ID Q7PZD2_ANOGA Unreviewed; 276 AA.
AC Q7PZD2;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 2.
DT 24-JAN-2024, entry version 96.
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};
DE Flags: Fragment;
GN ORFNames=AgaP_AGAP011848 {ECO:0000313|EMBL:EAA00095.2};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA00095.2};
RN [1] {ECO:0000313|EMBL:EAA00095.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EAA00095.2};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000313|EMBL:EAA00095.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA00095.2};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAA00095.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA00095.2};
RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT "The Anopheles gambiae genome: an update.";
RL Trends Parasitol. 20:49-52(2004).
RN [4] {ECO:0000313|EMBL:EAA00095.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA00095.2};
RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT "Update of the Anopheles gambiae PEST genome assembly.";
RL Genome Biol. 8:R5.1-R5.13(2007).
RN [5] {ECO:0000313|EMBL:EAA00095.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA00095.2};
RG VectorBase;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAA00095.2}.
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DR EMBL; AAAB01008986; EAA00095.2; -; Genomic_DNA.
DR RefSeq; XP_320671.2; XM_320671.2.
DR AlphaFoldDB; Q7PZD2; -.
DR STRING; 7165.Q7PZD2; -.
DR PaxDb; 7165-AGAP011848-PA; -.
DR GeneID; 1280804; -.
DR KEGG; aga:AgaP_AGAP011848; -.
DR VEuPathDB; VectorBase:AGAP011848; -.
DR eggNOG; KOG3071; Eukaryota.
DR HOGENOM; CLU_048483_0_0_1; -.
DR InParanoid; Q7PZD2; -.
DR OMA; SRFEMVV; -.
DR OrthoDB; 168669at2759; -.
DR PhylomeDB; Q7PZD2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009922; F:fatty acid elongase activity; IBA:GO_Central.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IBA:GO_Central.
DR GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IBA:GO_Central.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
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 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 48..66
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 78..94
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 212..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 245..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EAA00095.2"
FT NON_TER 276
FT /evidence="ECO:0000313|EMBL:EAA00095.2"
SQ SEQUENCE 276 AA; 32613 MW; BAA7F98A0A0B9DB6 CRC64;
IMQLAIDEYQ ADRNWTRLID RYWNLVEDLI GDPRAKQLPF MDNPLPTVGM VLTYLAWVLI
IGPTYMRDRK PMQLTNTLFY YNLGQVLLSA YMFYEHLMAG WARGYSLTCQ PVDYSDDQLS
RRMFNLCYIY YLSKLSEFAD TVFFVLRKKK SQISYLHLYH HSLTPIEAWI LTKFLAGGNA
TLPNIINNFV HTLMYLYYML SAMGPRYQKY LFWKQFLTEL QIAQFVICIG HAINALLTDC
AFPKFITFLL LCNASIFFVL FMNFYLENYR KQATAK
//
