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Database: UniProt
Entry: G1NMG8_MELGA
LinkDB: G1NMG8_MELGA
Original site: G1NMG8_MELGA 
ID   G1NMG8_MELGA            Unreviewed;      1130 AA.
AC   G1NMG8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 3.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Peroxidasin {ECO:0000313|Ensembl:ENSMGAP00000014780.3};
GN   Name=PXDN {ECO:0000313|Ensembl:ENSMGAP00000014780.3};
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000014780.3, ECO:0000313|Proteomes:UP000001645};
RN   [1] {ECO:0000313|Ensembl:ENSMGAP00000014780.3, ECO:0000313|Proteomes:UP000001645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA   Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA   Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA   Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA   Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA   Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA   Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA   Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA   Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA   Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA   Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA   Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA   Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA   Zhang Y., Reed K.M.;
RT   "Multi-platform next-generation sequencing of the domestic turkey
RT   (Meleagris gallopavo): genome assembly and analysis.";
RL   PLoS Biol. 8:E1000475-E1000475(2010).
RN   [2] {ECO:0000313|Ensembl:ENSMGAP00000014780.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; G1NMG8; -.
DR   Ensembl; ENSMGAT00000015720.3; ENSMGAP00000014780.3; ENSMGAG00000013971.3.
DR   GeneTree; ENSGT00940000157666; -.
DR   HOGENOM; CLU_006087_0_1_1; -.
DR   TreeFam; TF314316; -.
DR   Proteomes; UP000001645; Chromosome 2.
DR   Bgee; ENSMGAG00000013971; Expressed in gizzard and 16 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd05745; Ig3_Peroxidasin; 1.
DR   CDD; cd05746; Ig4_Peroxidasin; 1.
DR   CDD; cd09826; peroxidasin_like; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR047018; Peroxidasin_Ig-like3.
DR   InterPro; IPR034828; Peroxidasin_Ig-like4.
DR   InterPro; IPR034824; Peroxidasin_peroxidase.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   PANTHER; PTHR11475:SF75; PEROXIDASIN HOMOLOG; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF07679; I-set; 4.
DR   Pfam; PF13855; LRR_8; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SMART; SM00406; IGv; 3.
DR   SMART; SM00369; LRR_TYP; 1.
DR   SMART; SM00082; LRRCT; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS50835; IG_LIKE; 4.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR619791-2};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          91..177
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          187..273
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          278..365
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          366..455
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   BINDING         919
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   1130 AA;  126421 MW;  1E37BF7085B57BA6 CRC64;
     HLPKLERLFL HNNRIAHLIP GTFSHLESMK RLRLDSNALH CDCEILWLAE LLKTYVESGN
     AQAAATCEYP RRIQGRSVAT ITPEELNCER PRITSEPQDV DVTSGNTVYF TCRAEGNPKP
     EIIWLRNNNE LIMKEDSRLN LLDDGTLMIQ NTQETDQGIY QCMAKNVAGE VKTQEVTLRY
     FGSPARPSFV IHPQNTEVLV GESVTLECSA TGHPQPQITW TKGDRTPLPS DPRITITPSG
     GLYIQNVKQE DSGEYTCFAT NSVGNIHATA YIIVQALPQF TVTPQDKTVI EGQTVDFPCE
     AQGYPQPVIA WTKGGGQLSV DRRHLVLSSG TLRISRVALH DQGQYECQAV NIIGSQRIVV
     YLTVQPRVTP VFASVPSDMT VEVGTNVQIP CSAQGEPEPV ITWNKDGVQV TESGKFHVSP
     EGYLTIRDVG TADEGRYECV ARNTIGYSSV SMVLSVNVPN VSRNGDPFVQ TSIVEAIATV
     DRAINSTRTH LFDSRPRSPN DLLALFRYPR DPYTVEQARA GEIFERTLQL IQDHVQDGLM
     VDLNGTSYHY NDLVSPQYLN LIANLSGCTA HRRVNNCSDM CFHQKYRTHD GTCNNLQHPM
     WGASLTAFER LLKSVYENGF NLPRGIEPKR LSNGYALPMP RLVSTTLIGT ETITPDEQYT
     HMLMQWGQFL DHDLDLTVAA LSEARFSDGQ HCSSVCTNDP PCFSIMIPPN DPRVRNGARC
     MFFVRSSPVC GSGMTSLLMN SVYPREQINQ LTSYIDASNV YGSSDHEALE IRDLASQRGL
     LRQGIVQRSG KPLLPFATGP PTECMRDENE SPIPCFLAGD QRSNEQLGLT SIHTLWFREH
     NRIATELLKL NPHWDGDTIY HETRKIVGAE MQHITFSHWL PKIFGEVGMK MLGEYKGYDP
     SVNSGITNEF ATAAFRFGHT LINPFLYRLD ENFEPIPQGH LPLHKAFFSP FRIVNEGGID
     PLLRGLFGVA GKMRVPSQLL NTELTERLFS MARTVALDLA AMNIQRGRDH GIPPYHDFRV
     YCNLSSAQTF EDLKNEIKNP EIREKLSRLY GSPLNIDLFP ALMVEDLVPG SRLGPTLMCL
     LTDIIHLLSL TFNDFIDKEI AIIKTCTISA IKLGLRKYCS VHLIPVRFSI
//
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