ID A0A1S3J0E5_LINUN Unreviewed; 607 AA.
AC A0A1S3J0E5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=NADPH oxidase 4 isoform X1 {ECO:0000313|RefSeq:XP_013403279.1};
GN Name=LOC106168672 {ECO:0000313|RefSeq:XP_013403279.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013403279.1};
RN [1] {ECO:0000313|RefSeq:XP_013403279.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013403279.1};
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_013403279.1; XM_013547825.1.
DR AlphaFoldDB; A0A1S3J0E5; -.
DR STRING; 7574.A0A1S3J0E5; -.
DR EnsemblMetazoa; XM_013547825.1; XP_013403279.1; LOC106168672.
DR GeneID; 106168672; -.
DR KEGG; lak:106168672; -.
DR InParanoid; A0A1S3J0E5; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000085678; 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 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:SF209; NADPH OXIDASE 4; 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 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:UP000085678};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 327..444
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 607 AA; 69514 MW; 2F5B5DC9C835C7FD CRC64;
MNMWRWLRGF LRNCGLRYSV VVLWIVLNAV VFTSTYRHWK YAPKYYYVHQ ILGPTLCISR
GTAAVLNLNC GLVLLPMCRV LVSLMRFSRI SRRSFRMLLD HCKGFHMLCG LTIVLASVIH
FIGHLFNAAN FSIHFNPYYV DVNGASYKGQ DPLYIVAGSV PGITGLVLML VLCTMATTSL
YVVRTNNYDL FWYTHRFYLV FYFFLMVHAV RGVLKEQINL SRHSPGCDKE NLNLSIPWPE
PEHWDTQETV CEEPPVFGTV GCSVCILHNT VCEEPPVFGT VGCSVCILHN TVCEEPPVFG
TVGCSSWMWV GLPLLVYLVD LTYRRCKQGH CTRILNVTEH PGDVLEIRVW KKGFKAKPGQ
FILVQCPAIS SFEWHPFTVS MCPTSQCESF TIHIHAVGDW SGRLQQYLTG SEGWKYVLPP
LASSKEDLDK RLVIEGPYGS PSGDILKYRV NVLIAGGIGV TPFTAFLHHL YSNEKLHLQN
IERIYFIWMC KDLRSFKWFT QLLCRLYQKL WSLNRPDLLC IRLHVTAPVP GSQLKMFVKQ
YPLLEKRLYI GRRPDWPLTL MEICSSHKGT DIGVFCCGPK GLATNVEEEC SRIWHKNANL
FCHHESF
//
