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Database: UniProt
Entry: A0A3Q3FXA0_9LABR
LinkDB: A0A3Q3FXA0_9LABR
Original site: A0A3Q3FXA0_9LABR 
ID   A0A3Q3FXA0_9LABR        Unreviewed;       887 AA.
AC   A0A3Q3FXA0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Eosinophil peroxidase-like {ECO:0000313|Ensembl:ENSLBEP00000024822.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000024822.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000024822.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR   AlphaFoldDB; A0A3Q3FXA0; -.
DR   STRING; 56723.ENSLBEP00000024822; -.
DR   Ensembl; ENSLBET00000026086.1; ENSLBEP00000024822.1; ENSLBEG00000018966.1.
DR   GeneTree; ENSGT00940000166204; -.
DR   InParanoid; A0A3Q3FXA0; -.
DR   OrthoDB; 4560at2759; -.
DR   Proteomes; UP000261660; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0032502; P:developmental process; IEA:UniProt.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00033; CCP; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR11475:SF63; EOSINOPHIL PEROXIDASE; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SMART; SM00032; CCP; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
DR   PROSITE; PS50923; SUSHI; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW   ProRule:PRU00302}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..887
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018540335"
FT   TRANSMEM        843..867
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          755..809
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   BINDING         508
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   887 AA;  98919 MW;  362A3F2A0B6119D2 CRC64;
     MDRAPMVSVC LLGLALILLS FSEHASMDAV SQNNSGVSET VYPGSVFVKE ALQRAIKLTD
     AAYARTSERV KKSLSEGALR PNDLLAQFKQ TEARTRTQIW AAELLDNTVE LIREMVYTHT
     MTIPSPHELL SEGDVENLLQ ATGCSTELQR PSCDTDCLSN RYRSLTGECN NRRHPRWGAA
     NIPYSRWLPP EYEDEWGMPR GWDPEHTYHN TTLPPVRLVS QEVLFTHNDN ISLDSTLSHL
     LVEWGQWIDH DIVLTPQSPS TASFRNGADC TRTCSRDTPC FPIQIPLSDP RYGIQSCMPF
     FRSAPSCVSG ILSHRQREQL NAITSFVDAS MVYGSSTSLA SALRNNSSPL GMMAHNSQHL
     DQELAYMPFL PRLQAHLDPC GPRNSTTSGE WDRSTHQKNT TSCFHAGDSR ANEHLGMIAL
     HTLFLREHNR LVKELHLLNP HWSPDTLYQE ARKILGAIHQ ILTWNHYLPL VLGEITMPHL
     MPPYEGYNPE VDPSIANAFA AAAFRFAHVT VHPVVNRLGP GYTTDSQHAP LPLHHSLFAS
     WRVIQEGGID PVLRGLLLSP AKLQTPGQMM VEELTERLFQ AQGGMPLDLG ALNLQRGRDH
     GLPGYCSWRK FCSLSVPNTT SELAEILSNF TLAHKLQLLY GTPHNIDVWV GAISEPALPG
     GRVGPLLSCL LARQFRALRD GDRFWWEREG LFTSTQRRHL HSVSLSRIIC DNSHITHVPA
     DPFSRTERPE DMLACSHPLI SKLDISPWKE PDTDPSCGPI PRIQSGYSLL CDSAILYQCR
     AGFKLLGSSS VKCDLNSQQW SPKPPTCEDI NECEEQSSLC QQNLECLNTP GSFICSEPFS
     QSAVSVVTAV IVVIGGVAVL LLIMFCYRRY FPKKEELINA ACCQGQS
//
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