ID A0A2Y9KF17_ENHLU Unreviewed; 720 AA.
AC A0A2Y9KF17;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=LOW QUALITY PROTEIN: NADPH oxidase 5 {ECO:0000313|RefSeq:XP_022368025.1};
GN Name=LOC111153339 {ECO:0000313|RefSeq:XP_022368025.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022368025.1};
RN [1] {ECO:0000313|RefSeq:XP_022368025.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022368025.1};
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_022368025.1; XM_022512317.1.
DR STRING; 391180.A0A2Y9KF17; -.
DR KEGG; elk:111153339; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 2.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 1.10.238.10; EF-hand; 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; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR PANTHER; PTHR11972:SF58; NADPH OXIDASE 5; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00450; RECOVERIN.
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; 3.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 191..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 376..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 538..559
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..74
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 75..110
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 119..154
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 395..531
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 720 AA; 82768 MW; 11A859C151B60668 CRC64;
MSTKEDTKWL QWVTHQFETI VGEDREIDLQ EFKAALNVKE PFFAERFFNL FDSDGSGTIT
LQELLEALTL LIHGNPMDKL KFLFQVYDVD GSGSIDVDEL RTVLQSCMRE SAISLPDEKL
DQLTLALFES ADKNCNGAIT FDELRDELQR FPGVMENLTI SAAHWLTPPA AQQRRRRPRL
LTSAYWHNHC SHLLCLTAYA VLHVLLFALA ASAHRARGPS VMVAKGCGQC LNFDCSFIAV
LMLRRCLTWL RATWLAQVLP LDWNXQFHQL MGYVVVVLSL VHTVAHVVNF VLQAQSKDSP
FRFWELLLTT RPGIGWVYGS ASPTGVALLL LLVLMFACSS SCIRRSGHFE VFYWTHLSYL
PMWILLILHG PNFWKWLLVP GILFFLEKII GLAVSRMGAL CIVEVNLLPS KVTHLLIERP
PLFHYRPGDY LYLNVPSIAR YEWHPFTISS APEQKDTIWL HVRSEGHWTN RLYESFKMLC
PMDCGSGQLS RSLRRRRSQR EPQVSEMSSE NHLLCNIKCY ISGPYGTPTR RIFVSEHAVL
IGAGIGITPF ASILQSIMYR HQKRKHICPS CQHFWMDSIQ DEDMKLRKED FIWINRDQQS
FEWFVSLLTK LEMDQAEMTQ EDPFLELHMY MTSALGKNDM KAIGLQMALD LLAKKEKKDS
ITGLQTRTQP GRPDWNKVFQ KVVAEKKGKM QVFFCGSPAL AKVLKGHCEQ FSFKFFQENF
//
