TECR_RAT
ID TECR_RAT Reviewed; 308 AA.
AC Q64232;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1404491; DOI=10.1002/jnr.490320205;
RA Johnston I.G., Rush S.J., Gurd J.W., Brown I.R.;
RT "Molecular cloning of a novel mRNA using an antibody directed against
RT synaptic glycoproteins.";
RL J. Neurosci. Res. 32:159-166(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Expressed at high levels in brain and is also found
CC at lower levels in several other tissues. {ECO:0000269|PubMed:1404491}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:1404491}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
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DR EMBL; S45663; AAB23534.1; -; mRNA.
DR EMBL; BC059115; AAH59115.1; -; mRNA.
DR RefSeq; NP_612558.1; NM_138549.1.
DR AlphaFoldDB; Q64232; -.
DR SMR; Q64232; -.
DR BioGRID; 251323; 2.
DR IntAct; Q64232; 3.
DR STRING; 10116.ENSRNOP00000035416; -.
DR GlyGen; Q64232; 2 sites.
DR iPTMnet; Q64232; -.
DR PhosphoSitePlus; Q64232; -.
DR jPOST; Q64232; -.
DR PaxDb; Q64232; -.
DR PRIDE; Q64232; -.
DR Ensembl; ENSRNOT00000037608; ENSRNOP00000035416; ENSRNOG00000021808.
DR GeneID; 191576; -.
DR KEGG; rno:191576; -.
DR CTD; 9524; -.
DR RGD; 620376; Tecr.
DR eggNOG; KOG1639; Eukaryota.
DR GeneTree; ENSGT00950000182886; -.
DR HOGENOM; CLU_059260_1_0_1; -.
DR InParanoid; Q64232; -.
DR OMA; TVFVIEY; -.
DR OrthoDB; 720263at2759; -.
DR PhylomeDB; Q64232; -.
DR TreeFam; TF300908; -.
DR BRENDA; 1.3.1.93; 5301.
DR Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q64232; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000021808; Expressed in cerebellum and 19 other tissues.
DR ExpressionAtlas; Q64232; baseline and differential.
DR Genevisible; Q64232; RN.
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 1: Evidence at protein 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_0000213685"
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:0007744|PubMed:22673903"
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; 36123 MW; 9E1B6280F61DD463 CRC64;
MKHYEVEIRD AKTREKLCFL DKVEPQATIS EIKTLFTKTH PQWYPARQSL RLDPKGKSLK
DEDVLQKLPV GTTATLYFRD LGAQISWVTV FLTEYAGPLF IYLLFYFRVP FIYGRKYDFT
SSRHTVVHLA CMCHSFHYIK RLLETLFVHR FSHGTMPLRN IFKNCTYYWG FAAWMAYYIN
HPLYTPPTYG VQQVKLALAI FVICQLGNFS IHMALRDLRP AGSKTRKIPY PTKNPFTWLF
LLVSCPNYTY EVGSWIGFAI MTQCVPVALF SLVGFTQMTI WAKGKHRSYL KEFRDYPPLR
MPIIPFLL
