ID A0A0R4IT00_DANRE Unreviewed; 320 AA.
AC A0A0R4IT00; A0A8M1PF52;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Elongation of very long chain fatty acids protein 1 {ECO:0000256|HAMAP-Rule:MF_03201};
DE EC=2.3.1.199 {ECO:0000256|HAMAP-Rule:MF_03201};
DE AltName: Full=3-keto acyl-CoA synthase ELOVL1 {ECO:0000256|HAMAP-Rule:MF_03201};
DE AltName: Full=ELOVL fatty acid elongase 1 {ECO:0000256|HAMAP-Rule:MF_03201};
DE Short=ELOVL FA elongase 1 {ECO:0000256|HAMAP-Rule:MF_03201};
DE AltName: Full=Very long chain 3-ketoacyl-CoA synthase 1 {ECO:0000256|HAMAP-Rule:MF_03201};
DE AltName: Full=Very long chain 3-oxoacyl-CoA synthase 1 {ECO:0000256|HAMAP-Rule:MF_03201};
GN Name=elovl1b {ECO:0000313|Ensembl:ENSDARP00000139034,
GN ECO:0000313|RefSeq:NP_001315523.1, ECO:0000313|RefSeq:NP_998581.2,
GN ECO:0000313|RefSeq:XP_009304164.1, ECO:0000313|RefSeq:XP_009304165.1,
GN ECO:0000313|ZFIN:ZDB-GENE-040426-2755};
GN Synonyms=ELOVL1 {ECO:0000256|HAMAP-Rule:MF_03201}, wu:fj32h05
GN {ECO:0000313|RefSeq:NP_001315523.1, ECO:0000313|RefSeq:NP_998581.2,
GN ECO:0000313|RefSeq:XP_009304164.1, ECO:0000313|RefSeq:XP_009304165.1},
GN zgc:56567 {ECO:0000313|RefSeq:NP_001315523.1,
GN ECO:0000313|RefSeq:NP_998581.2, ECO:0000313|RefSeq:XP_009304164.1,
GN ECO:0000313|RefSeq:XP_009304165.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000139034};
RN [1] {ECO:0000313|RefSeq:NP_001315523.1, ECO:0000313|RefSeq:NP_998581.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315523.1,
RC ECO:0000313|RefSeq:NP_998581.2};
RX PubMed=22438865;
RA Gomez G., Lee J.H., Veldman M.B., Lu J., Xiao X., Lin S.;
RT "Identification of vascular and hematopoietic genes downstream of etsrp by
RT deep sequencing in zebrafish.";
RL PLoS ONE 7:E31658-E31658(2012).
RN [2] {ECO:0000313|Ensembl:ENSDARP00000139034, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000139034};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:NP_001315523.1, ECO:0000313|RefSeq:NP_998581.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315523.1,
RC ECO:0000313|RefSeq:NP_998581.2};
RX PubMed=24947308;
RA Azuaje F.J.;
RT "Selecting biologically informative genes in co-expression networks with a
RT centrality score.";
RL Biol. Direct 9:12-12(2014).
RN [4] {ECO:0000313|Ensembl:ENSDARP00000139034}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000139034};
RG Ensembl;
RL Submitted (NOV-2015) to UniProtKB.
RN [5] {ECO:0000313|RefSeq:NP_001315523.1, ECO:0000313|RefSeq:NP_998581.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315523.1,
RC ECO:0000313|RefSeq:NP_998581.2};
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [6] {ECO:0000313|RefSeq:NP_001315523.1, ECO:0000313|RefSeq:NP_998581.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315523.1,
RC ECO:0000313|RefSeq:NP_998581.2};
RX PubMed=27078170;
RA Bhandari S., Lee J.N., Kim Y.I., Nam I.K., Kim S.J., Kim S.J., Kwak S.,
RA Oh G.S., Kim H.J., Yoo H.J., So H.S., Choe S.K., Park R.;
RT "The fatty acid chain elongase, Elovl1, is required for kidney and swim
RT bladder development during zebrafish embryogenesis.";
RL Organogenesis 12:78-93(2016).
