ID A0A3P8Q875_ASTCA Unreviewed; 1466 AA.
AC A0A3P8Q875;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peroxidasin {ECO:0000313|Ensembl:ENSACLP00000025695.1};
GN Name=PXDN {ECO:0000313|Ensembl:ENSACLP00000025695.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000025695.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000025695.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000025695.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSACLT00000026308.1; ENSACLP00000025695.1; ENSACLG00000017492.1.
DR GeneTree; ENSGT00940000157666; -.
DR OrthoDB; 4560at2759; -.
DR Proteomes; UP000265100; Chromosome 19.
DR Bgee; ENSACLG00000017492; Expressed in zone of skin and 7 other cell types or tissues.
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; 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 Membrane {ECO:0000256|ARBA:ARBA00022989};
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, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1466
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018288691"
FT DOMAIN 234..322
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 330..416
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 421..506
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 513..600
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1398..1456
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT REGION 1331..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1374..1401
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1332..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1062
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 1466 AA; 164304 MW; 9451466BF2384897 CRC64;
MALRAALLSS LLLLCAVRRF GLCCPSRCLC FRTTVRCMHL NLETVPAVSP QTTILDLRFN
KIKDLQPGSF RRLKNLNTLL LNNNHIRRIP RGAFEDLENL KYLYLYKNEI QSIDRQAFKG
LVSLEQLYLH FNNIESLEPE SFTHLPKLER LFLHNNRITQ LVPGTFSHLQ AMKRLRLDSN
SLNCDCELLW LADLLKQYAE SGNAQAAATC DYPSRLQGRS VATLTAEELN CEVPRITSEP
HDVDVTSGNT VYFTCRAEGN PKPQIIWLRN NNALNMRDDS RLNLLEDGTL MIQNTRETDQ
GVYQCMAKNV AGEVKTSEVT LRYFGAPSRP SFVIQPQNTE VLVGESVTLE CSATGQPQPR
VSWTKGDRTP LPNDARITIT PSGGLYIQNV EQADGGQYTC FASNNVDTIH ATAHIIVQAI
PQFTVTPQDQ LALEGHTVDF PCEATGYPQP VIAWTRGGSP LPSDRRHVTL PSGTLRITRV
AAHDEGQYEC QAVSPVGTTR TAVQLSIQQR VTPVFTNAPR DLTVESGQDV QIPCSAQGQP
QPVLTWNKDG VQVTESGKFH ISPDGYLEVK DVGTADAGRY ECVARNPIGY QVASMVLTVT
VPAISREGDT FVSTSIEQAI RTVDSAIEST RRRLFDGQPR TPGELLALFR YPRDPYTVEQ
ARAGEIFEQT LLLIQNHVNQ GLMVDTNGTA FRYNDLVSPR FLDMIANLSG CTAHRRINNC
SDICFHQKYR SHDGTCNNLQ HPMWGASLTA FERLLKSVYD NGFNLPRGAT DRVHNGYKLP
LPRLVSTTMI GSETITPDDR YTHMLMQWGQ FLDHDLDSTV VALSQSRFSD GQLCAQVCTN
DPPCFPIQFP PNDQRQLRSG ARCMFFVRSS PVCGSGMTSL LMNSVYPREQ INQLTSYIDA
SNVYGSSRHE SEEVRDLASQ RGLLRQGIIQ RTGKPLLPFA SGPPTECMRD ENESPIPCFL
AGDHRANEQL GLTAMHTAWF REHNRIATEL LRLNPHWDGD TIYHEARKIV GAQMQHITYS
HWLPKILGEV GMKMMGPYGG YDPNVNAGVF NAFATAAFRF GHTLINPILY RLDEDFQPIP
QGHISLHRAF FSPFRIVNEG GIDPLLRGLF GVAGKMRVTT QLLNTELTER LFSMAHAVAL
DLAAMNIQRG RDHGIPPYND YRTFCNLTSA RTFDDLKNEI KNPSVREKLQ RLYGTPLNID
LFPALMAEDL VPGSRLGPTL MCLLTTQFKR VRDGDRFWYE NPGVFTPAQL TQLKQASLAR
VLCDNGDNIT RVQRDVFRVA ELPHGYISCD DVPQIDLRMW QDCCEDCRTK GQFNALSYHF
RGRRSAEHSY KEYKPASSSQ ENSSVEETPG SLGNVSATSR KSTEPSINDF QDFVSDMQKT
ITSLRKQIKR LEARLSTTDC TDSEGRERAD GERWKKDPCA TCECRDAQVT CFVESCPATE
CKRPVKLKGS CCPVCLEQLT APARRP
//
