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Database: UniProt
Entry: A0A2K6F901_PROCO
LinkDB: A0A2K6F901_PROCO
Original site: A0A2K6F901_PROCO 
ID   A0A2K6F901_PROCO        Unreviewed;       507 AA.
AC   A0A2K6F901;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=NADPH oxidase 3 {ECO:0000313|Ensembl:ENSPCOP00000010455.1};
GN   Name=NOX3 {ECO:0000313|Ensembl:ENSPCOP00000010455.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000010455.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000010455.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K6F901; -.
DR   STRING; 379532.ENSPCOP00000010455; -.
DR   Ensembl; ENSPCOT00000021034.1; ENSPCOP00000010455.1; ENSPCOG00000016698.1.
DR   GeneTree; ENSGT00940000160501; -.
DR   OMA; DENQAIH; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0043020; C:NADPH oxidase complex; IEA:Ensembl.
DR   GO; GO:0020037; F:heme binding; IEA:Ensembl.
DR   GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IEA:Ensembl.
DR   GO; GO:0009590; P:detection of gravity; IEA:Ensembl.
DR   GO; GO:0048840; P:otolith development; IEA:Ensembl.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:UniProt.
DR   GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl.
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; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
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; PF08030; NAD_binding_6; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        51..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          224..334
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   507 AA;  58029 MW;  21F000E93ECCB4BA CRC64;
     MMGCWILHEG LTIILVLSWL GVNLYLFIDT FCWYEEEESF HYTRAILGST LAWARASALC
     LNFNCMLILL PISRNLISFV RGTSICCRGP WRRQLDKNLK FHKLVAYGIA VNATIHIVAH
     LFNLERYHLS QREEAEGLLA ALSKLGNTPN ETYLNPIRTF HTRIVRGQTP ESLSLHNVTF
     CRDRYAEWQP AAQCPVPQFS GKEPSAWKWV LGPVVLYACE RIIRFWRFQQ EVVITKVVSH
     PSGVLELHMK KRGFKMAPGQ YILVQCPAIS SLEWHPFTLT SAPQEDFFSV HVRAAGDWTR
     ALLKAFGADG QAPKEPWSLP RLAVDGPFGA TLTDVFHYPV SVCIAAGIGV TPFAALLKSI
     WYQCCDSQTQ LKLSKVYFYW ICRDASAFEW FADLLLSLET RMSEQGKTHF LSYHIFLTGW
     DENQAIHIAL HWDENTDVIT GLKQKTFYGR PHWNNEFKRI AYNHPGSSIG VFFCGPKALS
     KTLQRMCHLY SSADPRGVHF YYNKESF
//
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