ELOV2_RAT
ID ELOV2_RAT Reviewed; 279 AA.
AC D4A612;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 78.
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:22216341, ECO:0000269|PubMed:23873268};
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22216341; DOI=10.1371/journal.pone.0029662;
RA Gregory M.K., Gibson R.A., Cook-Johnson R.J., Cleland L.G., James M.J.;
RT "Elongase reactions as control points in long-chain polyunsaturated fatty
RT acid synthesis.";
RL PLoS ONE 6:E29662-E29662(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF CYS-217.
RX PubMed=23873268; DOI=10.1194/jlr.m041368;
RA Gregory M.K., Cleland L.G., James M.J.;
RT "Molecular basis for differential elongation of omega-3 docosapentaenoic
RT acid by the rat Elovl5 and Elovl2.";
RL J. Lipid Res. 54:2851-2857(2013).
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. {ECO:0000255|HAMAP-Rule:MF_03202,
CC ECO:0000269|PubMed:22216341, ECO:0000269|PubMed:23873268}.
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:22216341, ECO:0000269|PubMed:23873268};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000305|PubMed:22216341};
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:22216341,
CC ECO:0000269|PubMed:23873268};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36492;
CC Evidence={ECO:0000305|PubMed:22216341};
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:22216341,
CC ECO:0000269|PubMed:23873268};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36484;
CC Evidence={ECO:0000305|PubMed:22216341};
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:22216341};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476;
CC Evidence={ECO:0000305|PubMed:22216341};
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:22216341};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36480;
CC Evidence={ECO:0000305|PubMed:22216341};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:22216341,
CC ECO:0000269|PubMed:23873268}.
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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR06090841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06090842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06090843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06090844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06090845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473977; EDL98219.1; -; Genomic_DNA.
DR EMBL; CH473977; EDL98220.1; -; Genomic_DNA.
DR RefSeq; NP_001102588.1; NM_001109118.1.
DR RefSeq; XP_006253841.1; XM_006253779.3.
DR AlphaFoldDB; D4A612; -.
DR SMR; D4A612; -.
DR BioGRID; 270038; 1.
DR STRING; 10116.ENSRNOP00000019756; -.
DR SwissLipids; SLP:000000273; -.
DR iPTMnet; D4A612; -.
DR PhosphoSitePlus; D4A612; -.
DR PaxDb; D4A612; -.
DR Ensembl; ENSRNOT00000019756; ENSRNOP00000019756; ENSRNOG00000014702.
DR GeneID; 498728; -.
DR KEGG; rno:498728; -.
DR UCSC; RGD:1308605; rat.
DR CTD; 54898; -.
DR RGD; 1308605; Elovl2.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_1_1; -.
DR InParanoid; D4A612; -.
DR OMA; FHKDYFA; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; D4A612; -.
DR TreeFam; TF323454; -.
DR Reactome; R-RNO-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-RNO-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00658; -.
DR PRO; PR:D4A612; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000234681; Chromosome 17.
DR Bgee; ENSRNOG00000014702; Expressed in testis and 12 other tissues.
DR Genevisible; D4A612; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0009922; F:fatty acid elongase activity; ISO:RGD.
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:RGD.
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; ISO:RGD.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:RGD.
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..279
FT /note="Elongation of very long chain fatty acids protein 2"
FT /id="PRO_0000423425"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT MOTIF 276..279
FT /note="Di-lysine motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT MUTAGEN 217
FT /note="C->A: Decreased elongase activity toward
FT (7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA."
FT /evidence="ECO:0000269|PubMed:23873268"
FT MUTAGEN 217
FT /note="C->F: Decreased elongase activity toward
FT (7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA."
FT /evidence="ECO:0000269|PubMed:23873268"
FT MUTAGEN 217
FT /note="C->W: Loss of elongase activity toward
FT (7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA."
FT /evidence="ECO:0000269|PubMed:23873268"
SQ SEQUENCE 279 AA; 32417 MW; 6D3103A7470E8A14 CRC64;
MFGPRDSRVR GWFLLDSYLP TFTLTIVYLL SIWLGNKYMK NRPALSLRGI LTLYNLGITL
LSAYMLVELV LSSWEGGYNL QCQNLDSAGE GDIRVAKVLW WYYFSKLVEF LDTIFFVLRK
KTSQITFLHV YHHASMFNIW WCVLNWIPCG QSFFGPTLNS FIHILMYSYY GLSVFPSMHR
YLWWKKYLTQ AQLVQFVLTI THTLSAVVKP CGFPFGCLIF QSSYMMTLVI LFLNFYIQTY
RKKPMKKEMP EGAAGKEVKN GFPKAHSIAA NGVTDKKVQ
