ELOV2_MOUSE
ID ELOV2_MOUSE Reviewed; 292 AA.
AC Q9JLJ4; Q9D5Z2;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Elongation of very long chain fatty acids protein 2 {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000305};
DE EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:12371743, ECO:0000269|PubMed:21106902};
DE AltName: Full=3-keto acyl-CoA synthase Elovl2 {ECO:0000255|HAMAP-Rule:MF_03202};
DE AltName: Full=ELOVL fatty acid elongase 2 {ECO:0000255|HAMAP-Rule:MF_03202};
DE Short=ELOVL FA elongase 2 {ECO:0000255|HAMAP-Rule:MF_03202};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 2 {ECO:0000255|HAMAP-Rule:MF_03202};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 2 {ECO:0000255|HAMAP-Rule:MF_03202};
GN Name=Elovl2 {ECO:0000255|HAMAP-Rule:MF_03202}; Synonyms=Ssc2;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=10791983; DOI=10.1083/jcb.149.3.707;
RA Tvrdik P., Westerberg R., Silve S., Asadi A., Jakobsson A., Cannon B.,
RA Loison G., Jacobsson A.;
RT "Role of a new mammalian gene family in the biosynthesis of very long chain
RT fatty acids and sphingolipids.";
RL J. Cell Biol. 149:707-718(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=12371743; DOI=10.1007/s11745-002-0955-6;
RA Leonard A.E., Kelder B., Bobik E.G., Chuang L.-T., Lewis C.J.,
RA Kopchick J.J., Mukerji P., Huang Y.-S.;
RT "Identification and expression of mammalian long-chain PUFA elongation
RT enzymes.";
RL Lipids 37:733-740(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=21106902; DOI=10.1194/jlr.m011346;
RA Zadravec D., Tvrdik P., Guillou H., Haslam R., Kobayashi T., Napier J.A.,
RA Capecchi M.R., Jacobsson A.;
RT "ELOVL2 controls the level of n-6 28:5 and 30:5 fatty acids in testis, a
RT prerequisite for male fertility and sperm maturation in mice.";
RL J. Lipid Res. 52:245-255(2011).
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 that catalyzes the synthesis of
CC polyunsaturated very long chain fatty acid (C20- and C22-PUFA), acting
CC specifically toward polyunsaturated acyl-CoA with the higher activity
CC toward C20:4(n-6) acyl-CoA. May participate in 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. Essential for the formation of C24:5(n-6) up to
CC C30:5(n-6) PUFAs in testis, these fatty acids being indispensable for
CC normal spermatogenesis and fertility. {ECO:0000255|HAMAP-Rule:MF_03202,
CC ECO:0000269|PubMed:12371743, ECO:0000269|PubMed:21106902}.
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_03202,
CC ECO:0000269|PubMed:12371743, ECO:0000269|PubMed:21106902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000305|PubMed:12371743};
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:0000269|PubMed:12371743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476;
CC Evidence={ECO:0000305|PubMed:12371743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + H(+) + malonyl-CoA =
CC (9Z,12Z,15Z,18Z)-3-oxotetracosatetraenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36479, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:73856,
CC ChEBI:CHEBI:73857; Evidence={ECO:0000269|PubMed:12371743,
CC ECO:0000269|PubMed:21106902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36480;
CC Evidence={ECO:0000305|PubMed:12371743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + H(+) + malonyl-CoA
CC = (7Z,10Z,13Z,16Z,19Z)-3-oxodocosapentaenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36483, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:73862,
CC ChEBI:CHEBI:73863; Evidence={ECO:0000269|PubMed:12371743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36484;
CC Evidence={ECO:0000305|PubMed:12371743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA + H(+) + malonyl-CoA
CC = (9Z,12Z,15Z,18Z,21Z)-3-oxotetracosapentaenoyl-CoA + CO2 + CoA;
CC Xref=Rhea:RHEA:36491, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:73870,
CC ChEBI:CHEBI:73871; Evidence={ECO:0000269|PubMed:12371743,
CC ECO:0000269|PubMed:21106902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36492;
CC Evidence={ECO:0000305|PubMed:12371743};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:12371743,
CC ECO:0000269|PubMed:21106902}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03202}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03202}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, lower level in liver.
