVE6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Eosinophil peroxidase {ECO:0000313|RefSeq:XP_022365067.1};
GN Name=LOC111151375 {ECO:0000313|RefSeq:XP_022365067.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022365067.1};
RN [1] {ECO:0000313|RefSeq:XP_022365067.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022365067.1};
RG RefSeq;
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 RefSeq; XP_022365067.1; XM_022509359.1.
DR AlphaFoldDB; A0A2Y9JVE6; -.
DR STRING; 391180.A0A2Y9JVE6; -.
DR KEGG; elk:111151375; -.
DR OrthoDB; 4560at2759; -.
DR Proteomes; UP000248482; Unplaced.
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: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 Peroxidase {ECO:0000313|RefSeq:XP_022365067.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..732
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015877720"
FT BINDING 491
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 732 AA; 82439 MW; BAA4176EAFD2142E CRC64;
MQVSIPCPAV ARGLTAEKKL FLALAGVLAA LILALPCEST GSASPATVET SVLRDCITEA
KLLVDAAYNQ TQRSITERLR SGLASPMDLL SYFKQPLATT RTVVRAADYM HVALELLEGK
LQLQGSSSLN VTDVLTEPQL RLLSQASGCA LQDQEEKCSN KYRTITGRCN NRRRPLLGSS
NQALARWLPA EYEDRLSLPF GWTPNRRRNG FLLPLVRAVS NQIVRFPSER LTSDRGRALM
FMQWGQFIDH DLDFAPESPA RVAFTAGVDC EKSCAQLPPC FPIKIPPNDP RIRNQRDCIP
FFRSAPACPQ NRNKVRNQLN SLTSFLDASM VYGSEVSLAL RLRNQTNFLG LLAVNTRFSD
NGRALLPFDN LRDDPCLLTN REARIPCFLA GDSRSSETPK LAAMHTLFMR EHNRLATELK
RLNPQWTGDK LYQEARKIVG AMVQIITYRD FLPLVLGKAR ARRTLGPYRG YCSKVDPRVA
NVFTLAFRFG HTMLQPFMFR LDSQYRASAP NSRVPLSTSF FASWRVVHEG GIDPIIRGLM
ATPAKLNRQD SILVDELRDR LFQQVRRIGL DLAALNMQRS RDHGLPGYNA WRHFCGLSQP
RNLAQLSRVL QNQGLARKFL NLYGTPDNID IWIGAIAEPL LPGARVGPLL ACLFENQFRR
ARDGDRFWWE KRGVFTKRQR KALRKISLSR IVCDNTGITT VSRDIFRANT YPRGFVSCTS
IPKLNLSAWR GT
//