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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//