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Database: UniProt
Entry: A0A401T416_CHIPU
LinkDB: A0A401T416_CHIPU
Original site: A0A401T416_CHIPU 
ID   A0A401T416_CHIPU        Unreviewed;       718 AA.
AC   A0A401T416;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=NADPH oxidase 5 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=chiPu_0015851 {ECO:0000313|EMBL:GCC37347.1};
OS   Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC   Chiloscyllium.
OX   NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC37347.1, ECO:0000313|Proteomes:UP000287033};
RN   [1] {ECO:0000313|EMBL:GCC37347.1, ECO:0000313|Proteomes:UP000287033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCC37347.1}.
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DR   EMBL; BEZZ01000983; GCC37347.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401T416; -.
DR   STRING; 137246.A0A401T416; -.
DR   OMA; QWTTRLY; -.
DR   Proteomes; UP000287033; Unassembled WGS sequence.
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; PF13405; EF-hand_6; 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:UP000287033};
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..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        348..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        535..558
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          36..71
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          72..107
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          116..151
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          392..528
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   718 AA;  82848 MW;  FE6FECD26430C7C7 CRC64;
     MSADDDAKWL EWVTKQFENI AGEDKEINLE EFKTALKSFF AERFFTLFDS DGSGSISLDE
     LLKALNLLTH GSETDKLRFL FQVYDVDGSG SIDPDELRIV LKSCLRESAI SLPEEKLDDL
     TMALFESADK DNSGAITFEE LKEELENFPE VMENLTISAA NWLKPPATEK FTRQTPRYLT
     PAYWHNNSRK LLFMCCYILV NIFLFTFAAL KHVDAGGWVM LAKGCGQCLN FNCTFIGVLM
     LRRCLTWLRA TWVVRVLPLD QHVLLHQLVG FAIFGLSVVH AIAHLINFVN LTFSGGTYQL
     WEYLFTTRPG IGWIYGTASI TGVILLLLII LMLICSSTFV RRSGHFEVFY WTHLSYIWVW
     SLLVLHGSNF WKWFVVSGFL FLMEKIVGIT VSRIGGTQVV EVNLLPSKVT HLVIKRSPFF
     HYKPGDYVYV NIPAIAKYEW HPFTISSAPE QQDTIWLHIR SLGQWTNQLY EYFRQPELLG
     NEPKRLTRNL RNKKHQKSAQ VSTKLSDNHR YCNIKCYIDG PYGTPTRTIF TSEHAVLIGA
     GIGITPFASI LQSIMYRYRM RKQNCPNCSY SWCENVKDNE MSLRKVDFIW INRDQKSFEW
     FVSLLTKLEM DQADEEPQGR FLEMHMYMTS ALSKNDMKAL GLQMALDLLA KKENRDSITG
     LRTRTQPGRP DWAKVFQKIA EERKGKVHVF FCGSPVLAKT IKAQCEHFGF KFYKENFQ
//
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