ID A0A3Q2LHJ1_HORSE Unreviewed; 1457 AA.
AC A0A3Q2LHJ1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peroxidasin {ECO:0000313|Ensembl:ENSECAP00000040420.2};
GN Name=PXDN {ECO:0000313|VGNC:VGNC:22055};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000040420.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000040420.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000040420.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000040420.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000040420.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
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DR STRING; 9796.ENSECAP00000040420; -.
DR PaxDb; 9796-ENSECAP00000040420; -.
DR Ensembl; ENSECAT00000058795.2; ENSECAP00000040420.2; ENSECAG00000019739.4.
DR VGNC; VGNC:22055; PXDN.
DR GeneTree; ENSGT00940000157666; -.
DR InParanoid; A0A3Q2LHJ1; -.
DR OMA; QHFKCAK; -.
DR Proteomes; UP000002281; Chromosome 15.
DR ExpressionAtlas; A0A3Q2LHJ1; baseline.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0004601; F:peroxidase activity; IBA:GO_Central.
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; 6.20.200.20; -; 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; 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 InterPro; IPR001007; VWF_dom.
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; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00093; VWC; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF57603; FnI-like domain; 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; PS51450; LRR; 3.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 224..310
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 320..406
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 411..498
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 499..588
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1391..1449
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT REGION 1320..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1052
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 1457 AA; 162462 MW; FA8AAB809901A720 CRC64;
MGLASQTWHV VFSPLFPRAP GIASFWVPLA SMSVAVPSVG RRPPRDLRFN RIREIQPGAF
RRLRNLNTLL LNNNQIKSIP GGSFEDLENL KYLYLYKNEI QSIDRQAFKG LSSLEQLYLH
FNQIETLDPE SFQHLPKLER LFLHNNRITH LVPGTFNHLE SMKRLRLDSN ALHCDCEILW
LADLLKTYAK SGNAQAAATC EHPRRIQGRS VATITPEELD CERPRITSEP QDADVTSGNT
VFFTCRAEGN PKPEIIWLRN NNELSMKTDS RLNLLDDGTL MIQNTQETDQ GIYQCMAKNV
AGEVKTQEVT LRYFGSPARP AFVIQPQNTE VLVGESVTLE CSATGHPVPR ITWTKGDQTP
VPEDPRVRVT PSGGLYIQNV AQEDSGEYAC TASNSIGSIH ATAFIIVQAL PQFTVTPQDR
AVIEGQTVDF QCEAKGYPQP VIAWTKGGSQ LSVDRRHLVL SSGTLRISGV ALHDQGQYEC
QAVNIIGSQR VVAHLTVQPR VTPVFASIPS DMTVEVGSNV QLPCSSQGEP EPAITWNKDG
VQVTESGKFH ISPEGFLTIH DVGTADAGRY ECVARNTIGQ ASVSMVLSVN VPDVSRNGDP
FVATSIVEAI ATVDRAINST RTHLFDSRPR SPNDLLALFR YPRDPYTVEQ ARAGEIFERT
LQLIQEHVQH GLMVDLNGTS YHYNDLVSPQ YLSLIANLSG CTAHRRVNNC SDMCFHQKYR
TQDGTCNNLQ HPMWGASLTA FERLLKSVYE NGFNTPRGIN PGRLYHGHPL PMPRLVSTSL
IGTEAITPDE QFTHMLMQWG QFLDHDLDST VVALSQARFS DGQHCSSVCG NDPPCFSVAI
PPNDPRVRSG ARCMFFVRSS PVCGSGMTSL LMNSVYPREQ INQLTSYIDA SNVYGSTDHE
ARAIRDLASH RGLLRQGIVQ RSGKPLLPFA TGPPTECMRD ENESPIPCFL AGDHRANEQL
GLTSMHTLWF REHNRVAAEL LSLNPHWDGD TIYHEARKIV GAQVQHITYQ HWLPKVLGEV
GMKMLGEYRG YEPGVNAGIF NAFATAAFRF GHTLVNPVLY RLDENFQPIA QGHIPLHKAF
FSPFRIVNEG GIDPLLRGLF GVAGKMRVPS QLLNTELTER LFSMAHTVAL DLAAINIQRG
RDHGIPPYHD YRVYCNLSSA HTFEDLKNEI KNPEIREKLR RLYGSPLNID LFPALMVEDL
VPGSRLGPTL MCLLSTQFKR LRDGDRLWYE NPGVFSPAQL TQIKQTSLAR ILCDNSDNIT
RVQRDVFRVA EFPHGYGSCD EIPRVDLRVW QDCCEDCRTR GQFNAFSYHF RGRRSLEFSY
EEDEPAKKAQ PGKTLSVGKR SQRPSNTTSA SYEHPQAPGT NEFKDFVLEM QRTITDLRAQ
IKKLESRLST SVCTDAAGQT RTDGAQWKQD ACTACECRDG QVTCFVEACA PAECPAPVRL
DGACCPVCLR DTAGNKP
//
