ID W5JLE5_ANODA Unreviewed; 455 AA.
AC W5JLE5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Elongation of very long chain fatty acids protein {ECO:0000256|RuleBase:RU361115};
DE EC=2.3.1.199 {ECO:0000256|RuleBase:RU361115};
DE AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase {ECO:0000256|RuleBase:RU361115};
GN ORFNames=AND_003322 {ECO:0000313|EMBL:ETN64921.1};
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:ETN64921.1};
RN [1] {ECO:0000313|EMBL:ETN64921.1, 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:ETN64921.1}
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:ETN64921.1}
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:ADAC003322-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC EC=2.3.1.199; Evidence={ECO:0000256|RuleBase:RU361115};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000256|RuleBase:RU361115}.
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DR EMBL; ADMH02000834; ETN64921.1; -; Genomic_DNA.
DR AlphaFoldDB; W5JLE5; -.
DR STRING; 43151.W5JLE5; -.
DR EnsemblMetazoa; ADAC003322-RA; ADAC003322-PA; ADAC003322.
DR VEuPathDB; VectorBase:ADAC003322; -.
DR VEuPathDB; VectorBase:ADAR2_007743; -.
DR eggNOG; KOG3071; Eukaryota.
DR HOGENOM; CLU_048483_7_0_1; -.
DR OrthoDB; 3425948at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009922; F:fatty acid elongase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR002076; ELO_fam.
DR PANTHER; PTHR11157:SF22; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN; 1.
DR PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01151; ELO; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU361115};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361115};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361115};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361115};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361115};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361115};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361115}.
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 98..114
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 202..220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 240..259
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 265..286
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT REGION 328..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 51782 MW; 1F413F4AC1776D88 CRC64;
METPMVAFEL TAGTTDMIKQ EVLLTMDDYF RGSSISSLIA HWWRSMVDLI ADPRAKQLPF
MDNPLPTLGM IMIYLFWVLL IGPMYMRDRK PMDLRRGIIF YNLFQVLLSG YMFYEHLMAG
WLRGYSLTCQ TVDYSDSPQS RRMFNLCYVY YLSKLSEFAD TVFFVLRKKQ SQITDLHVYH
HSLTPIEAWI LTKFIAGGNA TLPNVINNFV HVLMYFYYML SAMGPRYQKY LWWKKYMTEV
QIIQFIICIA HCINALVTGC PFPRFISTLL LINASIFLAL FMNFYIESYK RKPRGTVATV
AKSITVETAP TVTPAVSGVQ EVELVAEERD VKDGTSQDST TTTTATPVED DINNNRTVMM
AVDGKREPQP QEKVKRDTPV DGEHQQPLQQ HNEHDESSEL EITKLESTLE STTTPGSLRQ
RIVSVKGGEG GGLGEMEVEM RTSASTVLST IATAP
//
