ID W5JLG6_ANODA Unreviewed; 432 AA.
AC W5JLG6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=NADP-retinol dehydrogenase {ECO:0000256|ARBA:ARBA00012852};
DE EC=1.1.1.300 {ECO:0000256|ARBA:ARBA00012852};
GN ORFNames=AND_004523 {ECO:0000313|EMBL:ETN63755.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN63755.1};
RN [1] {ECO:0000313|EMBL:ETN63755.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN63755.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN63755.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC004523-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) +
CC NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.300; Evidence={ECO:0000256|ARBA:ARBA00000975};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000256|ARBA:ARBA00004891}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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DR EMBL; ADMH02001200; ETN63755.1; -; Genomic_DNA.
DR AlphaFoldDB; W5JLG6; -.
DR STRING; 43151.W5JLG6; -.
DR EnsemblMetazoa; ADAC004523-RA; ADAC004523-PA; ADAC004523.
DR VEuPathDB; VectorBase:ADAC004523; -.
DR VEuPathDB; VectorBase:ADAR2_008303; -.
DR VEuPathDB; VectorBase:ADAR2_010671; -.
DR eggNOG; KOG1201; Eukaryota.
DR HOGENOM; CLU_010194_2_5_1; -.
DR OMA; PYRSMGA; -.
DR OrthoDB; 6845at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd05339; 17beta-HSDXI-like_SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR24322; PKSB; 1.
DR PANTHER; PTHR24322:SF736; RETINOL DEHYDROGENASE 10; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673}.
FT REGION 20..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 47258 MW; C92B6D9E3FFB3130 CRC64;
MNILEDDNID NAISVFRSDR QFIDNNSSGI PPRPTPARQP TTTESAAGVV DRSGQRHSPI
TSGLVARRWQ NAKLDILAPR RTGSRSRAAR DDSKKPTNGR GGGRSLGSRQ NLMLSAVDAE
GETSNNPAVI AYNAVLILFD VLVFLVKSVY ITVKAIVEMA MLPPARDVSG DIVLITGAGH
GMGKNLALQY AALGTTVVCV DVNEKTNSET VAAIKSAKGG KAFGFTCDVT NRQQVMDTCK
KIKEQVGVVS ILINNAGIMP THSLLQQTET EIRKTFDINV LAHFWFIQSL LPDMLKQNRG
HIVVLSSIAG MIGFKYLVPY CGTKFAVRGI MEALSEELRA DPTKPNIKFT TIYPYMVDTG
LCKRPYTRFP SLLKMVKPDD AAAAIIDAQR RGLTEASIPK YLLYLNTWFR NLPLRVGQEF
GDLLDTGLQS DL
//
