ID H2YK37_CIOSA Unreviewed; 1532 AA.
AC H2YK37;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=NAD(P)H oxidase (H2O2-forming) {ECO:0000256|ARBA:ARBA00012698};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
OS Ciona savignyi (Pacific transparent sea squirt).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000005686.1, ECO:0000313|Proteomes:UP000007875};
RN [1] {ECO:0000313|Proteomes:UP000007875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000005686.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Generates hydrogen peroxide which is required for the
CC activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a
CC role in thyroid hormones synthesis and lactoperoxidase-mediated
CC antimicrobial defense at the surface of mucosa. May have its own
CC peroxidase activity through its N-terminal peroxidase-like domain.
CC {ECO:0000256|ARBA:ARBA00003796}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:11264,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000518};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000547};
CC -!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005197}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004424}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the peroxidase
CC family. {ECO:0000256|ARBA:ARBA00005644}.
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DR STRING; 51511.ENSCSAVP00000005686; -.
DR Ensembl; ENSCSAVT00000005761.1; ENSCSAVP00000005686.1; ENSCSAVG00000003383.1.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000163963; -.
DR InParanoid; H2YK37; -.
DR OMA; AREVIYT; -.
DR TreeFam; TF105424; -.
DR UniPathway; UPA00194; -.
DR Proteomes; UP000007875; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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:0016174; F:NAD(P)H oxidase H2O2-forming activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0006590; P:thyroid hormone generation; IEA:UniProtKB-UniPathway.
DR CDD; cd09820; dual_peroxidase_like; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR034821; DUOX_peroxidase.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972:SF175; NAD(P)H OXIDASE (H(2)O(2)-FORMING); 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007875};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thyroid hormones biosynthesis {ECO:0000256|ARBA:ARBA00022534};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 920..941
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1028..1048
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1068..1088
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1109..1129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1163..1189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1201..1224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 804..839
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 840..875
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1252..1357
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 30..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 318
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 1532 AA; 175714 MW; B69C7346A27A4456 CRC64;
EYPPYDGWYN NRAHPDWGVV DGTLTRRLPS HYADGTYTPS GDERPNPRTI SQNTMAGNTG
LGSSVNLTAL MVFYGQHIVE EILDAQRAGC PPEYFNIKIP KGDPLYDNGG TGEVEMPFLR
TRYDQSSSGY SPNNPRQQLN EITPFIDGGL TYGINKAWSD ALRLLKKREL ASYKGEGKFP
LENSIGLPLI NPPPPRDNVI KSVTRFFRLG NPRGNENPFL LAFGMLWFRH HNWLARYLRD
QHSNWSDEKV YNEARVLNIA VHQKITMYDW LPLYLGECSA IAALNGTCEV VPNYTGYKSS
IHPGITNVFQ AAAMRFGHTL VPPGVYHRHA FQEAHVNRLG LRTCNTYGNS VEAIVESDID
KLMMGMASQI AEKEDNIITP DLRGSVFGPL DFSRRDLMAL NIQRGRDHGL PDYNTARKSF
GLKKRVTFEE INPVLFRNNA NNGGKLLQDV NDTHGGDISK MDVWTGGLLE TLPTGPGELF
RLIIRDQFIR IRDGDRFWFE NADNGLLTPS ELEFVRNTTI RDVILRTNPN LDPNFDIQQN
PFLWQSSDPL ALCPQPMQLN ETDMEECTAP ETFDYFTGSE LSYALTFASF GLFVICRSEQ
NKLQMRRAIN KHRSTKQGDS EISDIATEIL GPTRTREVQV KLSCCNQSFI KLKQCKIHIK
TASGRQNLRT IDLTKSKDVM ISTAYNRGRN TMFLRADKDT HDLVLKFNDT EERDYFIVRC
INFLQASNVP HKRNNMSLKQ LMEKASTSQM RDDALQKFFK AALSASLKLE DGGMYEVLNS
KEATKFIHIE LSKKEFADYF KLKPTSMFVD QMFTTADTDG SGSVSFREFL DIMVLFTKGS
PQDKAKLMFD MYDLDKSGQL SLKEFKTMLR SMMDMVNASV ATEQMEELVN TMLTTHGYQN
KQSLTLNDFQ IIMNKYSNEL IFMNTVLVVA CLSITFVFIC LSIKNYFFSI PIVKPIKVAK
WSRSITGDKM CKSKKNNPSL CRKTPVKKTQ QQKSRVQIKV SKKVFKPGRL NVWTMALANY
VQNYRLQIFW LTLYLLVLAG IFVERAYFYS VEREFAGLRR IAGYGVSITR GAASAMMFTY
SSLLVTMCRN TITALRETFL HLYIPFDSAI IMHRIIAWLA LIFTAMHIIG HSLNIYSIST
QTPGDLTCLF RDYWRLTNEL PKFHYWCWQT ITGITGVLLT LILIVMYTFA SDYSRRRIFK
WFWWTHNFGY IFLYFFMVLH GSGFLVQDPF FYYFFLGPAI LYTLDKLYSL SRSKSEISVV
NAELLPSDVT HLEFKRPVSF NYKAGQWVRI ACLSQSPNEY HPFTLTSAPH EETLKVHIRA
VGPWTINLRN IYNPDVLRDS PYPKLYLDGP FGEGHQDWYK YDVAVLVGGG IGVTPFAAIL
KDLVNMAQSG VRIQCKKVYF MWVTRDQKQY EWLTDIIQEV ESKDKNDLVD THIFITQFPQ
KFDLRTTMLY ICERQFQKVA GKSLFTGLRA VTHFGRPEFK SFFVSLTEEH TQVDKFGVFS
CGPPPMTNEV DKTCSKLNKY EGPTFLHHFE NF
//
