ID M3YND0_MUSPF Unreviewed; 1434 AA.
AC M3YND0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Peroxidasin {ECO:0000313|Ensembl:ENSMPUP00000012837.1};
GN Name=PXDN {ECO:0000313|Ensembl:ENSMPUP00000012837.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000012837.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000012837.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
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DR EMBL; AEYP01018597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01018598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01018599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01018600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01018601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9669.ENSMPUP00000012837; -.
DR Ensembl; ENSMPUT00000013045.1; ENSMPUP00000012837.1; ENSMPUG00000012936.1.
DR eggNOG; KOG2408; Eukaryota.
DR GeneTree; ENSGT00940000157666; -.
DR HOGENOM; CLU_006087_0_1_1; -.
DR InParanoid; M3YND0; -.
DR OMA; QHFKCAK; -.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; IEA:Ensembl.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0043237; F:laminin-1 binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0070831; P:basement membrane assembly; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0001654; P:eye development; IEA:Ensembl.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:Ensembl.
DR GO; GO:0070207; P:protein homotrimerization; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd05745; Ig3_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; 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; PF13855; LRR_8; 1.
DR Pfam; PF01463; LRRCT; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 201..287
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 297..383
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 388..475
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 476..567
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1368..1426
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT REGION 1299..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1344..1371
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 1029
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 1434 AA; 159520 MW; 72FE51F53B7100D3 CRC64;
MTCPQKWRKS PSAKWISSWK TRDLRFNRIR EIQPGAFRKL RNLNTLLLNN NQIKSIPSGV
FQDLENLKYL YLYKNEIQSI DRQAFKGLAS LEQLYLHFNQ IETLDPESFQ HLPKLERLFL
HNNRITHLAP GTFDHLESMK RLRLDSNALR CDCAILWLAD LLRTYAQSGH AQAAATCEHP
RRVQGRSVAT VTPEELDCER PRITSEPQDA DVTSGNTVFF TCRAEGNPKP EIIWLRNNNE
LSMKTDSRLN LLDDGTLMIQ NTQETDQGIY QCMAKNVAGQ VKTQEVTLRY FGSPARPAFV
IQPQNTEVLV GESVTLECSA TGHPPPQVTW TKGDRTPLPE DPRVSITPSG GLYIQNVLQA
DSGEYTCFAS NSAGSIHAAA LIIVQALPQF TVTPADRAVI EGQTVDFQCE AKGYPQPVIA
WTKGGSPLSV DRRHLVLSSG TLRISAVALH DQGQYECQAV NIIGSQRAVA QLTVQPRVTP
VFASIPSDMT VEVGTSVQLP CSSQGEPEPA ITWNKDGVQV TESGKFHISP EGFLTIHDVG
TADAGRYECV ARNTIGQASV SMVLSVSVPD VSRNGDPFVA TSIVEAIATV DRAINSTRTH
LFDSRPRSPN DLLALFRYPR DPYTVGQARA GEIFERTLQL IQEHVRHGLM VDLNGTSYHY
NDLVSPQYLS LIANLSGCTA HRRVNNCSDM CFHQKYRTHD GTCNNLQRPM WGASLTAFER
LLKAVYENGF NTPRGIDPGR LYHGHALPMP RLVSTSLIGT DTITPDPQYT HMLMQWGQFL
DHDLDSTVVA LSQARFSDGQ HCSSVCSNDP PCFPVAVPPD DPRARSGARC MFFVRSSPVC
GSGMTSLLMN SVYPREQINQ LTSYIDASNV YGSSEHEARA VRDLASQRGL LRQGVVQRSG
KPLLPFAAGP PTECMRDENE SPIPCFLAGD HRANEQLGLT SLHTLWFREH NRVATELLAL
NPHWDGDTIY HEARKVVGAQ MQHITYRHWL PKVLGEVGMK ALGEYRGYDP GVNAGIVNAF
ATAAFRFGHT LINPVLYRLD ENFEPIAQGH VPLHKAFFSP FRIVNEGGID PLLRGLFGAA
SKMRVPSQLL NRELTERLFS MAHTVALDLA AINIQRGRDH GIPPYHEYRV YCNLSSAHTF
EDLKNEITSP EIREKLRRLY GSPLNIDLFP ALMVEDLVPG SRLGPTLMCL LSTQFKRLRD
GDRLWYENPG VFSPAQLTQI KQTSLARILC DNADNITRVQ RDVFRVAEFP HGYGSCDEIP
RVDLRVWQDC CEDCRTRGQF NAFSHHFRGR RSLGFSYQED EPIGEAGPGG TPSIGKHRKH
PGNATAPSHE HPQMPGTSDF KDFVQEMQKT IADLREQIKR LELRLSSTDC ADADGGPHAN
GAKWRRDACS VCECRDGQVT CFVEACPPAD CPAPVRASGA CCPVCPRDGM GRKP
//
