ELOV2_HUMAN
ID ELOV2_HUMAN Reviewed; 296 AA.
AC Q9NXB9; Q6P9E1; Q86W94;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 155.
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:11734209, ECO:0000269|PubMed:12371743, ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905};
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};
GN Synonyms=ELG3 {ECO:0000303|PubMed:11734209}, SSC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-216.
RC TISSUE=Brain, and Testis;
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).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11734209; DOI=10.1016/s0014-5793(01)03135-0;
RA de Antueno R.J., Knickle L.C., Smith H., Elliot M.L., Allen S.J., Nwaka S.,
RA Winther M.D.;
RT "Activity of human Delta5 and Delta6 desaturases on multiple n-3 and n-6
RT polyunsaturated fatty acids.";
RL FEBS Lett. 509:77-80(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=19575253; DOI=10.1007/s11745-009-3320-8;
RA Kitazawa H., Miyamoto Y., Shimamura K., Nagumo A., Tokita S.;
RT "Development of a high-density assay for long-chain fatty acyl-CoA
RT elongases.";
RL Lipids 44:765-773(2009).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20937905; DOI=10.1073/pnas.1005572107;
RA Ohno Y., Suto S., Yamanaka M., Mizutani Y., Mitsutake S., Igarashi Y.,
RA Sassa T., Kihara A.;
RT "ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid
RT synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18439-18444(2010).
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:11734209, ECO:0000269|PubMed:12371743,
CC ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905}.
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:11734209, ECO:0000269|PubMed:12371743,
CC ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000305|PubMed:11734209};
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:11734209,
CC ECO:0000269|PubMed:12371743, ECO:0000269|PubMed:19575253,
CC ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476;
CC Evidence={ECO:0000305|PubMed:11734209};
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:11734209,
CC ECO:0000269|PubMed:12371743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36480;
CC Evidence={ECO:0000305|PubMed:11734209};
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:11734209,
CC ECO:0000269|PubMed:12371743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36484;
CC Evidence={ECO:0000305|PubMed:11734209};
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:11734209,
CC ECO:0000269|PubMed:12371743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36492;
CC Evidence={ECO:0000305|PubMed:11734209};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:11734209,
CC ECO:0000269|PubMed:12371743, ECO:0000269|PubMed:19575253,
CC ECO:0000269|PubMed:20937905}.
CC -!- INTERACTION:
CC Q9NXB9; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-17206972, EBI-713304;
CC Q9NXB9; Q01628: IFITM3; NbExp=3; IntAct=EBI-17206972, EBI-7932862;
CC Q9NXB9; Q13021: MALL; NbExp=3; IntAct=EBI-17206972, EBI-750078;
CC Q9NXB9; A2RU14: TMEM218; NbExp=3; IntAct=EBI-17206972, EBI-10173151;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03202, ECO:0000269|PubMed:20937905}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03202}.
CC -!- TISSUE SPECIFICITY: Liver and testis. {ECO:0000269|PubMed:20937905}.
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}.
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DR EMBL; AK000341; BAA91096.1; -; mRNA.
DR EMBL; AL121955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55291.1; -; Genomic_DNA.
DR EMBL; BC050278; AAH50278.2; -; mRNA.
DR EMBL; BC060809; AAH60809.1; -; mRNA.
DR CCDS; CCDS4518.1; -.
DR RefSeq; NP_060240.3; NM_017770.3.
DR AlphaFoldDB; Q9NXB9; -.
DR SMR; Q9NXB9; -.
DR BioGRID; 120244; 57.
DR IntAct; Q9NXB9; 12.
DR STRING; 9606.ENSP00000346693; -.
DR BindingDB; Q9NXB9; -.
DR ChEMBL; CHEMBL5911; -.
DR DrugBank; DB00132; alpha-Linolenic acid.
DR SwissLipids; SLP:000000245; -.
DR iPTMnet; Q9NXB9; -.
DR PhosphoSitePlus; Q9NXB9; -.
