ID W5JE68_ANODA Unreviewed; 321 AA.
AC W5JE68;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=sphingolipid 4-desaturase {ECO:0000256|ARBA:ARBA00012021};
DE EC=1.14.19.17 {ECO:0000256|ARBA:ARBA00012021};
GN ORFNames=AND_005653 {ECO:0000313|EMBL:ETN62652.1};
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:ETN62652.1};
RN [1] {ECO:0000313|EMBL:ETN62652.1, 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:ETN62652.1}
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:ETN62652.1}
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:ADAC005653-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000256|ARBA:ARBA00006146,
CC ECO:0000256|PIRNR:PIRNR017228}.
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DR EMBL; ADMH02001408; ETN62652.1; -; Genomic_DNA.
DR AlphaFoldDB; W5JE68; -.
DR STRING; 43151.W5JE68; -.
DR EnsemblMetazoa; ADAC005653-RA; ADAC005653-PA; ADAC005653.
DR VEuPathDB; VectorBase:ADAC005653; -.
DR VEuPathDB; VectorBase:ADAR2_001063; -.
DR eggNOG; KOG2987; Eukaryota.
DR HOGENOM; CLU_032156_0_0_1; -.
DR OMA; FEWVYND; -.
DR OrthoDB; 5485164at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
DR CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR InterPro; IPR011388; DES1/DES2.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
DR PANTHER; PTHR12879; SPHINGOLIPID DELTA 4 DESATURASE/C-4 HYDROXYLASE PROTEIN DES2; 1.
DR PANTHER; PTHR12879:SF8; SPHINGOLIPID DELTA(4)-DESATURASE DES1; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR Pfam; PF08557; Lipid_DES; 1.
DR PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1.
DR SMART; SM01269; Lipid_DES; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR017228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR017228};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR017228};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 43..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..43
FT /note="Sphingolipid delta4-desaturase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01269"
SQ SEQUENCE 321 AA; 37411 MW; 4E604ADC0ACC6A8C CRC64;
MGQHVSRTDF EWTYTEEPHA SRRKLILEKY PQIKKLFGYD PQFKWVASAM VLIQFAMLFV
MKDRSWKFIF LMAYCFGGVI NHSLMLACHE IAHNLAFGHA RPMANRLFGF FCNLPIGLPM
SVSFKKYHLE HHRYQGDEVI DTDLPTYVEA KLFCTTLGKF FWVCLQPLFY IFRPLIVNPK
PPQKLELVNG VIQLAFNTVV VYYFGWKVMV YLIVGSLLAM GLHPVAGHFI SEHYMFAKGF
ETYSYYGPLN WITFNVGYHN EHHDFPAVPG RLLPEVKRIA PEFYDDIPQH TSWTRVLYDF
ITDPAVGPYA RIKRKARGLD S
//
