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Database: UniProt
Entry: A0A423TE13_PENVA
LinkDB: A0A423TE13_PENVA
Original site: A0A423TE13_PENVA 
ID   A0A423TE13_PENVA        Unreviewed;       844 AA.
AC   A0A423TE13;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=Chorion peroxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C7M84_006771 {ECO:0000313|EMBL:ROT74709.1};
OS   Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT74709.1, ECO:0000313|Proteomes:UP000283509};
RN   [1] {ECO:0000313|EMBL:ROT74709.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT74709.1};
RA   Zhang X., Yuan J., Li F., Xiang J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ROT74709.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT74709.1};
RA   Sun Y., Gao Y., Yu Y.;
RT   "The decoding of complex shrimp genome reveals the adaptation for benthos
RT   swimmer, frequently molting mechanism and breeding impact on genome.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ROT74709.1}.
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DR   EMBL; QCYY01001853; ROT74709.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423TE13; -.
DR   Proteomes; UP000283509; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd09823; peroxinectin_like; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   PANTHER; PTHR11475:SF106; CURLY SU; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..844
FT                   /note="Chorion peroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019296639"
FT   REGION          37..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         608
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   844 AA;  94689 MW;  DC33BAC5B74F884F CRC64;
     MKVVCVFLAM LLVIALASET TTLRIIEDNI SYVKRGKKSN QVTPEEHPGT QQVLGGTTWK
     SIETPPVLNI SKDDNVSRSS IEHGLTQLRE KDRIERDMAA KNMSVSHDSP TFIHQTLFKS
     FNNISYVKTR EEIQPGEPEE HPGTQQVLGG TTWKSIETPP VLNISKDDNV SRSSIEHGLT
     QLREKDRIER DMAAKNMSVS HDSPTFIHQT LFKSFSPQSI TAARTGFMID CATEFIMDRL
     QLNKTDITFD IIVSDQLAQE EFCDQDQVSS SCEAFSKYRS SNGTCNNLAN PLWGATFRPF
     RRVAPPDYGN GVSSLRRSQD GQPLPSARRV SAAVNSIRPN GESFLLSVLH MTYGQFLDHD
     LTFTPLNKGM YGDAIPCCPD ALGDPTLLHP ECAAISIPAD DPFYSRFNQT CMEFIRSAPA
     PRCLFGPREQ MNEKTAYIDG SQVYGIDDEM MNSLRTMDDG LLIAQMTNEG EELLPANTDL
     TNECNKAEQA SMNQFCFRAG DRRVNEQVLL VLFHTVWARH HNHLASRLKN INPSWNDEEL
     FQEARRIVGA QLQHVTYNEY LPPIFGENII KDSKLKPLKN KKRKNFYIPD KSAAISAEFA
     TAAFRFGHSQ IAGHMERVDD FGDISSTETS SVFMNPFVVY MKGAVPQLTR GEVRQSAGDV
     DPFFTPQVAG KLFKGMNMFG LDLMSLNIQR GRDHGIASYT ALRASCDLSS IHDFPDLSGI
     MDEDVIEILE DVYSHVDDID LFVGGLAEHP VEGGVVGPTF ACILLDQFLR LKVGDRYWYE
     TNDKDTRFKK EQVKEIRKTT LAGIMCEVIP ELTEIQESSE SGISRIQWYL ALLSKNWTSA
     TGKE
//
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