ID A0A2C9JPQ7_BIOGL Unreviewed; 290 AA.
AC A0A2C9JPQ7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 Name=106062719 {ECO:0000313|EnsemblMetazoa:BGLB005952-PB};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB005952-PB, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB005952-PB}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB005952-PB};
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}.
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DR RefSeq; XP_013076488.1; XM_013221034.1.
DR AlphaFoldDB; A0A2C9JPQ7; -.
DR STRING; 6526.A0A2C9JPQ7; -.
DR EnsemblMetazoa; BGLB005952-RB; BGLB005952-PB; BGLB005952.
DR GeneID; 106062719; -.
DR KEGG; bgt:106062719; -.
DR VEuPathDB; VectorBase:BGLB005952; -.
DR OrthoDB; 168669at2759; -.
DR Proteomes; UP000076420; 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:SF166; ELONGATION OF VERY LONG CHAIN 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 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 55..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 112..130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 142..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361115"
FT REGION 260..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 290 AA; 34437 MW; 43701F6FE6E35457 CRC64;
MVLYSNFSEF VTNRIDHRVS GWLLMSSPVP TLLIITAYLV FVFQGQKMMK QHQPWDLRSL
IVVYNFFLVI LSAFMVYEFM MSSWTVPGFS LACQRMDYSY DPNSIRLAGA CWWFYFSKLI
ELMDTVFFVL RKKNSQISFL HVYHHSTMPF LWWLGVRFVG GGEAYFSPTI NSMIHVLMYL
YYMLSAMGPS MQPYLWWKKY MTRLQLAQFW LVLCKTVCAI YINCGYPLEY QYFLVFYMMS
HIVLFSNFYF KTYQDKGKLS VEETPSDNNN RSKPIGLSPQ EINDSVRQRK
//