TECR_BOVIN
ID TECR_BOVIN Reviewed; 308 AA.
AC Q3ZCD7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Very-long-chain enoyl-CoA reductase {ECO:0000305};
DE EC=1.3.1.93 {ECO:0000250|UniProtKB:Q9NZ01};
DE AltName: Full=Synaptic glycoprotein SC2;
DE AltName: Full=Trans-2,3-enoyl-CoA reductase;
DE Short=TER;
GN Name=TECR; Synonyms=GPSN2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in both the production of very long-chain fatty
CC acids for sphingolipid synthesis and the degradation of the sphingosine
CC moiety in sphingolipids through the sphingosine 1-phosphate metabolic
CC pathway (By similarity). Catalyzes the last of the four reactions of
CC the long-chain fatty acids elongation cycle (By similarity). This
CC endoplasmic reticulum-bound enzymatic process, allows the addition of 2
CC carbons to the chain of long- and very long-chain fatty acids/VLCFAs
CC per cycle (By similarity). This enzyme reduces the trans-2,3-enoyl-CoA
CC fatty acid intermediate to an acyl-CoA that can be further elongated by
CC entering a new cycle of elongation (By similarity). Thereby, it
CC participates in the production of VLCFAs of different chain lengths
CC that are involved in multiple biological processes as precursors of
CC membrane lipids and lipid mediators (By similarity). Catalyzes the
CC saturation step of the sphingosine 1-phosphate metabolic pathway, the
CC conversion of trans-2-hexadecenoyl-CoA to palmitoyl-CoA (By
CC similarity). {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 PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14475;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + octadecanoyl-CoA = (2E)-octadecenoyl-CoA + H(+) +
CC NADPH; Xref=Rhea:RHEA:35351, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:71412;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35353;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,7Z,10Z,13Z,16Z)-docosapentaenoyl-CoA + H(+) + NADPH =
CC (7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:39331, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:73856, ChEBI:CHEBI:76416;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39332;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + H(+) + NADPH =
CC (7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:39467, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:73870, ChEBI:CHEBI:76461;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39468;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + NADPH =
CC (8Z,11Z,14Z)-eicosatrienoyl-CoA + NADP(+); Xref=Rhea:RHEA:39319,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:74264, ChEBI:CHEBI:76412;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39320;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexadecenoyl-CoA + H(+) + NADPH = hexadecanoyl-CoA +
CC NADP(+); Xref=Rhea:RHEA:36143, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61526;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36144;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q9NZ01}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:Q9NZ01}.
CC -!- SUBUNIT: Interacts with ELOVL1 and LASS2.
CC {ECO:0000250|UniProtKB:Q9NZ01}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NZ01}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q64232}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
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DR EMBL; BC102503; AAI02504.1; -; mRNA.
DR RefSeq; NP_001029920.1; NM_001034748.2.
DR AlphaFoldDB; Q3ZCD7; -.
DR BMRB; Q3ZCD7; -.
DR SMR; Q3ZCD7; -.
DR BioGRID; 541780; 1.
DR STRING; 9913.ENSBTAP00000036133; -.
DR PaxDb; Q3ZCD7; -.
DR PeptideAtlas; Q3ZCD7; -.
DR PRIDE; Q3ZCD7; -.
DR Ensembl; ENSBTAT00000036271; ENSBTAP00000036133; ENSBTAG00000012632.
DR GeneID; 614105; -.
DR KEGG; bta:614105; -.
DR CTD; 9524; -.
DR VEuPathDB; HostDB:ENSBTAG00000012632; -.
DR VGNC; VGNC:35730; TECR.
DR eggNOG; KOG1639; Eukaryota.
DR GeneTree; ENSGT00950000182886; -.
DR HOGENOM; CLU_059260_1_0_1; -.
DR InParanoid; Q3ZCD7; -.
DR OMA; TVFVIEY; -.
DR OrthoDB; 720263at2759; -.
DR TreeFam; TF300908; -.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000012632; Expressed in retina and 106 other tissues.
DR ExpressionAtlas; Q3ZCD7; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0102758; F:very-long-chain enoyl-CoA reductase activity; ISS:UniProtKB.
DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISS:UniProtKB.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039357; SRD5A/TECR.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10556; PTHR10556; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Membrane; NADP; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Sphingolipid metabolism; Steroid biosynthesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..308
FT /note="Very-long-chain enoyl-CoA reductase"
FT /id="PRO_0000317715"
FT TRANSMEM 87..107
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 MOD_RES 22
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZ01"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CY27"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CY27"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 308 AA; 36072 MW; A1DCD120A10B6E5C CRC64;
MKHYEVEILD AKTREKLCFL DKVEPQATIA EIKNLFTKTH PQWYPARQSL RLDPKGKSLK
DEDVLQKLPV GTTATLYFRD LGAQISWVTV FLTEYAGPLF IYLLFYFRVP FIYGRKYDFT
SSRHTVVHLA CICHSFHYIK RLLETLFVHR FSHGTMPLRN IFKNCTYYWG FAAWMAYYIN
HPLYTPPTYG AQQVKLALAI FVICQLGNFS IHMALRDLRP AGSKTRKIPY PTRNPFTWLF
LLVSCPNYTY EVGSWIGFAI MTQCLPVALF SLVGFTQMTI WAKGKHRSYL KEFRDYPPLR
MPIIPFLL
