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Database: UniProt
Entry: M4ATU6_XIPMA
LinkDB: M4ATU6_XIPMA
Original site: M4ATU6_XIPMA 
ID   M4ATU6_XIPMA            Unreviewed;       833 AA.
AC   M4ATU6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Eosinophil peroxidase-like {ECO:0000313|Ensembl:ENSXMAP00000017891.2};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000017891.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000017891.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000017891.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; M4ATU6; -.
DR   STRING; 8083.ENSXMAP00000017891; -.
DR   Ensembl; ENSXMAT00000017917.2; ENSXMAP00000017891.2; ENSXMAG00000017815.2.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00940000156009; -.
DR   HOGENOM; CLU_006087_1_1_1; -.
DR   InParanoid; M4ATU6; -.
DR   OMA; NSCMPFI; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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:UP000002852};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..833
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017282598"
FT   REGION          724..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          811..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..768
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         489
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   833 AA;  92406 MW;  4178C943D4464AF3 CRC64;
     MNKFLCLLAV GLTLALQCQV DAKRHLSQSF IEKCVNKAKT SVDEAYTYSR QVSLDRVKRN
     AASPADILRI LKQPNGPSRE AVRAADYMAN TLHVINHYLS KRHKRSINAT DLISKDDLGV
     IARLTGCAAQ VRNIHCQDLP NLNTYRTASS ICNNLKNPRW GASNIPFLRW LPSEYEDGIN
     SPKGWTHDLR VNNQLLPFVR EVSNRILAIN SSEVNSDPLY THLVTIFGQW TDHDITFTPQ
     SPSIRSFNDG IDCEKTCGNT EPCFPIEFPS NEPRIRDHSE KCMPFSRSAP ACGSGNTGYI
     FGSSTVRQQI NTLTAFIDVG QVYGSDDSKA RNLRNLTTDR GLLRVNNNYT DNGRDLLPFT
     TMGANMCATR RRMTNDNSAE EVLCFFAGDD RSNENIGLAS LHTLMMREHN RLVRALAQLN
     PKWDGERLYQ EARKIMGGYM QVITYRDYLL HIVGPEAVSK KLSTYPGYNE TIDPSIANVF
     ATAAYRFAHL MVQPFIFRLD ENYQDHPNYP TNLLHRTMFA PWRIVFEGGL DPILRGLIGR
     PAKLNTQDRM LTEELRDKLF KFSVNLALDL GSLNMQRGRD HGLPGYNKWR KFCGLSQPTT
     LSELAEVLNN TVLAQKLLDL YGTPDNIDPW LGGVAEPFVR GGRVGPLFAC LISTQFQNIR
     EGDRFWWENK GVFTDAQKLA IRDTSLARII CDNTGITEVP EKPFQYRPRG SGYTQCDAIP
     AFDLSPWKDG AEGPEKPQPP TGQPGPPGPP GPPGPIGLPG PPGPPGPSGA AAHVAFSVRL
     GSNVPKAGTP LPSMMSSTMD RTAMTPRLAF SPVSTQASMS LSSTAPSMTV QAA
//
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