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Database: UniProt
Entry: B7Q893_IXOSC
LinkDB: B7Q893_IXOSC
Original site: B7Q893_IXOSC 
ID   B7Q893_IXOSC            Unreviewed;       161 AA.
AC   B7Q893;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
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=IscW_ISCW011553 {ECO:0000313|EMBL:EEC15065.1};
OS   Ixodes scapularis (Black-legged tick) (Deer tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=6945;
RN   [1] {ECO:0000313|EMBL:EEC15065.1, ECO:0000313|Proteomes:UP000001555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC   {ECO:0000313|EMBL:EEC15065.1};
RG   Ixodes scapularis Genome Project Consortium;
RA   Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA   Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA   Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA   Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT   "Annotation of Ixodes scapularis.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ISCW011553-PA}
RP   IDENTIFICATION.
RC   STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW011553-PA};
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   EMBL; ABJB010787951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS881792; EEC15065.1; -; Genomic_DNA.
DR   RefSeq; XP_002412322.1; XM_002412277.1.
DR   AlphaFoldDB; B7Q893; -.
DR   PaxDb; 6945-B7Q893; -.
DR   EnsemblMetazoa; ISCW011553-RA; ISCW011553-PA; ISCW011553.
DR   KEGG; isc:IscW_ISCW011553; -.
DR   VEuPathDB; VectorBase:ISCI011553; -.
DR   VEuPathDB; VectorBase:ISCP_011468; -.
DR   VEuPathDB; VectorBase:ISCW011553; -.
DR   HOGENOM; CLU_048483_5_0_1; -.
DR   InParanoid; B7Q893; -.
DR   OMA; TIMIRWG; -.
DR   Proteomes; UP000001555; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009922; F:fatty acid elongase activity; IBA:GO_Central.
DR   GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IBA:GO_Central.
DR   GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IBA:GO_Central.
DR   GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
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}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361115};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   161 AA;  18869 MW;  DFD1B77D2D22367B CRC64;
     MALAVPQLIL DLVDRYKYVT SLRDPRTVDW GWTENSKFML PLAFGYLYAV RFGGPRWMEN
     RKPYKLKSAI MVYNLFQVIA NAYLFVQYTR HSYLGGDYNA FCQGVSYSRD NNTMTILRLV
     WWSLFVRIAD FLDTFFFVAT KKVSHITALH GARNERLTHA D
//
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