ID A0A401RX16_CHIPU Unreviewed; 683 AA.
AC A0A401RX16;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Thyroid peroxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=chiPu_0001073 {ECO:0000313|EMBL:GCC22685.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC22685.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC22685.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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:GCC22685.1}.
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DR EMBL; BEZZ01000015; GCC22685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401RX16; -.
DR STRING; 137246.A0A401RX16; -.
DR OMA; VENCCAV; -.
DR Proteomes; UP000287033; 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 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; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF60; THYROID 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..683
FT /note="Thyroid peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019438566"
FT BINDING 494
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 683 AA; 77127 MW; 885000F8A4189E93 CRC64;
MRVKTILCIA VMVGCVGLVL HFNKEGEEIV TEYLENPGDS FLPHAIQEGI NMVDGAIHHT
MKREIDVSKL PSSTELLSFS KRPEPESKKI SRAAEVMEMS VYLIQKEVHQ KYKRSTNSTD
LLSLEVLNAL ATTSGCLPHV QPLTCSNSCF IQKYRLINGT CNNRNNPRWG SSNIALTRWL
PPEYEDGYSQ PKGWNPECLY RGFKLPLVRD ITNKILRTSV QTNMTEDHLY SHILVEWGQY
IDHDFAFTPQ SISLAAFVGG VDCRSTCQNL NPCFPIKVHQ SDPHFKINEC ITFYRSSPSC
GTGHQEMPFE TLNPRQQINA VTSFIDASTV YGSNAAQATK LRNHSSEEGL LLTNAKYKDG
SYELLPFVDQ VPSPCLQAPN ATHSERVECF LAGEGRANEV LTLASMHTLW MREHNRLAKA
LHRMNSHWNS ETLYQETRKI IGALHQIITM RDYIPKILGS QAFDQRLGKY HGYDEMLNPT
LSNVFATAAF RFGHATISPR IQRLDENFKE HPKGLLAKPA KLQTSDQMMI EELTEKLFTL
TSAAAMDLAS LNLQRGRDHA LPGYNDWREF CELERLETKA NLRKAISDLD LVEKIMDLYG
HPNNIDIWLG GLAEDFLPGA RIGPLFACLI GKQMKTLREG DSQIIKKKGS LMLLSVYCEK
VNAFIDVNKL CIFDEYIKTG TTS
//