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Database: UniProt
Entry: G3P0M6_GASAC
LinkDB: G3P0M6_GASAC
Original site: G3P0M6_GASAC 
ID   G3P0M6_GASAC            Unreviewed;       883 AA.
AC   G3P0M6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Eosinophil peroxidase {ECO:0000313|Ensembl:ENSGACP00000011149.1};
GN   Name=EPX {ECO:0000313|Ensembl:ENSGACP00000011149.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000011149.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000011149.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000011149.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   AlphaFoldDB; G3P0M6; -.
DR   Ensembl; ENSGACT00000011172.1; ENSGACP00000011149.1; ENSGACG00000008429.1.
DR   GeneTree; ENSGT00940000156009; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000008429; Expressed in pharyngeal gill and 4 other cell types or tissues.
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; 2.60.120.40; -; 1.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   PANTHER; PTHR11475:SF63; EOSINOPHIL PEROXIDASE; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF00386; C1q; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   SUPFAM; SSF49842; TNF-like; 1.
DR   PROSITE; PS50871; C1Q; 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:UP000007635};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..883
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003449074"
FT   DOMAIN          756..883
FT                   /note="C1q"
FT                   /evidence="ECO:0000259|PROSITE:PS50871"
FT   REGION          131..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..756
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         483
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   883 AA;  98713 MW;  4FF2B987CBC9BA33 CRC64;
     RQQLLFLFKV NCVCFLLIRL SESHLSRSAI ERAVIAAKAT VDSAYEYSRR VSVDRVRRNA
     VSPSDVLRLL KQPAGATRNA VRSADYMENA VKLIQASLHR RQKRSINATD LISAEDLKFI
     AELTGCSARR QNPTCPTESK FRTPSNTCNN RKNPRWGASN TPFARWLPAE YQDGISLPKG
     FDPERKVNSF VLPLVRAVSN NILKTAKADV EIDPLYTYLV TIFAQWTDHD LTLTPTSPVI
     RSFNNGMDCA KSCENSEPCF PIKFPKNDPR NASEECIPFF RSAPACGSGN TGHIFGASTV
     RQQINSLTAF LDVGQVYGSE DTKVRFLRNL TSNEGLLRVN TRFDDNGREL LPFSSMTTNM
     CATRKRITND SFAEEVPCFV AGDDRVDENI GLNSLHTLFM REHNRLARAL AKLNPHWDGE
     RLYQEARKIM GGYTQVLTFR DFLHHIVGPD FIASHLSTYP GYDENVDPSI ANVFATAAFR
     FAHLMVQPKM FRLNEQYEEH PVYPSPLLHK SFFAPWRVVF EGGVDPLIRG LVGRQAKLNT
     QDNMMTDELR DRLFQFTQKL ALDLASLNMQ RARDHAIPGY NQWRKFCGLS QPKNLNELSQ
     VLNNRDLAKR LLDLYSTPDN IDVWLGGVAE PFVRGARVGP LFACLISTQF QRIRQGDRLW
     WENDGVFTDA QKNSLRSTSL ARIICDNTGI TEVPEKPFQY RPRGTGYTKC ENIAPFDLGP
     WKENSNERGP PGPPGPSGPS GPPGPPGPPG PPGPPGSAHK VAFSVRLGNN FPKPGVPLVF
     RDVIYNGQNS YDTSTGVFTC AQPGVYEFQF HCTIHDGTGS VDLIRNSKLI LHSFTTTQSG
     YLIASGSVYV KLDKGDRVYL VANYGGNGLT TDSYFSGHLL FTE
//
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