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Database: UniProt
Entry: M3Y689_MUSPF
LinkDB: M3Y689_MUSPF
Original site: M3Y689_MUSPF 
ID   M3Y689_MUSPF            Unreviewed;      1345 AA.
AC   M3Y689;
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 like {ECO:0000313|Ensembl:ENSMPUP00000006840.1};
GN   Name=PXDNL {ECO:0000313|Ensembl:ENSMPUP00000006840.1};
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:ENSMPUP00000006840.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000006840.1}
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; AEYP01091330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01091331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01091332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01091333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01091334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01091335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01091336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01091337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01091338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01091339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012903893.1; XM_013048439.1.
DR   STRING; 9669.ENSMPUP00000006840; -.
DR   Ensembl; ENSMPUT00000006954.1; ENSMPUP00000006840.1; ENSMPUG00000006895.1.
DR   KEGG; mpuf:101690178; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00940000163562; -.
DR   HOGENOM; CLU_006087_0_1_1; -.
DR   InParanoid; M3Y689; -.
DR   OMA; DCVARNS; -.
DR   OrthoDB; 4560at2759; -.
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; 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; IPR034824; Peroxidasin_peroxidase.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   PANTHER; PTHR11475:SF38; OXIDOREDUCTASE PXDNL-RELATED; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF07679; I-set; 4.
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; 3.
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; 1.
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          113..201
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          209..293
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          298..383
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          390..475
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1275..1333
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   COILED          1251..1278
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         939
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   1345 AA;  150626 MW;  471F4114007417A0 CRC64;
     MSLEQLYIHF NQIETLQAET FGDLLKLERL FLHNNRLSKI PAGSFSHLDS LKRLRLDSNA
     LVCDCDLMWL GELMQGYARN GQTQAAATCE YPRRLQGRSI ASLTVEEFNC ESPRITFEPQ
     DVEVTSGNTV YFTCRAEGNP KPKIIWIHNN HSLDLEDDSR FNLFDDGTLM IRNTRESDQG
     EYQCMARNSA GEVKTQNAML RYSSPPAKPS FIIQPQDTEV LIGTSTTLEC MATGHPHPHV
     TWTRGSGEAL DRSRHLTTSG GLYLQNVTLQ DHGQFTCHAD NNQGSVQATA NIIVQAPPQF
     RVIPKDQVVL EGHTVKFLCE AEGNPPPIIA WTKAGRQLSQ ESLHTVLSSG TLRIEHAAHY
     DQGQYECQAV SPLGVKKVSV QLTVKPKALP VFTQLPQDTS VEVGNNINIS CHAQGEPQPI
     ITWNKAGVQI TESGKFHVSG EGMLTIYDAG QADQGRYECV ARNSFGFVVT NMFLTVVAIQ
     GRQAGDDFVE SSILDAVQRV DSAINSTRRH LFSQKPRTPG DLLARFRYPH DPFTVETARA
     GEIFEHTLLL IQEHVKQGLT VDLEGREFRY NDLVSPHYLS LIANLSGCTA HRQVPNCSDM
     CFHQKYRAQD GTCNNLQHPT WGASLTAFER ILKPAYENGF NVPRGVGRHT LSGRLPLPPP
     RLVSTELVAT ATVTPDHQYT HMLMQWGQFL DHDLDHTVPA LSTSRFSDGR LCSSECTNDP
     PCFPIIIPDS DPRGTGAPCM FFARSSPVCG SGMTSLVMNS VYAREQINQL TAYIDASNIY
     GSSERESQIL RDYSEPRGLL RTGLPWVPSG KPLLPFSSGP PTECTRPEQD SRSPCFLAGD
     HRANEQLALT AMHTLWFREH NRVVTELSAL NPHWDGDTLY HEARKIVGAQ LQHITYSHWL
     PKILGEPGMK MLQDYQGYNP NVNAGIINSF ATAAFRFGHT LINPILYRLN DTFGEIPEGH
     LPLHKAFFSP SRIIEEGGID PLLRGLFGVA AKLRVPSQLL SVELTEKLFS MAHSVTLDLA
     ATNIQRGRDH GIPPYADFRV FCNLTSVENF EDLQNEIKDS EIRQKLKKLY STPGNIDFWP
     ALMVEDLIPG TRVGPTLMCL FVTQFQRLRD GDRFWYENPG VFTPAQLTQL KQASLGRVLC
     DNGDNIQQVQ ADVFVKAQYP QDYLSCSEIP QVDLRVWQDC CEDCRSRGQF RAFTQESRKK
     RSAQYSYPDE KDKNLSDLLS RQQDYLYIDE DGRHVTFLPK AEFAQDFSNF AVETQKTIKA
     LREQINKLEA RLRQAGCTDD KGIRRKDNEH WMKEDCVSCM CKSGQVTCVV ETCPPAPCPS
     LELVKGTCCP VCRGPGMPAD SSEKH
//
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