ID A0A2K6G2F1_PROCO Unreviewed; 270 AA.
AC A0A2K6G2F1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Elongation of very long chain fatty acids protein 3 {ECO:0000256|HAMAP-Rule:MF_03203};
DE EC=2.3.1.199 {ECO:0000256|HAMAP-Rule:MF_03203};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL3 {ECO:0000256|HAMAP-Rule:MF_03203};
DE AltName: Full=ELOVL fatty acid elongase 3 {ECO:0000256|HAMAP-Rule:MF_03203};
DE Short=ELOVL FA elongase 3 {ECO:0000256|HAMAP-Rule:MF_03203};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 3 {ECO:0000256|HAMAP-Rule:MF_03203};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 3 {ECO:0000256|HAMAP-Rule:MF_03203};
GN Name=ELOVL3 {ECO:0000256|HAMAP-Rule:MF_03203,
GN ECO:0000313|Ensembl:ENSPCOP00000020407.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000020407.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000020407.1}
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. Condensing enzyme with higher activity toward C18
CC acyl-CoAs, especially C18:0 acyl-CoAs. May participate to the
CC production of saturated and monounsaturated VLCFAs of different chain
CC lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators. {ECO:0000256|HAMAP-
CC Rule:MF_03203}.
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_03203,
CC ECO:0000256|RuleBase:RU361115};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03203}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|HAMAP-Rule:MF_03203};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|HAMAP-Rule:MF_03203}. 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_03203}.
CC -!- PTM: N-Glycosylated. {ECO:0000256|HAMAP-Rule:MF_03203}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL3 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03203}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03203}.
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DR AlphaFoldDB; A0A2K6G2F1; -.
DR STRING; 379532.ENSPCOP00000020407; -.
DR Ensembl; ENSPCOT00000031061.1; ENSPCOP00000020407.1; ENSPCOG00000022173.1.
DR GeneTree; ENSGT01050000244965; -.
DR OMA; ILTYIWR; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000233160; 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:0034625; P:fatty acid elongation, monounsaturated fatty acid; 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:UniProtKB-UniRule.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03203; VLCF_elongase_3; 1.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033679; ELOVL3.
DR PANTHER; PTHR11157:SF68; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 3; 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_03203};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_03203};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_03203}; Glycoprotein {ECO:0000256|HAMAP-Rule:MF_03203};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03203,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03203,
KW ECO:0000256|RuleBase:RU361115};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03203};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03203};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03203};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03203}.
FT TRANSMEM 33..55
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03203,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 67..93
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03203,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03203,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 197..223
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03203,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 235..254
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03203,
FT ECO:0000256|RuleBase:RU361115"
FT MOTIF 266..270
FT /note="Di-lysine motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03203"
SQ SEQUENCE 270 AA; 31618 MW; DA88FEB844697201 CRC64;
VVTAMNISHE VEQLFQPYDF ERSQDMRPFL EEYWATCFPI VLIYLLLIIV GQNYMKARKG
FNLQRPLILW SFCLAIFSIL GAVRMWGFMG AVLLRGGLKQ TVCFVNFLDT STIKFWSCIF
LLSKIIELGD TAFIILRKRP LIFVHWYHHS TVLMYTSFGY KNKVPAGGWF MTMNFGVHAI
MYTYYTLKAA SVKPPKLLAM LITSLQILQM LLGAIIGLLT YIWRQEQGCY TTVEHFFWSF
ILYATYFILF AHFFRQTYIR PKVKAKTKSQ
//
