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Database: UniProt
Entry: B7QN71_IXOSC
LinkDB: B7QN71_IXOSC
Original site: B7QN71_IXOSC 
ID   B7QN71_IXOSC            Unreviewed;       293 AA.
AC   B7QN71;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
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_ISCW015228 {ECO:0000313|EMBL:EEC20293.1};
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:EEC20293.1, 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:EEC20293.1};
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:ISCW015228-PA}
RP   IDENTIFICATION.
RC   STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW015228-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; ABJB010280018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS976708; EEC20293.1; -; Genomic_DNA.
DR   RefSeq; XP_002400751.1; XM_002400707.1.
DR   AlphaFoldDB; B7QN71; -.
DR   PaxDb; 6945-B7QN71; -.
DR   EnsemblMetazoa; ISCW015228-RA; ISCW015228-PA; ISCW015228.
DR   KEGG; isc:IscW_ISCW015228; -.
DR   VEuPathDB; VectorBase:ISCI015228; -.
DR   VEuPathDB; VectorBase:ISCP_016480; -.
DR   VEuPathDB; VectorBase:ISCW015228; -.
DR   HOGENOM; CLU_048483_0_1_1; -.
DR   InParanoid; B7QN71; -.
DR   OMA; MIMWINT; -.
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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361115};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001555};
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        33..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        62..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        142..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        169..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        205..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        233..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361115"
FT   REGION          270..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   293 AA;  33760 MW;  8B92A80333EF79EB CRC64;
     METLRATTPD VLTTILSLRD PRVKNWETMD NPMYMFVLLT SYLYVAKSLG PRYMKDKDPY
     ELKGVIMVYN LFQVLANVYF LSQIFYHSFY AAGYSLFCQG LTYSTDPHAI SLLNALYWYL
     WVRVADFLDT IFFIMKKKFT HITVLHVVHH TIVVFSGWMF LQFGGDGQVV FGVCLNSFVH
     IIMYTYYFLA CLGPSVQKYL WWKRYLTRVQ IGQFIVIIAH ALIPIFVDCG YPRVLICVAI
     PQVVLILGLF VNFYVQSYIK RRNAGADKTT KMSSAQDGAS MNGAVKGMDK KKS
//
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