CC Weakly expressed in white adipose tissue, brain and kidney.
CC {ECO:0000269|PubMed:10791983, ECO:0000269|PubMed:12371743}.
CC -!- DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000255|HAMAP-Rule:MF_03202}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03202}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29559.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF170908; AAF72573.1; -; mRNA.
DR EMBL; AK014803; BAB29559.1; ALT_INIT; mRNA.
DR EMBL; AK029855; BAC26646.1; -; mRNA.
DR CCDS; CCDS36639.1; -.
DR RefSeq; NP_001298050.1; NM_001311121.1.
DR RefSeq; NP_062296.1; NM_019423.2.
DR AlphaFoldDB; Q9JLJ4; -.
DR SMR; Q9JLJ4; -.
DR STRING; 10090.ENSMUSP00000021793; -.
DR SwissLipids; SLP:000000258; -.
DR SwissLipids; SLP:000000556; -.
DR iPTMnet; Q9JLJ4; -.
DR PhosphoSitePlus; Q9JLJ4; -.
DR jPOST; Q9JLJ4; -.
DR MaxQB; Q9JLJ4; -.
DR PaxDb; Q9JLJ4; -.
DR PRIDE; Q9JLJ4; -.
DR ProteomicsDB; 277852; -.
DR Antibodypedia; 44274; 177 antibodies from 25 providers.
DR DNASU; 54326; -.
DR Ensembl; ENSMUST00000021793; ENSMUSP00000021793; ENSMUSG00000021364.
DR GeneID; 54326; -.
DR KEGG; mmu:54326; -.
DR UCSC; uc007qfb.2; mouse.
DR CTD; 54898; -.
DR MGI; MGI:1858960; Elovl2.
DR VEuPathDB; HostDB:ENSMUSG00000021364; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR InParanoid; Q9JLJ4; -.
DR OMA; FHKDYFA; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q9JLJ4; -.
DR TreeFam; TF323454; -.
DR Reactome; R-MMU-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-MMU-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00658; -.
DR BioGRID-ORCS; 54326; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q9JLJ4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9JLJ4; protein.
DR Bgee; ENSMUSG00000021364; Expressed in liver and 190 other tissues.
DR ExpressionAtlas; Q9JLJ4; baseline and differential.
DR Genevisible; Q9JLJ4; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:MGI.
DR GO; GO:0009922; F:fatty acid elongase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:MGI.
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; PTHR11157; 1.
DR PANTHER; PTHR11157:SF16; PTHR11157:SF16; 1.
DR Pfam; PF01151; ELO; 1.
DR PROSITE; PS01188; ELO; 1.
PE 1: Evidence at protein 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..292
FT /note="Elongation of very long chain fatty acids protein 2"
FT /id="PRO_0000207539"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT MOTIF 289..292
FT /note="Di-lysine motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
SQ SEQUENCE 292 AA; 34207 MW; E1959B8DFC43A7D3 CRC64;
MEQLKAFDNE VNAFLDNMFG PRDSRVRGWF LLDSYLPTFI LTITYLLSIW LGNKYMKNRP
ALSLRGILTL YNLAITLLSA YMLVELILSS WEGGYNLQCQ NLDSAGEGDV RVAKVLWWYY
FSKLVEFLDT IFFVLRKKTN QITFLHVYHH ASMFNIWWCV LNWIPCGQSF FGPTLNSFIH
ILMYSYYGLS VFPSMHKYLW WKKYLTQAQL VQFVLTITHT LSAVVKPCGF PFGCLIFQSS
YMMTLVILFL NFYIQTYRKK PVKKELQEKE VKNGFPKAHL IVANGMTDKK AQ
