ID A0A2U3X9B5_LEPWE Unreviewed; 281 AA.
AC A0A2U3X9B5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Elongation of very long chain fatty acids protein 7 {ECO:0000256|HAMAP-Rule:MF_03207};
DE EC=2.3.1.199 {ECO:0000256|HAMAP-Rule:MF_03207};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL7 {ECO:0000256|HAMAP-Rule:MF_03207};
DE AltName: Full=ELOVL fatty acid elongase 7 {ECO:0000256|HAMAP-Rule:MF_03207};
DE Short=ELOVL FA elongase 7 {ECO:0000256|HAMAP-Rule:MF_03207};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 7 {ECO:0000256|HAMAP-Rule:MF_03207};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 7 {ECO:0000256|HAMAP-Rule:MF_03207};
GN Name=ELOVL7 {ECO:0000256|HAMAP-Rule:MF_03207,
GN ECO:0000313|RefSeq:XP_006728036.1, ECO:0000313|RefSeq:XP_030891720.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006728036.1};
RN [1] {ECO:0000313|RefSeq:XP_006728036.1, ECO:0000313|RefSeq:XP_030891720.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006728036.1,
RC ECO:0000313|RefSeq:XP_030891720.1};
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. Condensing enzyme with higher activity toward C18
CC acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also
CC active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly
CC toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or
CC C26:0-CoAs. May participate to the production of saturated and
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_03207}.
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_03207,
CC ECO:0000256|RuleBase:RU361115};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_03207}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03207}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03207}. 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_03207}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL7 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03207}.
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DR RefSeq; XP_006728036.1; XM_006727973.2.
DR RefSeq; XP_030891720.1; XM_031035860.1.
DR STRING; 9713.A0A2U3X9B5; -.
DR GeneID; 102749705; -.
DR KEGG; lww:102749705; -.
DR CTD; 79993; -.
DR OrthoDB; 168669at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000245341; 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: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_03207; VLCF_elongase_7; 1.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033670; ELOVL7.
DR PANTHER; PTHR11157:SF118; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 7; 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_03207};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_03207};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_03207};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03207,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03207,
KW ECO:0000256|RuleBase:RU361115};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03207};
KW Reference proteome {ECO:0000313|Proteomes:UP000245341};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03207};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03207};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03207}.
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03207,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 69..87
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03207,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 118..136
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03207,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 143..162
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03207,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03207,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 206..227
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03207,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 233..258
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03207,
FT ECO:0000256|RuleBase:RU361115"
FT MOTIF 277..281
FT /note="Di-lysine motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03207"
SQ SEQUENCE 281 AA; 33419 MW; ADFF2FD84CE29A03 CRC64;
MVFSDLTSRT VRLYDNWIKD ADPRVEDWFL MSSPLPQTII LGLYVYFVTS LGPKLMENRK
PFELKKVMIT YNFSIVLFSV YMCYEFVMSG WGTGYSFRCE IVDYSRSPSA LRMARTCWLY
YFSKFIELLD TIFFVLRKKN SQVTFLHVFH HTIMPWTWWF GVKFAAGGLG TFHALLNTAV
HVVMYSYYGL SAMGPAFQKY LWWKKYLTLL QLAQFIIVTI HIGQFFFMED CKYQFPVFLY
IIMSYGCIFL LLFLHFWYRA YTKGQRLPKT VKNGICKNKD H
//
