ID A0A182YHI3_ANOST Unreviewed; 507 AA.
AC A0A182YHI3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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};
OS Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=30069 {ECO:0000313|EnsemblMetazoa:ASTEI07919-PA, ECO:0000313|Proteomes:UP000076408};
RN [1] {ECO:0000313|Proteomes:UP000076408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Indian {ECO:0000313|Proteomes:UP000076408};
RX PubMed=25244985; DOI=10.1186/preaccept-1262842421127991;
RA Jiang X., Peery A., Hall A.B., Sharma A., Chen X.G., Waterhouse R.M.,
RA Komissarov A., Riehle M.M., Shouche Y., Sharakhova M.V., Lawson D.,
RA Pakpour N., Arensburger P., Davidson V.L., Eiglmeier K., Emrich S.,
RA George P., Kennedy R.C., Mane S.P., Maslen G., Oringanje C., Qi Y.,
RA Settlage R., Tojo M., Tubio J.M., Unger M.F., Wang B., Vernick K.D.,
RA Ribeiro J.M., James A.A., Michel K., Riehle M.A., Luckhart S.,
RA Sharakhov I.V., Tu Z.;
RT "Genome analysis of a major urban malaria vector mosquito, Anopheles
RT stephensi.";
RL Genome Biol. 15:459-459(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASTEI07919-PA}
RP IDENTIFICATION.
RC STRAIN=Indian {ECO:0000313|EnsemblMetazoa:ASTEI07919-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361115}.
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DR AlphaFoldDB; A0A182YHI3; -.
DR STRING; 30069.A0A182YHI3; -.
DR EnsemblMetazoa; ASTEI07919-RA; ASTEI07919-PA; ASTEI07919.
DR VEuPathDB; VectorBase:ASTE016477; -.
DR VEuPathDB; VectorBase:ASTEI07919; -.
DR VEuPathDB; VectorBase:ASTEI20_045660; -.
DR OMA; VIVHIIM; -.
DR Proteomes; UP000076408; 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; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR PANTHER; PTHR11157:SF116; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN-RELATED; 1.
DR PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01151; ELO; 2.
DR PROSITE; PS01188; ELO; 2.
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:UP000076408};
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 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 72..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 116..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 149..166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 236..257
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 269..291
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 303..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 353..372
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 384..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 408..429
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 441..462
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 474..493
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
SQ SEQUENCE 507 AA; 60039 MW; 63762C2E5C1BD109 CRC64;
MTLVWERMYD VYHEYIVERR DMRSVNLPLA GTPWPLMLVL GTYLFVVLHA GPKFMAQRKA
YDLRKVIRVY NIAQVLINSV LFLWIVIKMF IVYRDYNFSC QVCNYSTDYR GLEEMYLSYS
YFLLKVLDLA DTVFFVLRKK QSHVSFLHVY HHTVMVVGSY FGVLYVPGGH AIMLGIWNTL
VHAVMYLYYF LSSYGSQYSG WWKQHLTRMQ LLQFIHLAFH FGIPLFFNRE CKFPRFWMGV
GFLQALVILA LFMDFYIKSV LDLPLLRSFW TVPLITGTYL YFVLNLGPKL MANRKPFEMR
NLLIVYNLFQ VAANVATFVM GLNYLRSYPS YSYVCQPLQQ DTSARSMLEL RLGYAYFLLK
ILDLADTVFF VLKKKQSHVS FLHVYHHTIM AISVSLFMRY LAGGHCFMLG MLNTLVHAVM
YFYFFLTIYR PEETRGAAWK RYVTLLQMAQ FAYLVFHFFR PIVLGIDCGY PRAVMWFVGL
QNIFMLLMFG DFYRRSYLRK PKKGHEN
//
