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Database: UniProt
Entry: A0A2C9JPQ7_BIOGL
LinkDB: A0A2C9JPQ7_BIOGL
Original site: A0A2C9JPQ7_BIOGL 
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
//
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