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Database: UniProt
Entry: A0A0D9R3L2_CHLSB
LinkDB: A0A0D9R3L2_CHLSB
Original site: A0A0D9R3L2_CHLSB 
ID   A0A0D9R3L2_CHLSB        Unreviewed;      1479 AA.
AC   A0A0D9R3L2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Peroxidasin {ECO:0000313|Ensembl:ENSCSAP00000003201.1};
GN   Name=PXDN {ECO:0000313|Ensembl:ENSCSAP00000003201.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000003201.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000003201.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000003201.1}
RP   IDENTIFICATION.
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   EMBL; AQIB01029732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01029733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01029734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01029735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01029736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01029737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01029738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01029739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01029740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01029741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 60711.ENSCSAP00000003201; -.
DR   Ensembl; ENSCSAT00000004954.1; ENSCSAP00000003201.1; ENSCSAG00000006916.1.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00940000157666; -.
DR   OMA; QHFKCAK; -.
DR   OrthoDB; 4560at2759; -.
DR   Proteomes; UP000029965; Chromosome 14.
DR   Bgee; ENSCSAG00000006916; Expressed in fibroblast and 4 other cell types or tissues.
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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1479
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002344833"
FT   DOMAIN          246..332
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          342..428
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          433..520
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          521..610
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1413..1471
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   REGION          1342..1380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1389..1416
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1342..1361
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1363..1380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1074
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   1479 AA;  165093 MW;  432135E995511E28 CRC64;
     MAKLSRGPAR RCLLALVLCC AWGALAVVAQ KPGAGCPSRC LCFRTTVRCM HLLLEAVPAV
     APQTSILDLR FNRIREIQPG AFRRLRNLNT LLLNNNQIKR IPSGAFEDLE NLKYLYLYKN
     EIQSIDRQAF KGLASLEQLY LHFNQIETLD PESFQHLPKL ERLFLHNNRI THLVPGTFNH
     LESMKRLRLD SNTLHCDCEI LWLADLLKTY AESGNAQAAA TCEYPRRIQG RSVAAVTPEE
     LNCERPRITS EPQDADVTSG NTVYFTCRAE GNPKPEIIWL RNNNELSMKT DSRLNLLDDG
     TLMIQNTQET DQGIYQCMAK NVAGEVKTQE VTLRYFGSPA RPTFVIQPQN TEVLVGESVT
     LECSATGHPP PRISWTRGDR TPLPVDPRVN ITPSGGLYIQ NVVQEDSGEY ACSATNSIDS
     VHATAFIIVQ ALPQFTVTPQ DRVVIEGQTV DFQCEAKGNP PPVIAWTKGG SQLSVDRRHL
     VLSSGTLRIS GVALHDQGQY ECQAVNIIGS QKVVAHLTVQ PRVTPVFASI PSDTTVEVGA
     NVQLPCSSQG EPEPAITWNK DGVQVTESGK FHISPEGFLT INDVGPADAG RYECVARNTI
     GSASVSMVLS VNVPDVSRNG DPFVATSIVE AIATVDRAIN STRTHLFDSR PRSPNDLLAL
     FRYPRDPYTV EQARAGEIFE RTLQLIQEHV QHGLMVDLNG TSYHYNDLVS PQYLNLIANL
     SGCTAHRRVN NCSDMCFHQK YRTHDGTCNN LQHPMWGASL TAFERLLKSV YENGFNTPRG
     INPHRLYNGH ALPMPRLVST TLIGTETVTP DEQFTHMLMQ WGQFLDHDLD STVVALSQAR
     FSDGQHCSSV CSNDPPCFSV MIPPNDSRAR SGARCMFFVR SSPVCGSGMT SLLMNSVYPR
     EQINQLTSYI DASNVYGSTE HEARSIRDLA SHRGLLRQGI VQRSGKPLLP FAAGPPTECM
     RDENESPIPC FLAGDHRANE QLGLTSMHTL WFREHNRVAA ELLKLNPHWD GDTIYYETRK
     IVGAEIQHIT YQHWLPKILG EVGMRTLGEY QGYDPGINAG IFNAFATAAF RFGHTLVNPL
     LYRLDENFQP LAQGHLPLHK AFFSPFRIVN EGGIDPLLRG LFGVAGKMRV PSQLLNTELT
     ERLFSMAHTV ALDLAAINIQ RGRDHGIPPY HDYRVYCNLS AAHTFEDLKN EIKNPEIREK
     LKRLYGSTLN IDLFPALMVE DLVPGSRLGP TLMCLLSTQF KRLRDGDRLW YENPGVFSPA
     QLTQIKQTSL ARILCDNADN ITRVQSDVFR VAEFPHGYGS CDEIPRVDLR VWQDCCEDCR
     TRGQFNAFSY HFRGRRSLEF SYQEDKPTKK TRPRKIPSVG RHGEHLSNST SAFSTRSDTP
     GTNDFREFVL EMQKTITDLR TQIKKLESRL STTECVDAGG ESHANSTKWK KDACTICECK
     DGQVTCFVEA CPPATCAVPM NIPGACCPVC LQKRAEEKP
//
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