ID A0A3P8UDY7_CYNSE Unreviewed; 1440 AA.
AC A0A3P8UDY7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peroxidasin {ECO:0000313|Ensembl:ENSCSEP00000000049.1};
GN Name=PXDN {ECO:0000313|Ensembl:ENSCSEP00000000049.1};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000000049.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000000049.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000000049.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 244447.ENSCSEP00000000049; -.
DR Ensembl; ENSCSET00000000073.1; ENSCSEP00000000049.1; ENSCSEG00000000065.1.
DR GeneTree; ENSGT00940000157666; -.
DR InParanoid; A0A3P8UDY7; -.
DR Proteomes; UP000265120; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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:SF75; PEROXIDASIN HOMOLOG; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF13927; Ig_3; 1.
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 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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 215..303
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 311..397
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 402..487
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 494..580
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1365..1423
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT REGION 1307..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1042
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 1440 AA; 161326 MW; 811D51AB17ADF018 CRC64;
MQPGGALCPT RTLLCLTIQH GGCGPPLVHR CGVWSLDLRF NKIKDIQPGS FRRLKNLNTL
LLNNNHIRSI PRGAFEDLEN LKYLYLYKNE IQSIDRQAFK GLVSLEQLYL HFNNIESLEP
ESFTFLPKLE RLFLHNNRIT HLVPGTFSHL QTMKRLRLDS NALNCDCELL WLADLLKQYA
ESGNAQAAAT CDYPSRLQGR SVATLTAEEL NCEVPRITSE PQDVDVTSGN TVYFTCRAEG
NPKPQIIWLR NNNALNMRDD SRLNLLEDGT LMIQNTRETD QGVYQCMAKN VAGEVKTSEV
TLRYFGAPSR PSFVIQPLNT EVLVGESVTL ECSATGQPQP RISWTKGDRT PLPSDARIST
TASGGLYIQQ VVQSDAGQYT CFASNNVDTI HATAFIIVQA VPEFTVTPQD LSVVEGQSVD
FPCEARGYPQ PVIAWTRGGS PLPLDRRLVV LSSGTLRITR VAAHDEGQYE CQAVSPVGSV
QTAVQLGIQQ RVTPVFTNTP RDQTVVTGQD VRIPCRCRCL YELFFLLQDG VQVTESGKFH
ISPEGYLEVK DVGTADAGRY ECVARNPIGY QVAPMVLTVT VPAVSREGDL FVSTSIEQAI
RSVDSAIEST RRRLFDGQPR TPGELLALFR YPRDPYTVEQ ARAGEIFEQT LLLIQNHVNQ
GLMVDTNGTA FRYNDLVSPH FLDVIANLSG CTAHRRFNNC SDICFHQKYR SHDGTCNNLQ
HPMWGASLTA FERLLKSVYD NGFNLPRGTT ERLHNGYRLP LPRLVSTTMI GTETITPDDR
YTHMLMQWGQ FLDHDLDSTV AALSQSRFSD GQLCAQACTN DPPCFPIQFP PNDQRQLRSG
ARCMFFVRSS PVCGSGMTSL LMNSVYPREQ INQLTSYIDA SNVYGSSRHE SEEIRDLASQ
RGLLRQGIIQ RTGKPLLPFA TGPPTECMRD ENESPIPCFL AGDHRANEQL GLTAMHTVWF
REHNRIATEL LRLNPHWDGD TIYHEARKIV GAQMQHITYS HWLPKILGEA GVKMMGPYTG
YDPNINAAIF NAFATAAFRF GHTLINPILY RLDDDFQPIP QGHISLHRAF FSPFRIVNEG
GIDPLLRGLY GVAGKMRVTT QLLNTELTER LFSMAHAVAL DLAAMNIQRG RDHGIPSYND
YRTFCNLTSA QTFDDLRNEI KNPTVREKLQ RLYGTPLNVD LFPALMAEDL VPGSRLGPTL
MCLLAAQFKR LRDGDRFWYE NPGVFTPAQL TQLKQASLTR VLCDNGDNIT RVQADVFRVA
ELPHGYGSCD DVPQIDLRMW QDCCEDCRTK GQFNALSYHF RGRRSADHSY QEDKPDVDQP
SSPVNVTLTS KKSTEPSVND FQDFVSDMQK TIPSLRKLEA RLSKTDCTDS EGHDRTDGER
WKKDSCTTCD CSKTQVTCFV ESCPPVKCQR PVKLKGTCCP VCLPPADDDD KGREASTQQN
//
