ELOV7_MOUSE
ID ELOV7_MOUSE Reviewed; 281 AA.
AC Q9D2Y9; Q8BX38; Q8BYY8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Elongation of very long chain fatty acids protein 7 {ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000305};
DE EC=2.3.1.199 {ECO:0000250|UniProtKB:A1L3X0, ECO:0000255|HAMAP-Rule:MF_03207};
DE AltName: Full=3-keto acyl-CoA synthase Elovl7 {ECO:0000255|HAMAP-Rule:MF_03207};
DE AltName: Full=ELOVL fatty acid elongase 7 {ECO:0000255|HAMAP-Rule:MF_03207};
DE Short=ELOVL FA elongase 7 {ECO:0000255|HAMAP-Rule:MF_03207};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 7 {ECO:0000255|HAMAP-Rule:MF_03207};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 7 {ECO:0000255|HAMAP-Rule:MF_03207};
GN Name=Elovl7 {ECO:0000255|HAMAP-Rule:MF_03207};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum, Skin, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 in 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:0000255|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:0000255|HAMAP-Rule:MF_03207};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H(+) + malonyl-CoA = 3-oxodocosanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:35327, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:71451;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35328;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + malonyl-CoA =
CC (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36475, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:73852; Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA =
CC (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:35379, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57363, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:71481; Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z)-
CC 3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36503,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:57384, ChEBI:CHEBI:74012;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = (11Z)-3-
CC oxoicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36511,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-CoA + octadecanoyl-CoA = 3-oxoeicosanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:35319, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:65115;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35320;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + malonyl-CoA = 3-oxooctadecanoyl-CoA
CC + CO2 + CoA; Xref=Rhea:RHEA:35315, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:71407;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA =
CC (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36523, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:74034,
CC ChEBI:CHEBI:74054; Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC Evidence={ECO:0000250|UniProtKB:A1L3X0};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_03207}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03207}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03207}.
CC -!- DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000255|HAMAP-Rule:MF_03207}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL7 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03207}.
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DR EMBL; AK018616; BAB31310.1; -; mRNA.
DR EMBL; AK037162; BAC29727.1; -; mRNA.
DR EMBL; AK049118; BAC33552.1; -; mRNA.
DR EMBL; AK137668; BAE23454.1; -; mRNA.
DR EMBL; BC005602; AAH05602.1; -; mRNA.
DR CCDS; CCDS36779.1; -.
DR RefSeq; NP_083277.3; NM_029001.5.
DR AlphaFoldDB; Q9D2Y9; -.
DR SMR; Q9D2Y9; -.
DR STRING; 10090.ENSMUSP00000022207; -.
DR PhosphoSitePlus; Q9D2Y9; -.
DR MaxQB; Q9D2Y9; -.
DR PaxDb; Q9D2Y9; -.
DR PRIDE; Q9D2Y9; -.
DR ProteomicsDB; 275745; -.
DR Antibodypedia; 23642; 154 antibodies from 24 providers.
DR DNASU; 74559; -.
DR Ensembl; ENSMUST00000022207; ENSMUSP00000022207; ENSMUSG00000021696.
DR GeneID; 74559; -.
DR KEGG; mmu:74559; -.
DR UCSC; uc007rva.2; mouse.
DR CTD; 79993; -.
DR MGI; MGI:1921809; Elovl7.
DR VEuPathDB; HostDB:ENSMUSG00000021696; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_0_1; -.
DR InParanoid; Q9D2Y9; -.
DR OMA; YKAKYLN; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q9D2Y9; -.
DR TreeFam; TF323454; -.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 74559; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q9D2Y9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9D2Y9; protein.
DR Bgee; ENSMUSG00000021696; Expressed in tail skin and 211 other tissues.
DR ExpressionAtlas; Q9D2Y9; baseline and differential.
DR Genevisible; Q9D2Y9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0102336; F:3-oxo-arachidoyl-CoA synthase activity; IEA:RHEA.
DR GO; GO:0009922; F:fatty acid elongase activity; ISO:MGI.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IBA:GO_Central.
DR GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; ISO:MGI.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; ISS:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
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; ISS:UniProtKB.
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; PTHR11157; 1.
DR PANTHER; PTHR11157:SF118; PTHR11157:SF118; 1.
DR Pfam; PF01151; ELO; 1.
DR PROSITE; PS01188; ELO; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..281
FT /note="Elongation of very long chain fatty acids protein 7"
FT /id="PRO_0000311989"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT TRANSMEM 143..162
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT MOTIF 277..281
FT /note="Di-lysine motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03207"
FT CONFLICT 25
FT /note="V -> F (in Ref. 1; BAC29727)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="F -> S (in Ref. 1; BAC33552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 281 AA; 33479 MW; 025B3239F29BCB90 CRC64;
MAFSDLTSRT VRFYDNWIKD ADPRVEDYLL MSSPLPQTII LGLYVYFVTS LGPKLMENRK
PFELKKAMIT YNFFIVLFSV YMCYEFVMSG WGTGYSFRCD IVDYSQSPRA MRMVHTCWLY
YFSKFIELLD TIFFVLRKKN SQVTFLHVFH HTIMPWTWWF GVKFAAGGLG TFHAFLNTAV
HVVMYSYYGL CAMGPAYQKY LWWKKHLTSL QLVQFVLVTI HIGQIFFMED CNYQYPVFLY
IIMSYGCIFL LLFLHFWYRA YTKGQRLPKT LENGNCKSKR H
