ID A0A3Q0CKZ4_MESAU Unreviewed; 296 AA.
AC A0A3Q0CKZ4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:0000313|RefSeq:XP_021080634.1};
GN Synonyms=ELOVL2 {ECO:0000256|HAMAP-Rule:MF_03202};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021080634.1};
RN [1] {ECO:0000313|RefSeq:XP_021080634.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26319212;
RA Ying B., Toth K., Spencer J.F., Aurora R., Wold W.S.;
RT "Transcriptome sequencing and development of an expression microarray
RT platform for liver infection in adenovirus type 5-infected Syrian golden
RT hamsters.";
RL Virology 485:305-312(2015).
RN [2] {ECO:0000313|RefSeq:XP_021080634.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28071753;
RA McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT "De novo assembly, annotation, and characterization of the whole brain
RT transcriptome of male and female Syrian hamsters.";
RL Sci. Rep. 7:40472-40472(2017).
RN [3] {ECO:0000313|RefSeq:XP_021080634.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 -!- SIMILARITY: Belongs to the ELO family. ELOVL2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03202}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03202}.
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DR RefSeq; XP_021080634.1; XM_021224975.1.
DR AlphaFoldDB; A0A3Q0CKZ4; -.
DR STRING; 10036.ENSMAUP00000013310; -.
DR OrthoDB; 168669at2759; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000189706; 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:UP000189706};
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 34..52
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 117..135
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 147..164
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 230..254
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03202,
FT ECO:0000256|RuleBase:RU361115"
SQ SEQUENCE 296 AA; 34540 MW; B975B05C72E8B580 CRC64;
MEHLKAFDNE VNAFLDNMFG PRDSRVRGWF LLDSYLPTFI LTVLYLLSIW LGNKYMKNRP
ALSLRGILTF YNLGITLLSA YMLVELILSS WEGGYNLQCQ NLDSAGEGDI RVAKVLWWYY
FSKLVEFLDT IFFVLRKKTS QITFLHVYHH ASMFNIWWCV LNWIPCGQSF FGPTLNSFIH
ILMYSYYGLS VFPSMHKYLW WKKYLTQAQL VQFVLTITHT LSAVVKPCGF PFGCLVFQSS
YMMTLVILFL NFYVQTYRRK PAKREAREQP AGKEVKNGLP KAHLMAANGV TNRKVQ
//
