TECR_MOUSE
ID TECR_MOUSE Reviewed; 308 AA.
AC Q9CY27;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 CATALYTIC ACTIVITY.
RX PubMed=12482854; DOI=10.1074/jbc.m211684200;
RA Moon Y.-A., Horton J.D.;
RT "Identification of two mammalian reductases involved in the two-carbon
RT fatty acyl elongation cascade.";
RL J. Biol. Chem. 278:7335-7343(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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:0000269|PubMed:12482854};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35353;
CC Evidence={ECO:0000305|PubMed:12482854};
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; AK010984; BAB27305.1; -; mRNA.
DR EMBL; BC019984; AAH19984.1; -; mRNA.
DR CCDS; CCDS40403.1; -.
DR RefSeq; NP_081455.1; NM_027179.1.
DR RefSeq; NP_598879.1; NM_134118.5.
DR AlphaFoldDB; Q9CY27; -.
DR SMR; Q9CY27; -.
DR BioGRID; 223073; 12.
DR IntAct; Q9CY27; 2.
DR MINT; Q9CY27; -.
DR SwissLipids; SLP:000000437; -.
DR GlyGen; Q9CY27; 2 sites.
DR iPTMnet; Q9CY27; -.
DR PhosphoSitePlus; Q9CY27; -.
DR SwissPalm; Q9CY27; -.
DR EPD; Q9CY27; -.
DR jPOST; Q9CY27; -.
DR MaxQB; Q9CY27; -.
DR PaxDb; Q9CY27; -.
DR PeptideAtlas; Q9CY27; -.
DR PRIDE; Q9CY27; -.
DR ProteomicsDB; 263153; -.
DR Antibodypedia; 26742; 141 antibodies from 23 providers.
DR DNASU; 106529; -.
DR Ensembl; ENSMUST00000019382; ENSMUSP00000019382; ENSMUSG00000031708.
DR GeneID; 106529; -.
DR KEGG; mmu:106529; -.
DR UCSC; uc009mkl.2; mouse.
DR CTD; 9524; -.
DR MGI; MGI:1915408; Tecr.
DR VEuPathDB; HostDB:ENSMUSG00000031708; -.
DR GeneTree; ENSGT00950000182886; -.
DR HOGENOM; CLU_059260_1_0_1; -.
DR InParanoid; Q9CY27; -.
DR OMA; TVFVIEY; -.
DR OrthoDB; 720263at2759; -.
DR PhylomeDB; Q9CY27; -.
DR BRENDA; 1.3.1.38; 3474.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 106529; 22 hits in 76 CRISPR screens.
DR ChiTaRS; Tecr; mouse.
DR PRO; PR:Q9CY27; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9CY27; protein.
DR Bgee; ENSMUSG00000031708; Expressed in central gray substance of midbrain and 264 other tissues.
DR ExpressionAtlas; Q9CY27; baseline and differential.
DR Genevisible; Q9CY27; MM.
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_0000213684"
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:17208939"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
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; 36090 MW; 0576C2813F2C5E4A CRC64;
MKHYEVEIRD AKTREKLCFL DKVEPQATIS EIKTLFTKTH PQWYPARQSL RLDPKGKSLK
DEDVLQKLPV GTTATLYFRD LGAQISWVTV FLTEYAGPLF IYLLFYFRVP FIYGRKYDFT
SSRHTVVHLA CMCHSFHYIK RLLETLFVHR FSHGTMPLRN IFKNCTYYWG FAAWMAYYIN
HPLYTPPTYG VQQVKLALAV FVICQLGNFS IHMALRDLRP AGSKTRKIPY PTKNPFTWLF
LLVSCPNYTY EVGSWIGFAI LTQCVPVALF SLVGFTQMTI WAKGKHRSYL KEFRDYPPLR
MPIIPFLL
