ID Q9XXZ8_HALRO Unreviewed; 918 AA.
AC Q9XXZ8;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE SubName: Full=Homologue of mammlian thyroid peroxidase {ECO:0000313|EMBL:BAA76689.1};
OS Halocynthia roretzi (Sea squirt) (Cynthia roretzi).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC Pyuridae; Halocynthia.
OX NCBI_TaxID=7729 {ECO:0000313|EMBL:BAA76689.1};
RN [1] {ECO:0000313|EMBL:BAA76689.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Endostyle {ECO:0000313|EMBL:BAA76689.1};
RA Ogasawara M., Di Lauro R., Satoh N.;
RT "Ascidian homologue of the mammalian thyroid peroxidase genes are expressed
RT in the thyroid equivalent region of endostyle.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
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; AB022197; BAA76689.1; -; mRNA.
DR AlphaFoldDB; Q9XXZ8; -.
DR PeroxiBase; 4076; HrPOX.
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:UniProtKB-KW.
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; 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:SF121; THYROID PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 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; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; 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:0000313|EMBL:BAA76689.1};
KW Peroxidase {ECO:0000313|EMBL:BAA76689.1}; 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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..918
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004338750"
FT TRANSMEM 852..874
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 744..797
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT BINDING 501
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 DISULFID 768..795
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 918 AA; 104250 MW; 135417E4BA2EE36F CRC64;
MSSNSLPSLS LGMLLVLFFV LSKIRNARCY EDHFQDTNRM QAEGDEFATK CMYEAMLNVN
RAIRRTDIHW RKDTVWDSPM DLFQFFKRPP NEDAERMARA SDIFETTVNY VNEKVLQKYR
RMKRRVNATD VLSSKTLRDL AAFSGCIGNP LLKQCPDTCI ASKYRTITGQ CNNLQNVYWG
SSNHQLVRWQ PSQYENGFSH PIGWNAETLR NNYRMPLVRK VSNDIIQTSN TNVTDDTDYS
HMLVVWGQYI DHDFDLTPQS LSTSTFQGLT NCQQTCRNEP PCFPILLPGE DSKRADAECL
PFFRSSAVCG SGETSSLFNE LKPREQMNAV TSFLDASTVY GSTDRMAYNL RNHTTDEGLM
RVNDRFYDEG GRIFLPFNPN NPCVQDQSDA SGERIPCFTA GDPRVSEHLT LSAIHTLWVR
AHNRIARELK RINPHWYGET IYQEARKIVG SLHQIVHYKE YVPKIIGMTG MNLLGEYSEY
NPSVNPTISN VFATAAFRFG HVTIAPIFRR LDGNFNEHPT HGNIFLHEAF FSPWRIIRQG
GLDPIFRGLI GRPAKLITGT QIMHEELREK LFQLQNKVAL DLASLNLQRG RDHAIPLYSY
WREFCNLTRV ETFDELASEI SDASVELNWQ NYTGHPGNLD LWLAGLVEDL VPGSRVGPTF
LCLLTKQFQY LRDGDRFFYE RVHTDEQIEE LEKIRLANVL CYNSGLETVQ RDVFSLAQYP
DDFVRCSDLD PLNLEPWREE PEVGSCGRPQ NIEYGDWQRC NDLVSYRCKM GFYLDGQEEL
TCMDNGAFNA EPPMCVDVNE CDQELKCNCE DICMNTVGSC RCMCSDGKIL NEDGRTCSES
PVTVVAPVGT NVAAIVTGVV LGVALLVLVV AVTYGVHKYT LLMQVATQAG TSSVNTVKMG
ISNSGFDSSS IDKTNMMH
//
