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Database: UniProt
Entry: A0A3B4XPB8_SERLL
LinkDB: A0A3B4XPB8_SERLL
Original site: A0A3B4XPB8_SERLL 
ID   A0A3B4XPB8_SERLL        Unreviewed;      1443 AA.
AC   A0A3B4XPB8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Peroxidasin {ECO:0000313|Ensembl:ENSSLDP00000017580.1};
GN   Name=PXDN {ECO:0000313|Ensembl:ENSSLDP00000017580.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000017580.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000017580.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   STRING; 1841481.ENSSLDP00000017580; -.
DR   Ensembl; ENSSLDT00000018189.1; ENSSLDP00000017580.1; ENSSLDG00000013799.1.
DR   GeneTree; ENSGT00940000157666; -.
DR   Proteomes; UP000261360; Unplaced.
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; 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; 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; 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; 4.
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1443
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017200560"
FT   DOMAIN          217..305
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          313..399
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          404..489
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          496..583
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1369..1427
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   REGION          1310..1331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1345..1372
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         1045
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   1443 AA;  161798 MW;  36D8C40DD8285E8E CRC64;
     MALRAGQLFS PCLLAVALLS LASGPQFGLC CPSRCLCFRT TVRCMHLNLE TVPAVSPQTT
     ILDLRFNKIK DIQPGSFRRL KNLNTLLLNN NHIRRIPRGA FEDLENLKYL YLHFNNIESL
     EPESFTHLPK LERLFLHNNR ITQLVPGTFS HLQAMKRLRL DSNALNCDCE LLWLADLLKQ
     YAESGNAQAA ATCDYPSRLQ GRSVATLTAE ELNCEVPRIT SEPQDVDVTS GNTVYFTCRA
     EGNPKPQIIW LRNNNALNMR DDSRLNLLED GTLMIQDTRE TDQGVYQCMA KNVAGEVKTS
     QVTLRYFGAP SRPSFVIQPQ NTEVLVGESV TLECSATGQP QPRVSWTKGD RTPLPNDARI
     NITPSGGLFI QNVVQADGGQ YTCFASNNVD TIHATAYIIV QAIPQLTVTP QDQSVLEGHT
     VDFPCEASGY PQPVIAWTRG GSPLPLDRRH AVLSSGTLRI TRVAAHDEGQ YECQAVSPVG
     TVQTAVQLSI QQRVTPVFTN APRDLTVESG QDVQIPCSAQ GQPQPVLTWN KDGVQVTESG
     KFHISPEGYL EVKDVGTADA GRYECVARNP IGYQVASMVL TVTVPAVSRE GDTFVSTSIE
     QAIRNVDSAI ESTRRRLFDG QPRTPGELLA LFRYPRDPYT VEQARAGEIF EQTLLLIQNH
     VNQGLMVDTN GTAFRYNDLV SPHFLDVIAN LSGCTAHRRF NNCSDICFHQ KYRSHDGTCN
     NLQHPMWGAS LTAFERLLKS VYDNGFNLPR GATERLHNGF RLPLPRLVST TMIGTETITP
     DDRYTHMLMQ WGQFLDHDLD STVAALSQSR FSDGQLCTQV CTNDPPCFPI QFPPNDPRQL
     RSGARCMFFV RSSPVCGSGM TSLLMNSVYP REQINQLTSY IDASNVYGSS RHESEEIRDL
     ASQRGLLRQG IIQRTGKPLL PFATGPPTEC MRDENESPIP CFLAGDHRAN EQLGLTAMHT
     VWFREHNRIA TELLRLNPHW DGDTIYHEAR KIVGAQMQHI TYSHWLPKIL GEAGMKMMES
     YAGYNPNINA GILNAFATAA FRFGHTLINP ILYRLDEEFQ PIPQGHISLH RAFFSPFRIV
     NEGGIDPLLR GLFGVAGKMR VSTQLLNTEL TERLFSMAHA VALDLAAMNI QRGRDHGIPP
     YNDYRTFCNL TSAQTFDELR NEIKNPSVRE KLQRLYGTPL NIDLFPALMA EDLVPGSRLG
     PTLMCLLVTQ FKRLRDGDRF WYENPGVFTP AQLTQLKQAS LTRVLCDNGD NITRIQQDVF
     RVAELPHGYG SCDDIPQIDL RMWQDCCEDC RTKGQFNALS YHFRGRRSAE HSYRENKPDD
     KSPVNVTLTS KKSTEPSVTD FQDFVSDMQK TITSLRKQIK RLEARLRKTD CTDSEGRERT
     DGERWKKDSC SICECRDAQV TCFVESCPPA KCKRPVKLKG ACCPVCLEQP DVDKRQEANT
     HHD
//
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