DR SwissPalm; Q9NXB9; -.
DR BioMuta; ELOVL2; -.
DR DMDM; 187472388; -.
DR MassIVE; Q9NXB9; -.
DR MaxQB; Q9NXB9; -.
DR PaxDb; Q9NXB9; -.
DR PeptideAtlas; Q9NXB9; -.
DR PRIDE; Q9NXB9; -.
DR ProteomicsDB; 83070; -.
DR Antibodypedia; 44274; 177 antibodies from 25 providers.
DR DNASU; 54898; -.
DR Ensembl; ENST00000354666.4; ENSP00000346693.3; ENSG00000197977.4.
DR GeneID; 54898; -.
DR KEGG; hsa:54898; -.
DR MANE-Select; ENST00000354666.4; ENSP00000346693.3; NM_017770.4; NP_060240.3.
DR UCSC; uc003mzp.5; human.
DR CTD; 54898; -.
DR DisGeNET; 54898; -.
DR GeneCards; ELOVL2; -.
DR HGNC; HGNC:14416; ELOVL2.
DR HPA; ENSG00000197977; Tissue enhanced (liver, placenta, retina).
DR MIM; 611814; gene.
DR neXtProt; NX_Q9NXB9; -.
DR OpenTargets; ENSG00000197977; -.
DR PharmGKB; PA27761; -.
DR VEuPathDB; HostDB:ENSG00000197977; -.
DR eggNOG; KOG3071; Eukaryota.
DR GeneTree; ENSGT01050000244838; -.
DR HOGENOM; CLU_048483_0_1_1; -.
DR InParanoid; Q9NXB9; -.
DR OMA; FHKDYFA; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q9NXB9; -.
DR TreeFam; TF323454; -.
DR BioCyc; MetaCyc:ENSG00000096256-MON; -.
DR PathwayCommons; Q9NXB9; -.
DR Reactome; R-HSA-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SignaLink; Q9NXB9; -.
DR SIGNOR; Q9NXB9; -.
DR UniPathway; UPA00658; -.
DR BioGRID-ORCS; 54898; 9 hits in 1069 CRISPR screens.
DR ChiTaRS; ELOVL2; human.
DR GenomeRNAi; 54898; -.
DR Pharos; Q9NXB9; Tbio.
DR PRO; PR:Q9NXB9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NXB9; protein.
DR Bgee; ENSG00000197977; Expressed in ventricular zone and 132 other tissues.
DR ExpressionAtlas; Q9NXB9; baseline and differential.
DR Genevisible; Q9NXB9; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
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:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
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:0043651; P:linoleic acid metabolic process; TAS:Reactome.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
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 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..296
FT /note="Elongation of very long chain fatty acids protein 2"
FT /id="PRO_0000207538"
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 208..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 293..296
FT /note="Di-lysine motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03202"
FT VARIANT 216
FT /note="T -> A (in dbSNP:rs17855038)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039039"
FT VARIANT 225
FT /note="V -> M (in dbSNP:rs6919726)"
FT /id="VAR_039040"
FT CONFLICT 31
FT /note="M -> T (in Ref. 1; BAA91096)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="I -> V (in Ref. 1; BAA91096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 34585 MW; CFB09952FBE90957 CRC64;
MEHLKAFDDE INAFLDNMFG PRDSRVRGWF MLDSYLPTFF LTVMYLLSIW LGNKYMKNRP
ALSLRGILTL YNLGITLLSA YMLAELILST WEGGYNLQCQ DLTSAGEADI RVAKVLWWYY
FSKSVEFLDT IFFVLRKKTS QITFLHVYHH ASMFNIWWCV LNWIPCGQSF FGPTLNSFIH
ILMYSYYGLS VFPSMHKYLW WKKYLTQAQL VQFVLTITHT MSAVVKPCGF PFGCLIFQSS
YMLTLVILFL NFYVQTYRKK PMKKDMQEPP AGKEVKNGFS KAYFTAANGV MNKKAQ
