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Database: UniProt
Entry: G3NVZ6_GASAC
LinkDB: G3NVZ6_GASAC
Original site: G3NVZ6_GASAC 
ID   G3NVZ6_GASAC            Unreviewed;       282 AA.
AC   G3NVZ6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
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};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000009515.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000009515.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000009515.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   -!- SIMILARITY: Belongs to the ELO family. ELOVL7 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03207}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03207}.
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DR   AlphaFoldDB; G3NVZ6; -.
DR   Ensembl; ENSGACT00000009535.1; ENSGACP00000009515.1; ENSGACG00000007167.1.
DR   GeneTree; ENSGT01050000244838; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000007167; Expressed in pharyngeal gill and 4 other cell types or tissues.
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:UP000007635};
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        26..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03207,
FT                   ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        68..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        148..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03207,
FT                   ECO:0000256|RuleBase:RU361115"
FT   TRANSMEM        172..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"
SQ   SEQUENCE   282 AA;  33374 MW;  13ADA742F8216A79 CRC64;
     MEFDYLKSSA TLIYNEFLQN ADRRTASWFL MSSPLPQTVI IAAYIYFVHS LGPRLMENRK
     ALDLRGVLIV YNFGVVALSL YMCYEFVVSG WGTGYTFHCD PVDYSDSPQG LRMAATCWLY
     YFSKFIEMLD TIFFVLRKRN SQVTFLHVYH HSVMPFTWWF GVRFSAGGMG TFHALLNCIV
     HVIMYTYYGL TALGPKYQKY LWWKKHLTTI QLIQFVIVTS HISQYFFMKD CNYQFPIFVY
     IIAAYGLIFL FLFLNFWYHA YTKGKRLPKV LQNQNMVLKY FK
//
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