ID A0A091R448_MERNU Unreviewed; 787 AA.
AC A0A091R448;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Thyroid peroxidase {ECO:0000313|EMBL:KFQ34243.1};
DE Flags: Fragment;
GN ORFNames=N331_09679 {ECO:0000313|EMBL:KFQ34243.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ34243.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ34243.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ34243.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR EMBL; KK712496; KFQ34243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091R448; -.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0004447; F:iodide peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0006590; P:thyroid hormone generation; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd09825; thyroid_peroxidase; 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 InterPro; IPR029589; TPO.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF60; THYROID 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};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000313|EMBL:KFQ34243.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT DOMAIN 680..736
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT BINDING 434
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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ34243.1"
FT NON_TER 787
FT /evidence="ECO:0000313|EMBL:KFQ34243.1"
SQ SEQUENCE 787 AA; 88434 MW; 0F308EECD3701765 CRC64;
RSIQERGLAT PTLLLAFSKF PEQESQDISQ AAERMEMSIQ VLKQKVCQKH KRSLHPTDFL
SADLLTMIAN ISGCLPYMLP PKCPNNCLAN KYRLITGACN NREHPRWGAS NTALARWLPA
AYEDGLSQPQ GWDPTIRYNG VQLPLVREVT RKIIHASNEA VTEDNLYSDI IMVWGQYIDH
DIAFTPQSTS RTAFLNGKEC QMTCEKQNPC FPIKVTTNDT LSTGMDCLPF YRSSPACGTG
DHGILFGNLS ALTPRQQING LTSFLDASTV YGSTPAVENK LRNLTSKEGL LRVNIKYHDN
HREYLPFTDQ IPSPCAQDLN ASEGERIECF MAGDSRSSEV TSLAAMHTLW LREHNRLARA
LKNINSHWSA ETVYQEARKI VGALHQIITL RDYIPKIIGP DAFNLYIGLY TGYDPTMNPT
VSNVFSTAAF RFGHATIQPI VRRLNIQYLD DPGLPNLHLH EVFFSPWRLI KEGGLDPLLR
GLLAHSAKLQ VQDQLLNEEL TEKLFVLSNN GSLDLASLNL QRGRDHGLPG YNDWREFCGL
PKLETHTDLN TVITNDNITK KIMELYHNPS NIDVWLGGLV EDFLPGARTG PLFACLIGKQ
MKALRDGDRF WWENDNVFTE AQKHELKKHS LSRVICDNTG ISEVPADAFQ LGKFPEDFKH
CDNIPGMNLE AWQEFYQEEE ICGAPKSVEN GDFVYCSEFG KTTVTYSCQY GFQLQGEEQL
TCTSKGWNFE APICIDINEC ENKINPPCSP SAKCINTKGS YKCLHTDSYK LAEDGRTCIG
NVCEPTV
//
