ID A0A0L8G132_OCTBM Unreviewed; 323 AA.
AC A0A0L8G132;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=OCBIM_22002327mg {ECO:0000313|EMBL:KOF70726.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF70726.1};
RN [1] {ECO:0000313|EMBL:KOF70726.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF70726.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF70726.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) 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}.
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DR EMBL; KQ424629; KOF70726.1; -; Genomic_DNA.
DR RefSeq; XP_014785048.1; XM_014929562.1.
DR AlphaFoldDB; A0A0L8G132; -.
DR STRING; 37653.A0A0L8G132; -.
DR EnsemblMetazoa; Ocbimv22002327m; Ocbimv22002327m.p; Ocbimv22002327m.g.
DR EnsemblMetazoa; XM_014929562.1; XP_014785048.1; LOC106879848.
DR GeneID; 106879848; -.
DR KEGG; obi:106879848; -.
DR OMA; PISWVPI; -.
DR OrthoDB; 168669at2759; -.
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:SF171; ELONGATION OF FATTY ACIDS PROTEIN; 1.
DR PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01151; ELO; 1.
DR PROSITE; PS01188; 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 64..80
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 178..195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 201..223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 267..285
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
SQ SEQUENCE 323 AA; 37885 MW; A7DAA08DC884302D CRC64;
MVFGGAENKC EASYKEQYCD TDNKNSLDKM ADVVQALLQK IDYTSDTTAD PRTKDWFFLE
SSPLKVWILT AMYILFVIYG PKYMKNRKPF DIRIFMVLYN LAMVVLSIYM FVEIILSTQA
LGYTVICAPY TKSNAQNPKE MRLARVLWWY YFSKAIELMD TVLMILRKKN DQVTFLHVFH
HATMLNIWWW VMMFIPGGQT WFGACLNCFI HVVMYTYYGL SAIPSLKKRL WWKKYITKMQ
LIQFCITFVH SANSIRVNCE FPSWGKYLLT CYMILMIILF SNFYIQAYIK GRRNPNVDTA
NNYAKKKSSQ NGSTINGTVK KAQ
//
