ID D6NHN5_PIG Unreviewed; 633 AA.
AC D6NHN5;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Thyroid peroxidase transcript variant 3 {ECO:0000313|EMBL:ADG45822.1};
GN Name=TPO {ECO:0000313|EMBL:ADG45822.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ADG45822.1};
RN [1] {ECO:0000313|EMBL:ADG45822.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20621020; DOI=10.1016/S1673-8527(09)60056-4;
RA Wang Y., Zhao X., Jiang X., Hua X., Xu N.;
RT "Molecular characterization of thyroid peroxidase gene in porcine (Sus
RT scrofa).";
RL J. Genet. Genomics 37:381-388(2010).
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
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; GU433217; ADG45822.1; -; mRNA.
DR AlphaFoldDB; D6NHN5; -.
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:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 2.
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; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF60; THYROID PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF00084; Sushi; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00032; CCP; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:ADG45822.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT DOMAIN 566..622
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT BINDING 321
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 633 AA; 69852 MW; 2DC500831E380E31 CRC64;
MGARAVLGVT LAVACAGAFF ASILRRKDLL GGDTEASGVA GLVEASRLLV DEPIHTTMRR
NLRKRGIFSP SQLLSFSKLP EPTSRTASRA AEIMETAVQE VKRRVCRRRD TDELPTDVLS
EELLSTMANL SGCLPHMLPA SSPHTCLANK YRLITGACNN RDHPRWGASN TALARWLPPA
YEDGVTEPRG WNPHFLYNGL PLPPVREVTR QVIHVSNEAV TEDGQYSDLL MAWGEYIDHD
IAFTPQSTSK AAFAGGADCQ LTCENRSPCF PIQIVTLRDY VPKILGAEAF GQHVGPYQGY
DPAVDPTVSN VFSTAAFRFG HATIHPLVRT LDARFQEHPG SHLPLRAAFF QPWRLLREGG
VDPVLRGLLA RPAKLQVQDQ LMNEELTERL FVLSNSGTLD LASINLQRGR DHGLPGYNEW
REFCGLSRLE TWADLSAATA NGRVADRILG LYQHPDNIDV WLGGLAESFL PGARTGPLFA
CIIGKQMRAL RDGDRFWWEN PGVFTEAQRR ELSRHSMSRV ICDNSGLSHV PLDAFRVGQW
PQEFEPCASI QGMDLGAWRE APPSGDACGF PDPVEDGGFL LCEERGQRVL VFSCRHGFRL
RGPAQITCTP RGWDSPPPLC KQDLSCGSRG LCE
//
