ID A0A2K6A6Z4_MANLE Unreviewed; 295 AA.
AC A0A2K6A6Z4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ECO:0000313|Ensembl:ENSMLEP00000035835.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000035835.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000035835.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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|ARBA:ARBA00004477, ECO:0000256|HAMAP-Rule:MF_03202};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
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}.
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DR AlphaFoldDB; A0A2K6A6Z4; -.
DR STRING; 9568.ENSMLEP00000035835; -.
DR Ensembl; ENSMLET00000059434.1; ENSMLEP00000035835.1; ENSMLEG00000042047.1.
DR GeneTree; ENSGT01050000244838; -.
DR OMA; LQCQNLN; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000233140; Unplaced.
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:UP000233140};
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 33..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 146..163
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 169..191
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 229..253
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT MOTIF 292..295
FT /note="Di-lysine motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202"
SQ SEQUENCE 295 AA; 34421 MW; 7E587D3AB377027E CRC64;
EHLKAFDDEI NAFLDNMFGP RDSRVRGWFM LDSYLPTFFL TVIYLLSIWL GNKYMKNRPA
LSLRGILTLY NLGITLLSAY MLAELILSTW EGGYNLQCQD LTSAGEADIR VAKVLWWYYF
SKSVEFLDTI FFVLRKKTSQ ITFLHVYHHA SMFNIWWCVL NWIPCGQSFF GPTLNSFIHI
LMYSYYGLSV FPSMHKYLWW KKYLTQAQLV QFVLTITHTM SAVVKPCGFP FGCLIFQSSY
MLTLVILFLN FYVQTYRKKP MKKDMQEPPA GKEVKNGFSK AYFSAANGVM NKKAQ
//
