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Database: UniProt
Entry: F6VAT4_CIOIN
LinkDB: F6VAT4_CIOIN
Original site: F6VAT4_CIOIN 
ID   F6VAT4_CIOIN            Unreviewed;       580 AA.
AC   F6VAT4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000008272.3, ECO:0000313|Proteomes:UP000008144};
RN   [1] {ECO:0000313|Proteomes:UP000008144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12481130; DOI=10.1126/science.1080049;
RA   Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA   Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA   Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA   Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA   Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA   Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA   Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA   Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA   Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA   Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA   Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA   Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA   Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA   Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA   Satoh N., Rokhsar D.S.;
RT   "The draft genome of Ciona intestinalis: insights into chordate and
RT   vertebrate origins.";
RL   Science 298:2157-2167(2002).
RN   [2] {ECO:0000313|Ensembl:ENSCINP00000008272.3}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; EAAA01002282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F6VAT4; -.
DR   STRING; 7719.ENSCINP00000008272; -.
DR   Ensembl; ENSCINT00000008272.3; ENSCINP00000008272.3; ENSCING00000004013.3.
DR   GeneTree; ENSGT00940000167196; -.
DR   HOGENOM; CLU_005646_3_1_1; -.
DR   InParanoid; F6VAT4; -.
DR   OMA; FTFAKEH; -.
DR   TreeFam; TF105354; -.
DR   Proteomes; UP000008144; Chromosome 6.
DR   GO; GO:0043020; C:NADPH oxidase complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IBA:GO_Central.
DR   GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
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:SF69; METALLOREDUCTASE AIM14-RELATED; 1.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 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   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:UP000008144};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        103..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        211..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          300..409
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   580 AA;  66817 MW;  87DA70DFB65A9020 CRC64;
     MNARLNGFLV NEFPKYIVFL LWLGLNGFLF GYYYNFYNTK KTFFYTRVLL GPALALARPA
     ACLNLNCLLV LLPVCRNLLS LFRKACMCCP RRIRRVLDKN IKFHRMCAYM IVLMTLIHYF
     AHCFNVDFFT SAYQSKILAT DTPAIIQQKK LIAKLIQIGN NGNETYLNPI RKSVFSVGAV
     FLLTGGWTGV IITLSLFFMV TSSLEFIRRS YFEVFWFTHH LFIVFYGFLV VHGISMQVRG
     QTPQSLTVHD PIRCSTIDPA TWSQNNCPTP VFAGSPPMTW KWVIAPMVLY VIERIIRLVR
     FNQQVEVLKV IKHPSRVLEI QMRKNGFFAE VGQYVFIMCP QLSQLEWHPF TLTSAPEEDY
     FSIHVRIVGD WTTGLSKVLG ADEAGNEVQP SWKMPRLAID GPFGTASEDV FNYPVAICVG
     SGIGVTPFAS LLKSVWYKNL NPEHEMVLKK VYFFWICPET HAFEWFGDLL KYLERQLTEI
     GRQDLIEYHI YLTRGWDHKQ AKAIYAHEED THDVITGLEQ KTNYGRPNWD EIFSKTARDY
     PNTHIGVFFC GVAALSAKLH KMSNKHSGGG VYFHYNKENF
//
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