ELVL1_AEDAE
ID ELVL1_AEDAE Reviewed; 358 AA.
AC Q1HRV8; Q0IEV4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Elongation of very long chain fatty acids protein AAEL008004;
DE EC=2.3.1.199;
DE AltName: Full=3-keto acyl-CoA synthase AAEL008004;
DE AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase AAEL008004;
GN ORFNames=AAEL008004;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Black-eyed Liverpool; TISSUE=Salivary gland;
RX PubMed=17204158; DOI=10.1186/1471-2164-8-6;
RA Ribeiro J.M.C., Arca B., Lombardo F., Calvo E., Phan V.M., Chandra P.K.,
RA Wikel S.K.;
RT "An annotated catalogue of salivary gland transcripts in the adult female
RT mosquito, Aedes aegypti.";
RL BMC Genomics 8:6-6(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
CC -!- FUNCTION: Could be implicated in synthesis of very long chain fatty
CC acids. {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT40247.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ439986; ABF18019.1; -; mRNA.
DR EMBL; CH477478; EAT40247.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001658783.1; XM_001658733.1.
DR AlphaFoldDB; Q1HRV8; -.
DR SMR; Q1HRV8; -.
DR STRING; 7159.AAEL008004-PA; -.
DR VEuPathDB; VectorBase:AAEL024147; -.
DR eggNOG; KOG3071; Eukaryota.
DR HOGENOM; CLU_048483_4_3_1; -.
DR InParanoid; Q1HRV8; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0009922; F:fatty acid elongase activity; IEA:InterPro.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR002076; ELO_fam.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR Pfam; PF01151; ELO; 1.
PE 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..358
FT /note="Elongation of very long chain fatty acids protein
FT AAEL008004"
FT /id="PRO_0000314472"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 285..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 201
FT /note="W -> C (in Ref. 1; ABF18019)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="S -> G (in Ref. 1; ABF18019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 41392 MW; F21914B0AA5EBEEB CRC64;
MALIMKYIDS MHHYMDKYGD PRTKDWPLMS SPFPTLALCL GYVYLVKVLG PRLMENRKPF
QLRNTLILYN FVQVVFSAWL FYEIGISGWL TGHYNFRCQP VDYSNHPKTL RMVHACWWYY
FSKFTEFFDT FFFVMRKKTS QVSTLHVIHH GCMPMSVWFG VKFTPGGHST FFGLLNTFVH
IVMYTYYLFT AMGPQFQKYL WWKKYLTSLQ MVQFVAIMVH AFQLLFIDCN YPKAFVWWIG
MHAVMFLFLF NEFYQSTYKA TKRRRAAAAE ARRLAAEEAK LQNGSAVSSN GSAITANGHH
GKNGSVHHHS NGSATSNGTS LLSNGVGSNK AADYYVRGDL PAEIEITQRQ PSSRNQVQ
