ELOV3_HUMAN
ID ELOV3_HUMAN Reviewed; 270 AA.
AC Q9HB03; Q5VZL3; Q8N180;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Elongation of very long chain fatty acids protein 3 {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000305};
DE EC=2.3.1.199 {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL3 {ECO:0000255|HAMAP-Rule:MF_03203};
DE AltName: Full=Cold-inducible glycoprotein of 30 kDa;
DE AltName: Full=ELOVL fatty acid elongase 3 {ECO:0000255|HAMAP-Rule:MF_03203};
DE Short=ELOVL FA elongase 3 {ECO:0000255|HAMAP-Rule:MF_03203};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 3 {ECO:0000255|HAMAP-Rule:MF_03203};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 3 {ECO:0000255|HAMAP-Rule:MF_03203};
GN Name=ELOVL3 {ECO:0000255|HAMAP-Rule:MF_03203}; Synonyms=CIG30;
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 GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [2]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-270.
RA Semina E.V., Murray J.C.;
RT "The CIG30/PITX3/GBF1 gene configuration is conserved between human and
RT mouse genomes.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP CATALYTIC ACTIVITY.
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP AND TISSUE 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 exhibits activity toward
CC saturated and unsaturated acyl-CoA substrates with higher activity
CC toward C18 acyl-CoAs, especially C18:0 acyl-CoAs. May participate in
CC the production of saturated and monounsaturated VLCFAs of different
CC chain lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-
CC Rule:MF_03203, 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_03203,
CC ECO:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000305|PubMed:20937905};
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:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35328;
CC Evidence={ECO:0000305|PubMed:20937905};
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:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316;
CC Evidence={ECO:0000305|PubMed:20937905};
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:0000269|PubMed:19575253, ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35320;
CC Evidence={ECO:0000305|PubMed:20937905};
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:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512;
CC Evidence={ECO:0000305|PubMed:20937905};
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:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504;
CC Evidence={ECO:0000305|PubMed:20937905};
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:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524;
CC Evidence={ECO:0000305|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H(+) + malonyl-CoA = 3-oxotetracosanoyl-CoA +
CC CO2 + CoA; Xref=Rhea:RHEA:36507, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:65059, ChEBI:CHEBI:73977;
CC Evidence={ECO:0000269|PubMed:20937905};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36508;
CC Evidence={ECO:0000305|PubMed:20937905};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA
CC + CO2 + CoA; Xref=Rhea:RHEA:39167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57349,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000269|PubMed:19575253};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39168;
CC Evidence={ECO:0000305|PubMed:19575253};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:20937905}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:20937905}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03203}.
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:20937905}.
CC -!- DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000255|HAMAP-Rule:MF_03203}.
CC -!- PTM: N-Glycosylated. {ECO:0000255|HAMAP-Rule:MF_03203,
CC ECO:0000269|PubMed:20937905}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03203}.
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DR EMBL; AL160011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49711.1; -; Genomic_DNA.
DR EMBL; BC034344; AAH34344.1; -; mRNA.
DR EMBL; AF292387; AAG17875.1; -; Genomic_DNA.
DR CCDS; CCDS7531.1; -.
DR RefSeq; NP_689523.1; NM_152310.2.
DR RefSeq; XP_011538547.1; XM_011540245.2.
DR AlphaFoldDB; Q9HB03; -.
DR SMR; Q9HB03; -.
DR BioGRID; 123637; 10.
DR IntAct; Q9HB03; 1.
DR STRING; 9606.ENSP00000359022; -.
DR BindingDB; Q9HB03; -.
DR ChEMBL; CHEMBL5791; -.
DR SwissLipids; SLP:000000248; -.
DR GlyGen; Q9HB03; 2 sites.
DR iPTMnet; Q9HB03; -.
DR PhosphoSitePlus; Q9HB03; -.
DR BioMuta; ELOVL3; -.
DR DMDM; 26006738; -.