RN [7] {ECO:0000313|RefSeq:NP_001315523.1, ECO:0000313|RefSeq:NP_998581.2}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315523.1,
RC ECO:0000313|RefSeq:NP_998581.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 C18 to C26 acyl-CoA substrates, with the highest activity
CC towards C22:0 acyl-CoA. May participate to the production of both
CC saturated and monounsaturated VLCFAs of different chain lengths that
CC are involved in multiple biological processes as precursors of membrane
CC lipids and lipid mediators. {ECO:0000256|HAMAP-Rule:MF_03201}.
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:0000256|HAMAP-Rule:MF_03201,
CC ECO:0000256|RuleBase:RU361115};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_03201}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03201}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03201}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum
CC localization. {ECO:0000256|HAMAP-Rule:MF_03201}.
CC -!- SIMILARITY: Belongs to the ELO family. ELOVL1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03201}.
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DR EMBL; CR847923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FQ790218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001315523.1; NM_001328594.1.
DR RefSeq; NP_998581.2; NM_213416.2.
DR RefSeq; XP_009304164.1; XM_009305889.3.
DR RefSeq; XP_009304165.1; XM_009305890.3.
DR RefSeq; XP_009304166.1; XM_009305891.2.
DR STRING; 7955.ENSDARP00000139034; -.
DR PaxDb; 7955-ENSDARP00000075659; -.
DR Ensembl; ENSDART00000169052.2; ENSDARP00000139034.1; ENSDARG00000103735.2.
DR Ensembl; ENSDART00000181440.1; ENSDARP00000147084.1; ENSDARG00000103735.2.
DR Ensembl; ENSDART00000184477.1; ENSDARP00000151610.1; ENSDARG00000103735.2.
DR Ensembl; ENSDART00000190120.1; ENSDARP00000144796.1; ENSDARG00000103735.2.
DR Ensembl; ENSDART00000191997.1; ENSDARP00000154242.1; ENSDARG00000103735.2.
DR GeneID; 406725; -.
DR KEGG; dre:406725; -.
DR AGR; ZFIN:ZDB-GENE-040426-2755; -.
DR CTD; 406725; -.
DR ZFIN; ZDB-GENE-040426-2755; elovl1b.
DR eggNOG; KOG3071; Eukaryota.
DR OMA; HAMVNSM; -.
DR OrthoDB; 168669at2759; -.
DR Reactome; R-DRE-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-DRE-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-DRE-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000437; Chromosome 11.
DR Bgee; ENSDARG00000103735; Expressed in granulocyte and 48 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009922; F:fatty acid elongase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IMP:ZFIN.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0048794; P:swim bladder development; IGI:ZFIN.
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; IBA:GO_Central.
DR HAMAP; MF_03201; VLCF_elongase_1; 1.
DR InterPro; IPR002076; ELO_fam.
DR InterPro; IPR033681; ELOVL1.
DR PANTHER; PTHR11157:SF19; ELONGATION OF VERY LONG CHAIN FATTY ACIDS PROTEIN 1; 1.
DR PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01151; ELO; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03201};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_03201};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_03201};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03201,
KW ECO:0000256|RuleBase:RU361115};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03201,
KW ECO:0000256|RuleBase:RU361115};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03201};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03201};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03201};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03201}.
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 142..161
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 205..226
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT TRANSMEM 232..257
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201,
FT ECO:0000256|RuleBase:RU361115"
FT REGION 270..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 316..320
FT /note="Di-lysine motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03201"
FT COMPBIAS 270..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 320 AA; 37043 MW; 36D7432240FF0DDE CRC64;
MLETVKDRVL EAYGSLLAAR DPRLKDYPLM ESPFSMTAIL LAYLFFVLYA GPKFMANRKP
FQLKEAMIIY NLSLVGLSAY IVYEFLMSGW ATGYTWRCDP CDYSNSPQGL RMARVAWLFL
FSKFIELMDT VFFVLRKKHS QITFLHIFHH SFMPWTWWWG VSIVPGGMGS FHAMVNSCVH
VIMYFYYGLS AAGPRFQKFL WWKKYMTAIQ LTQFVLVSLH VSQWYFMESC DFQVPVIIHL
IWLYGTFFFV LFSNFWYQAY IKGKRLPKNT QETTKTNGST IVTNGSSGVS NGHAIHENGL
SNGKKHHENG NALNGKMKKA
//
