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Elongation of very long chain fatty acids protein 3 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl3) (CIN-2) (Cold-inducible glycoprotein of 30 kDa) (ELOVL fatty acid elongase 3) (ELOVL FA elongase 3) (Very long chain 3-ketoacyl-CoA synthase 3) (Very long chain 3-oxoacyl-CoA synthase 3)

 ELOV3_MOUSE             Reviewed;         271 AA.
O35949;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
28-MAR-2018, entry version 136.
RecName: Full=Elongation of very long chain fatty acids protein 3 {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000305};
EC=2.3.1.199 {ECO:0000250|UniProtKB:Q9HB03, ECO:0000255|HAMAP-Rule:MF_03203};
AltName: Full=3-keto acyl-CoA synthase Elovl3 {ECO:0000255|HAMAP-Rule:MF_03203};
AltName: Full=CIN-2;
AltName: Full=Cold-inducible glycoprotein of 30 kDa;
AltName: Full=ELOVL fatty acid elongase 3 {ECO:0000255|HAMAP-Rule:MF_03203};
Short=ELOVL FA elongase 3 {ECO:0000255|HAMAP-Rule:MF_03203};
AltName: Full=Very long chain 3-ketoacyl-CoA synthase 3 {ECO:0000255|HAMAP-Rule:MF_03203};
AltName: Full=Very long chain 3-oxoacyl-CoA synthase 3 {ECO:0000255|HAMAP-Rule:MF_03203};
Name=Elovl3 {ECO:0000255|HAMAP-Rule:MF_03203}; Synonyms=Cig30;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION AT ASN-6, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Brown adipose tissue;
PubMed=9395518; DOI=10.1074/jbc.272.50.31738;
Tvrdik P., Asadi A., Kozak L.P., Nedergaard J., Cannon B.,
Jacobsson A.;
"Cig30, a mouse member of a novel membrane protein gene family, is
involved in the recruitment of brown adipose tissue.";
J. Biol. Chem. 272:31738-31746(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=10473596; DOI=10.1074/jbc.274.37.26387;
Tvrdik P., Asadi A., Kozak L.P., Nuglozeh E., Parente F.,
Nedergaard J., Jacobsson A.;
"Cig30 and Pitx3 genes are arranged in a partially overlapping tail-
to-tail array resulting in complementary transcripts.";
J. Biol. Chem. 274:26387-26392(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
GLYCOSYLATION AT ASN-6, AND SUBCELLULAR LOCATION.
PubMed=10429212; DOI=10.1046/j.1432-1327.1999.00498.x;
Monne M., Gafvelin G., Nilsson R., von Heijne G.;
"N-tail translocation in a eukaryotic polytopic membrane protein:
synergy between neighboring transmembrane segments.";
Eur. J. Biochem. 263:264-269(1999).
[5]
FUNCTION.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=10791983; DOI=10.1083/jcb.149.3.707;
Tvrdik P., Westerberg R., Silve S., Asadi A., Jakobsson A., Cannon B.,
Loison G., Jacobsson A.;
"Role of a new mammalian gene family in the biosynthesis of very long
chain fatty acids and sphingolipids.";
J. Cell Biol. 149:707-718(2000).
[6]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=14581464; DOI=10.1074/jbc.M310529200;
Westerberg R., Tvrdik P., Unden A.B., Mansson J.E., Norlen L.,
Jakobsson A., Holleran W.H., Elias P.M., Asadi A., Flodby P.,
Toftgard R., Capecchi M.R., Jacobsson A.;
"Role for ELOVL3 and fatty acid chain length in development of hair
and skin function.";
J. Biol. Chem. 279:5621-5629(2004).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16326704; DOI=10.1074/jbc.M511588200;
Westerberg R., Mansson J.E., Golozoubova V., Shabalina I.G.,
Backlund E.C., Tvrdik P., Retterstol K., Capecchi M.R., Jacobsson A.;
"ELOVL3 is an important component for early onset of lipid recruitment
in brown adipose tissue.";
J. Biol. Chem. 281:4958-4968(2006).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20605947; DOI=10.1096/fj.09-152298;
Zadravec D., Brolinson A., Fisher R.M., Carneheim C., Csikasz R.I.,
Bertrand-Michel J., Boren J., Guillou H., Rudling M., Jacobsso A.;
"Ablation of the very-long-chain fatty acid elongase ELOVL3 in mice
leads to constrained lipid storage and resistance to diet-induced
obesity.";
FASEB J. 24:4366-4377(2010).