DR jPOST; Q9HB03; -.
DR PaxDb; Q9HB03; -.
DR PRIDE; Q9HB03; -.
DR Antibodypedia; 31401; 195 antibodies from 24 providers.
DR DNASU; 83401; -.
DR Ensembl; ENST00000370005.4; ENSP00000359022.3; ENSG00000119915.5.
DR GeneID; 83401; -.
DR KEGG; hsa:83401; -.
DR MANE-Select; ENST00000370005.4; ENSP00000359022.3; NM_152310.3; NP_689523.1.
DR UCSC; uc001kut.5; human.
DR CTD; 83401; -.
DR DisGeNET; 83401; -.
DR GeneCards; ELOVL3; -.
DR HGNC; HGNC:18047; ELOVL3.
DR HPA; ENSG00000119915; Tissue enriched (skin).
DR MIM; 611815; gene.
DR neXtProt; NX_Q9HB03; -.
DR OpenTargets; ENSG00000119915; -.
DR PharmGKB; PA27762; -.
DR VEuPathDB; HostDB:ENSG00000119915; -.
DR eggNOG; KOG3072; Eukaryota.
DR GeneTree; ENSGT01050000244965; -.
DR HOGENOM; CLU_048483_1_1_1; -.
DR InParanoid; Q9HB03; -.
DR OMA; QILQMFM; -.
DR OrthoDB; 1094172at2759; -.
DR PhylomeDB; Q9HB03; -.
DR TreeFam; TF106467; -.
DR BioCyc; MetaCyc:ENSG00000119915-MON; -.
DR PathwayCommons; Q9HB03; -.
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; Q9HB03; -.
DR SIGNOR; Q9HB03; -.
DR UniPathway; UPA00658; -.
DR BioGRID-ORCS; 83401; 10 hits in 1068 CRISPR screens.
DR GenomeRNAi; 83401; -.
DR Pharos; Q9HB03; Tchem.
DR PRO; PR:Q9HB03; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9HB03; protein.
DR Bgee; ENSG00000119915; Expressed in upper leg skin and 96 other tissues.
DR Genevisible; Q9HB03; 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:0102336; F:3-oxo-arachidoyl-CoA synthase activity; IEA:RHEA.
DR GO; GO:0102338; F:3-oxo-lignoceronyl-CoA synthase activity; IEA:RHEA.
DR GO; GO:0009922; F:fatty acid elongase activity; EXP:Reactome.
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; IDA:UniProtKB.
DR GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IDA:UniProtKB.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IDA:UniProtKB.
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:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
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; IDA:UniProtKB.
DR HAMAP; MF_03203; VLCF_elongase_3; 1.
DR InterPro; IPR030457; ELO_CS.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033679; ELOVL3.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR PANTHER; PTHR11157:SF68; PTHR11157:SF68; 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 Glycoprotein; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..270
FT /note="Elongation of very long chain fatty acids protein 3"
FT /id="PRO_0000207540"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03203"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03203"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03203"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03203"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03203"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03203"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03203"
FT MOTIF 266..270
FT /note="Di-lysine motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03203"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03203"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03203"
SQ SEQUENCE 270 AA; 31500 MW; 0C6C8F1E7B5DE8B1 CRC64;
MVTAMNVSHE VNQLFQPYNF ELSKDMRPFF EEYWATSFPI ALIYLVLIAV GQNYMKERKG
FNLQGPLILW SFCLAIFSIL GAVRMWGIMG TVLLTGGLKQ TVCFINFIDN STVKFWSWVF
LLSKVIELGD TAFIILRKRP LIFIHWYHHS TVLVYTSFGY KNKVPAGGWF VTMNFGVHAI
MYTYYTLKAA NVKPPKMLPM LITSLQILQM FVGAIVSILT YIWRQDQGCH TTMEHLFWSF
ILYMTYFILF AHFFCQTYIR PKVKAKTKSQ
