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Database: UniProt
Entry: A0A2I3LXY7_PAPAN
LinkDB: A0A2I3LXY7_PAPAN
Original site: A0A2I3LXY7_PAPAN 
ID   A0A2I3LXY7_PAPAN        Unreviewed;      1415 AA.
AC   A0A2I3LXY7;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Peroxidasin {ECO:0000313|Ensembl:ENSPANP00000028326.2};
GN   Name=PXDN {ECO:0000313|Ensembl:ENSPANP00000028326.2};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000028326.2, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000028326.2, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000028326.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; 9555.ENSPANP00000028326; -.
DR   Ensembl; ENSPANT00000034426.2; ENSPANP00000028326.2; ENSPANG00000011093.3.
DR   GeneTree; ENSGT00940000157666; -.
DR   OrthoDB; 4560at2759; -.
DR   Proteomes; UP000028761; Chromosome 14.
DR   Bgee; ENSPANG00000011093; Expressed in aorta and 42 other cell types or tissues.
DR   ExpressionAtlas; A0A2I3LXY7; baseline.
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; 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; 2.
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:UP000028761};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          182..268
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          278..364
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          369..456
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          457..546
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1349..1407
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   REGION          1278..1316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1325..1352
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1278..1297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1299..1316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1010
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   1415 AA;  158486 MW;  9B520B03E2522F88 CRC64;
     MLTDLRFNRI REIQPGAFRR LRNLNTLLLN NNQIKRIPSG AFEDLENLKY LYLYKNEIQS
     IDRQAFKGLA SLEQLYLHFN QIETLDPESF QHLPKLERLF LHNNRITHLV PGTFNHLESM
     KRLRLDSNTL HCDCEILWLA DLLKTYAESG NAQAAATCEY PRRIQGRSVA AVTPEELNCE
     RPRITSEPRD ADVTSGNTVY FTCRAEGNPK PEIIWLRNNN ELSMKTDSRL NLLDDGTLMI
     QNTQETDQGI YQCMAKNVAG EVKTQEVTLR YFGSPARPTF VIQPQNTEVL VGESVTLECS
     ATGHPPPRIS WTRGDRTPLP VDPRVNITPS GGLYIQNVVQ EDSGEYACSA TNSIDSVHAT
     AFIIVQALPQ FTVTPQDRVV IEGQTVDFQC EAKGNPPPVI AWTKGGSQLS VDRRHLVLSS
     GTLRISGVAL HDQGQYECQA VNIIGSQKVV AHLTVQPRVT PVFASIPSDT TVEVGANVQL
     PCSSQGEPEP AITWNKDGVQ VTESGKFHIS PEGFLTINDV GPADAGRYEC VARNTIGSAS
     VSMVLSVNVP DVSRNGDPFV ATSIVEAIAT VDRAINSTRT HLFDSRPRSP NDLLALFRYP
     RDPYTVEQAR AGEIFERTLQ LIQEHVQHGL MVDLNGTSYH YNDLVSPQYL NLIANLSGCT
     AHRRVNNCSD MCFHQKYRTH DGTCNNLQHP MWGASLTAFE RLLKSVYENG FNTPRGINPH
     RLYNGHALPM PRLVSTTLIG TETVTPDEQF THMLMQWGQF LDHDLDSTVV ALSQARFSDG
     QHCSSVCSND PPCFSVMIPP NDSRARSGAR CMFFVRSSPV CGSGMTSLLM NSVYPREQIN
     QLTSYIDASN VYGSTEHEAR SIRDLASHRG LLRQGIVQRS GKPLLPFAAG PPTECMRDEN
     ESPIPCFLAG DHRANEQLGL TSMHTLWFRE HNRVAAELLK LNPHWDGDTI YYETRKIVGA
     EIQHITYQHW LPKILGEVGM RTLGEYQGYD PGINAGIFNA FATAAFRFGH TLVNPLLYRL
     DENFQPLAQG HLPLHKAFFS PFRIVNEGGI DPLLRGLFGV AGKMRVPSQL LNTELTERLF
     SMAHTVALDL AAINIQRGRD HGIPPYHDYR VYCNLSAAHT FEDLKNEIKN PEIREKLKRL
     YGSTLNIDLF PALMVEDLVP GSRLGPTLMC LLSTQFKRLR DGDRLWYENP GVFSPAQLTQ
     IKQTSLARIL CDNADNITRV QSDVFRVAEF PHGYGSCDEI PRVDLRVWQD CCEDCRTRGQ
     FNAFSYHFRG RRSLEFSYQE DQPTKKTRPR KIPSVGRHGE HLSNSTSAFS TRSDTPGTND
     FREFVLEMQK TITDLRTQIK KLESRLSTTE CVDAGGESYA NNTKWKKDAC TICECKDGQV
     TCFVEACPPA TCAVPTNIPG ACCPVCLQRR SEEKP
//
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