-!- FUNCTION: Catalyzes the first and rate-limiting reaction of the
four that constitute the long-chain fatty acids elongation cycle.
This endoplasmic reticulum-bound enzymatic process, allows the
addition of 2 carbons to the chain of long- and very long-chain
fatty acids/VLCFAs per cycle. Condensing enzyme with higher
activity toward C18 acyl-CoAs, especially C18:0 acyl-CoAs. May
participate in the production of saturated and monounsaturated
VLCFAs of different chain lengths that are involved in multiple
biological processes as precursors of membrane lipids and lipid
mediators. Participates in the formation of certain VLCFA and
triglycerides in certain cells of the hair follicles and the
sebaceous glands, required for skin barrier function. Critical
enzyme for lipid accumulation and metabolic activity in brown
adipocytes during the early phase of the tissue recruitment. Play
a role in lipid storage and in resistance to diet-induced obesity.
{ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:10791983,
ECO:0000269|PubMed:14581464, ECO:0000269|PubMed:16326704,
ECO:0000269|PubMed:20605947}.
-!- CATALYTIC ACTIVITY: A very-long-chain acyl-CoA + malonyl-CoA = CoA
+ a very-long-chain 3-oxoacyl-CoA + CO(2). {ECO:0000255|HAMAP-
Rule:MF_03203}.
-!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid
biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03203}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:10429212};
Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03203}.
-!- TISSUE SPECIFICITY: Expressed in brown adipose tissue and liver.
In the skin, strong expressed in the cells of the inner layer of
the outer root sheath of the hair follicles and in the sebocytes
of the sebaceous glands. Hardly detectable in the epidermis and
not at all in fibroblasts. {ECO:0000269|PubMed:14581464,
ECO:0000269|PubMed:9395518}.
-!- INDUCTION: Strongly up-regulated in brown adipose tissue in
conditions of brown fat recruitment, such as cold stress,
perinatal development and after diet-induced thermogenesis. A
synergistic action of both catecholamines and glucocorticoids is
required for the induction.
-!- PTM: N-Glycosylated. {ECO:0000255|HAMAP-Rule:MF_03203,
ECO:0000269|PubMed:10429212}.
-!- DISRUPTION PHENOTYPE: Mutant mice grow normally and are fertile.
They display a sparse hair coat, a hyperplastic pilosebaceous
system and their hair lipid content is disturbed with
exceptionally high levels of eicosenoic acid (20:1). In the
triglyceride fraction, fatty acids longer than 20 carbon atoms are
almost undetectable. As a result, mice exhibited a severe defect
in water repulsion and increased trans-epidermal water loss. When
exposed to cold stress, mutants exhibit a significantly reduced
VLCFA elongation activity in brown adipose tissue, but only during
the initial phase. Cold-acclimated mutants are equally efficient
as normal mice at elongating fatty acids. Mutant mice are lean and
resistant to diet-induced weight gain, they show normal food
intake but increased metabolic rate, and show reduced hepatic
lipogenesis and triglycerides synthesis.
{ECO:0000269|PubMed:14581464, ECO:0000269|PubMed:16326704,
ECO:0000269|PubMed:20605947}.
-!- SIMILARITY: Belongs to the ELO family. ELOVL3 subfamily.
{ECO:0000255|HAMAP-Rule:MF_03203}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U97107; AAC06127.1; -; mRNA.
EMBL; AF054504; AAD51088.1; -; Genomic_DNA.
EMBL; BC016468; AAH16468.1; -; mRNA.
CCDS; CCDS29871.1; -.
RefSeq; NP_031729.1; NM_007703.2.
UniGene; Mm.21806; -.
STRING; 10090.ENSMUSP00000036357; -.
