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Database: UniProt
Entry: A0A0R3SJN5_HYMDI
LinkDB: A0A0R3SJN5_HYMDI
Original site: A0A0R3SJN5_HYMDI 
ID   A0A0R3SJN5_HYMDI        Unreviewed;       225 AA.
AC   A0A0R3SJN5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
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};
OS   Hymenolepis diminuta (Rat tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX   NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000515001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HDID_0000515001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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   AlphaFoldDB; A0A0R3SJN5; -.
DR   STRING; 6216.A0A0R3SJN5; -.
DR   WBParaSite; HDID_0000515001-mRNA-1; HDID_0000515001-mRNA-1; HDID_0000515001.
DR   Proteomes; UP000046397; Unplaced.
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; IPR002076; ELO_fam.
DR   PANTHER; PTHR11157:SF126; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 4; 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|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU361115};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   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        27..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        105..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        130..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        161..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        192..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
SQ   SEQUENCE   225 AA;  26605 MW;  6305F6200CB2BD4D CRC64;
     LYLFIVLWFG PWLMTFRKCA FDLRNFMIIY NTLLVLLNAY IAQILIKSAW ALNYDILCQR
     ISYSNDPLEI QIASGLWCYY VSKLIEFTDT IIFVLRKKKS QMTFLHVYHH ITMPFWCWIA
     VRWYAGGSTF FIPAMNSVIH CIMYTYYGAS ALGIRFVQKR WLTALQLVQF FTGIIFGISL
     LYNSCIFIPR PLIYLGLVYG ITIILLFINF YREVYTNKVQ KDRTA
//
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