ID A0A3M0KTY8_HIRRU Unreviewed; 316 AA.
AC A0A3M0KTY8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Elongation of very long chain fatty acids protein 2 {ECO:0000256|HAMAP-Rule:MF_03202};
DE EC=2.3.1.199 {ECO:0000256|HAMAP-Rule:MF_03202};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL2 {ECO:0000256|HAMAP-Rule:MF_03202};
DE AltName: Full=ELOVL fatty acid elongase 2 {ECO:0000256|HAMAP-Rule:MF_03202};
DE Short=ELOVL FA elongase 2 {ECO:0000256|HAMAP-Rule:MF_03202};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 2 {ECO:0000256|HAMAP-Rule:MF_03202};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 2 {ECO:0000256|HAMAP-Rule:MF_03202};
GN Name=ELOVL2 {ECO:0000256|HAMAP-Rule:MF_03202};
GN ORFNames=DUI87_08355 {ECO:0000313|EMBL:RMC16141.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC16141.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMC16141.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMC16141.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMC16141.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first and rate-limiting reaction of the four
CC reactions that constitute the long-chain fatty acids elongation cycle.
CC This endoplasmic reticulum-bound enzymatic process allows the addition
CC of 2 carbons to the chain of long- and very long-chain fatty acids
CC (VLCFAs) per cycle. Acts specifically toward polyunsaturated acyl-CoA
CC with the higher activity toward C20:4(n-6) acyl-CoA. Condensing enzyme
CC that catalyzes the synthesis of polyunsaturated very long chain fatty
CC acid (C20- and C22-PUFA). May participate to the production of
CC polyunsaturated VLCFAs of different chain lengths that are involved in
CC multiple biological processes as precursors of membrane lipids and
CC lipid mediators. {ECO:0000256|HAMAP-Rule:MF_03202}.
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|HAMAP-Rule:MF_03202,
CC ECO:0000256|RuleBase:RU361115};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03202}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03202}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000256|HAMAP-Rule:MF_03202}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03202}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMC16141.1}.
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DR EMBL; QRBI01000104; RMC16141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0KTY8; -.
DR STRING; 333673.A0A3M0KTY8; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009922; F:fatty acid elongase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IEA:UniProtKB-UniRule.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IEA:InterPro.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03202; VLCF_elongase_2; 1.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033680; ELOVL2.
DR PANTHER; PTHR11157:SF16; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 2; 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 Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03202};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_03202};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_03202};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03202,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03202,
KW ECO:0000256|RuleBase:RU361115};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03202};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03202};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03202};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03202}.
FT TRANSMEM 54..75
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 87..110
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 136..154
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 166..183
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 189..211
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 249..273
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT MOTIF 313..316
FT /note="Di-lysine motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202"
SQ SEQUENCE 316 AA; 36975 MW; 1B3CC384C2EC7C13 CRC64;
MDLIASRLRR QKKGQLSLSR ETLKAFDREV NAFVDYMFGP RDARVRGWFL LDSYLPTFFL
TGAYLLCIWL GNKFMKNRPP FSLRPHLIVY NLGITLLSFY MLIELILATW EGGYNLQCQN
LHSAGEADIR VAKVLWWYYF SKVIEFMDTI FFVLRKKSSQ ITFLHVYHHA TMFNIWWCVL
NWIPCGQSFF GPTLNSFIHV LMYSYYGLSV IPSMRKYLWW KKYLTQAQLI QFLLTIVHTL
SAAVKPCGFP FGCLMFQSSY MATLVILFIN FYIKTYRKAP SRTAVKETPA TTEIKNGFHK
DYFAAANGLQ NNKKAQ
//