BindingDB; O35949; -.
ChEMBL; CHEMBL5775; -.
iPTMnet; O35949; -.
PhosphoSitePlus; O35949; -.
MaxQB; O35949; -.
PaxDb; O35949; -.
PRIDE; O35949; -.
Ensembl; ENSMUST00000043739; ENSMUSP00000036357; ENSMUSG00000038754.
GeneID; 12686; -.
KEGG; mmu:12686; -.
UCSC; uc008hsk.1; mouse.
CTD; 83401; -.
MGI; MGI:1195976; Elovl3.
eggNOG; KOG3072; Eukaryota.
eggNOG; ENOG410Z3FZ; LUCA.
GeneTree; ENSGT00760000119122; -.
HOGENOM; HOG000038943; -.
HOVERGEN; HBG099423; -.
InParanoid; O35949; -.
KO; K10248; -.
OMA; FGYKNKV; -.
OrthoDB; EOG091G0EKU; -.
PhylomeDB; O35949; -.
TreeFam; TF106467; -.
Reactome; R-MMU-2046105; Linoleic acid (LA) metabolism.
Reactome; R-MMU-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
UniPathway; UPA00658; -.
PRO; PR:O35949; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000038754; -.
Genevisible; O35949; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0102336; F:3-oxo-arachidoyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0102337; F:3-oxo-cerotoyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0102338; F:3-oxo-lignoceronyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0009922; F:fatty acid elongase activity; ISO:MGI.
GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IMP:UniProtKB.
GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; ISO:MGI.
GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IMP:UniProtKB.
GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IMP:UniProtKB.
HAMAP; MF_03203; VLCF_elongase_3; 1.
InterPro; IPR030457; ELO_CS.
InterPro; IPR002076; ELO_fam.
InterPro; IPR033679; ELOVL3.
PANTHER; PTHR11157; PTHR11157; 1.
PANTHER; PTHR11157:SF68; PTHR11157:SF68; 1.
Pfam; PF01151; ELO; 1.
PROSITE; PS01188; ELO; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Fatty acid biosynthesis;
Fatty acid metabolism; Glycoprotein; Lipid biosynthesis;
Lipid metabolism; Membrane; Reference proteome; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 271 Elongation of very long chain fatty acids
protein 3.
/FTId=PRO_0000207541.
TRANSMEM 30 50 Helical. {ECO:0000255|HAMAP-
Rule:MF_03203}.
TRANSMEM 67 87 Helical. {ECO:0000255|HAMAP-
Rule:MF_03203}.
TRANSMEM 116 136 Helical. {ECO:0000255|HAMAP-
Rule:MF_03203}.
TRANSMEM 141 161 Helical. {ECO:0000255|HAMAP-
Rule:MF_03203}.
TRANSMEM 165 187 Helical. {ECO:0000255|HAMAP-
Rule:MF_03203}.
TRANSMEM 199 219 Helical. {ECO:0000255|HAMAP-
Rule:MF_03203}.
TRANSMEM 236 256 Helical. {ECO:0000255|HAMAP-
Rule:MF_03203}.
CARBOHYD 6 6 N-linked (GlcNAc...) asparagine.
{ECO:0000255|HAMAP-Rule:MF_03203,
ECO:0000269|PubMed:10429212,
ECO:0000269|PubMed:9395518}.
SEQUENCE 271 AA; 32060 MW; F7CA96199BE89401 CRC64;
MDTSMNFSRG LKMDLMQPYD FETFQDLRPF LEEYWVSSFL IVVVYLLLIV VGQTYMRTRK
SFSLQRPLIL WSFFLAIFSI LGTLRMWKFM ATVMFTVGLK QTVCFAIYTD DAVVRFWSFL
FLLSKVVELG DTAFIILRKR PLIFVHWYHH STVLLFTSFG YKNKVPSGGW FMTMNFGVHS
VMYTYYTMKA AKLKHPNLLP MVITSLQILQ MVLGTIFGIL NYIWRQEKGC HTTTEHFFWS
FMLYGTYFIL FAHFFHRAYL RPKGKVASKS Q


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