ID S4R8R6_PETMA Unreviewed; 662 AA.
AC S4R8R6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Peroxidasin {ECO:0000313|Ensembl:ENSPMAP00000001597.1};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000001597.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000001597.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 7757.ENSPMAP00000001597; -.
DR Ensembl; ENSPMAT00000001604.1; ENSPMAP00000001597.1; ENSPMAG00000001446.1.
DR GeneTree; ENSGT00940000157666; -.
DR HOGENOM; CLU_006087_2_2_1; -.
DR OMA; HTGFRRV; -.
DR Proteomes; UP000245300; 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:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF58; PEROXIDASIN; 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:UP000245300}.
FT REGION 72..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 405
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 662 AA; 73161 MW; 82A89FAB4B4AC25A CRC64;
FRYNDLVSPR YLELIANLSG CTAHRRAPSC SDACFHQRYR TVDGSCNNLQ HPMWGASLTA
FARLVEPAYE NGFNEPRGGG ASGRGRPRRG FPLPTPRRVS AELVGTEKIT PDERHTHMLM
QWGQFLDHDM DLTVVSPSQA RFSDGEPCAR ACTDDPPCFP IELLPDDPRG GRRGGGGGGA
AAAAAAAGRC MFFVRSSPVC GSGATSLLMS SVLPREQINQ LTSYIDGSNV YGSSEREAAD
VRDRSSRRGL LRRGIAVGAA GKHLLPFATG PPTEHMRDER ESPIPCFKKG DQRSNEQLGL
TSPRVSSHPL VRRDHALVSS PPPPPASTLV RLRQLNPHWD SDTIYHESRK IVGAQMQHIT
YAHWLPKVLG ADAMRSELRP YAGYDPSVNS AIFNSFATAA FRFGHTLINP VLLRLNESFQ
PIPEGHLPLH RAFFSPFRLV NEGGIDPLLR GLFATPAKKR VPSELLNLEL TEKLFHMAHS
VALDLASMNV QRGREHGLPS YAAYREFCNL TAAGDFEGLS GEIRDPVVRE KLRKCTHGLF
FLPENEKCAG GAIARWPIGS TSWGAGRQXL FTEQFRRLRD GDRLFWYENP GVFSPAQLTQ
IHQSSLSRVL CDNGDAITLV PPDAFAVSTY PQGYVACGTL PHVDLRMWQD CCQEREREDC
PH
//