TECR_CAEEL
ID TECR_CAEEL Reviewed; 308 AA.
AC Q9N5Y2;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable very-long-chain enoyl-CoA reductase art-1;
DE EC=1.3.1.93;
GN Name=art-1; ORFNames=C15F1.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Catalyzes the last of the four reactions of the long-chain
CC fatty acids elongation cycle. This endoplasmic reticulum-bound
CC enzymatic process, allows the addition of 2 carbons to the chain of
CC long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme
CC reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA
CC that can be further elongated by entering a new cycle of elongation.
CC Thereby, it participates in the production of VLCFAs of different chain
CC lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators.
CC {ECO:0000250|UniProtKB:Q9NZ01}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain 2,3-saturated fatty acyl-CoA + NADP(+) = a
CC very-long-chain (2E)-enoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:14473,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83724, ChEBI:CHEBI:83728; EC=1.3.1.93;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q9NZ01}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NZ01}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9NZ01}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
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DR EMBL; FO080553; CCD64616.1; -; Genomic_DNA.
DR RefSeq; NP_495430.1; NM_063029.5.
DR AlphaFoldDB; Q9N5Y2; -.
DR SMR; Q9N5Y2; -.
DR BioGRID; 39478; 9.
DR DIP; DIP-27027N; -.
DR STRING; 6239.C15F1.6; -.
DR EPD; Q9N5Y2; -.
DR PaxDb; Q9N5Y2; -.
DR PeptideAtlas; Q9N5Y2; -.
DR EnsemblMetazoa; C15F1.6.1; C15F1.6.1; WBGene00000198.
DR GeneID; 174140; -.
DR KEGG; cel:CELE_C15F1.6; -.
DR UCSC; C15F1.6.1; c. elegans.
DR CTD; 174140; -.
DR WormBase; C15F1.6; CE20509; WBGene00000198; art-1.
DR eggNOG; KOG1639; Eukaryota.
DR GeneTree; ENSGT00950000182886; -.
DR HOGENOM; CLU_059260_1_0_1; -.
DR InParanoid; Q9N5Y2; -.
DR OMA; AWKTVFM; -.
DR OrthoDB; 720263at2759; -.
DR PhylomeDB; Q9N5Y2; -.
DR Reactome; R-CEL-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9N5Y2; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000198; Expressed in larva and 4 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0102758; F:very-long-chain enoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039357; SRD5A/TECR.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10556; PTHR10556; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..308
FT /note="Probable very-long-chain enoyl-CoA reductase art-1"
FT /id="PRO_0000421284"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 7..85
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ SEQUENCE 308 AA; 35110 MW; CB1F4DAF70D1B9B1 CRC64;
MSGILEVYDA KRTDNLIITL EGISGSETIK AIKKRIAQKK LKLTEERQAL RVEPKGKPLA
DDQKLSDLGL SSQKAVLYVR DLGPQIAWKT VFMAEYAGPL FVYPLFYLRP TFIYGQAAVN
ATMHPAVQIA FFAWSFHYAK RLFETQFIHR FGNSTMPQFN LVKNCSYYWG FAAFVAYFVN
HPLFTPPAFG DLQVYFGLAG FVISEFGNLS IHILLRNLRP AGTRERRIPK PDGNPLSLLF
NYVSCPNYTY EVASWIFFSI MVQSLPAIIF TTAGFAQMAI WAQGKHRNYL KEFPDYPKNR
KAIVPFVL
