ID A0A2U3X3A9_ODORO Unreviewed; 566 AA.
AC A0A2U3X3A9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=NADPH oxidase 3 {ECO:0000313|RefSeq:XP_004416654.1};
GN Name=NOX3 {ECO:0000313|RefSeq:XP_004416654.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004416654.1};
RN [1] {ECO:0000313|RefSeq:XP_004416654.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_004416654.1; XM_004416597.1.
DR AlphaFoldDB; A0A2U3X3A9; -.
DR STRING; 9708.A0A2U3X3A9; -.
DR GeneID; 101373897; -.
DR KEGG; oro:101373897; -.
DR CTD; 50508; -.
DR InParanoid; A0A2U3X3A9; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 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; IPR000778; Cyt_b245_heavy_chain.
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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR PANTHER; PTHR11972:SF12; NADPH OXIDASE 3; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 284..394
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 566 AA; 64885 MW; 08F23FC379212A65 CRC64;
MECWILNESL SIILVLSWLG VNLYLFIDTF CWYEEEESFL YTRVILGSTL AWARASAVCL
NFNCMLILLP ISRNLISFMR GTSTCCRGPW RRQLDKNLKF HKLVAYGIAV NATIHIVAHL
CNLQRYHWSQ SAHAEGLLAV LSKLGNAPNE SYLNPIRTFH TNTITELLTT IAGVTGLIIS
LALILIMTSS TEFIRQVSYE LFWYTHHVFI IFFISLAIHG AGRIVRGQTP ESQLQHNVTF
CRDHYAQWQK AAPCPMPQFS GKEPSAWKWV LGPVVLYACE RIIRFWRFQQ DVVITKVVSH
PSGVLELHMK KRNFKMDPGQ YILIQCPSVS WLEWHPFTLT SAPQENFFSV HIRASGDWTE
ALCKAFRAEG PAPQELWSLP RLAVDGPFGT ALTDVFHYPV SVCIAAGIGV TPFASLLKSI
WYKSESQIQL KLSKVYFYWI CRDPKAFEWF ADLLLSLETL MSERGKAHFL SYHIFLTGWD
ENQAVHIALH WDESTDVITG LKQKTFYGRP NWSNEFRQMA YAHPSSSIGV FFCGPKALSK
TLQRMCRLYS SADPRGVHFY YNKESF
//
