TECR_ARATH
ID TECR_ARATH Reviewed; 310 AA.
AC Q9M2U2;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Very-long-chain enoyl-CoA reductase {ECO:0000305};
DE EC=1.3.1.93 {ECO:0000305|PubMed:14673020, ECO:0000305|PubMed:15829606};
DE AltName: Full=Enoyl-CoA reductase;
DE Short=AtECR;
DE AltName: Full=Protein ECERIFERUM 10;
DE AltName: Full=Synaptic glycoprotein SC2-like protein;
GN Name=ECR; Synonyms=AtTSC13, CER10; OrderedLocusNames=At3g55360;
GN ORFNames=T22E16.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=11113186; DOI=10.1128/mcb.21.1.109-125.2001;
RA Kohlwein S.D., Eder S., Oh C.-S., Martin C.E., Gable K., Bacikova D.,
RA Dunn T.M.;
RT "Tsc13p is required for fatty acid elongation and localizes to a novel
RT structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 21:109-125(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=14673020; DOI=10.1093/jxb/erh061;
RA Gable K., Garton S., Napier J.A., Dunn T.M.;
RT "Functional characterization of the Arabidopsis thaliana orthologue of
RT Tsc13p, the enoyl reductase of the yeast microsomal fatty acid elongating
RT system.";
RL J. Exp. Bot. 55:543-545(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15829606; DOI=10.1105/tpc.104.030155;
RA Zheng H., Rowland O., Kunst L.;
RT "Disruptions of the Arabidopsis Enoyl-CoA reductase gene reveal an
RT essential role for very-long-chain fatty acid synthesis in cell expansion
RT during plant morphogenesis.";
RL Plant Cell 17:1467-1481(2005).
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. Required for the
CC elongation of fatty acids precursors of sphingolipids, storage lipids
CC and cuticular waxes. {ECO:0000269|PubMed:14673020,
CC ECO:0000269|PubMed:15829606}.
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:0000305|PubMed:14673020, ECO:0000305|PubMed:15829606};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000305|PubMed:14673020, ECO:0000305|PubMed:15829606}.
CC -!- SUBUNIT: Part of the fatty acid elongase complex which contains a beta-
CC ketoacyl-CoA synthase (KCS), a beta-ketoacyl-CoA reductase (KCR), a
CC beta-hydroxyacyl-CoA dehydratase (HCD) and an enoyl-CoA reductase
CC (ECR). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15829606}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15829606}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. Detected in mature seeds. {ECO:0000269|PubMed:14673020}.
CC -!- DISRUPTION PHENOTYPE: Abnormal organ morphology and stem glossiness.
CC {ECO:0000269|PubMed:15829606}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
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DR EMBL; AL132975; CAB75894.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79372.1; -; Genomic_DNA.
DR EMBL; AY065136; AAL38312.1; -; mRNA.
DR EMBL; AY081583; AAM10145.1; -; mRNA.
DR EMBL; AY088452; AAM65988.1; -; mRNA.
DR PIR; T47675; T47675.
DR RefSeq; NP_191096.1; NM_115394.4.
DR AlphaFoldDB; Q9M2U2; -.
DR SMR; Q9M2U2; -.
DR BioGRID; 10018; 12.
DR IntAct; Q9M2U2; 2.
DR STRING; 3702.AT3G55360.1; -.
DR iPTMnet; Q9M2U2; -.
DR SwissPalm; Q9M2U2; -.
DR PaxDb; Q9M2U2; -.
DR PRIDE; Q9M2U2; -.
DR ProteomicsDB; 234211; -.
DR EnsemblPlants; AT3G55360.1; AT3G55360.1; AT3G55360.
DR GeneID; 824702; -.
DR Gramene; AT3G55360.1; AT3G55360.1; AT3G55360.
DR KEGG; ath:AT3G55360; -.
DR Araport; AT3G55360; -.
DR TAIR; locus:2099911; AT3G55360.
DR eggNOG; KOG1639; Eukaryota.
DR HOGENOM; CLU_059260_2_0_1; -.
DR InParanoid; Q9M2U2; -.
DR OMA; TVFVIEY; -.
DR OrthoDB; 720263at2759; -.
DR PhylomeDB; Q9M2U2; -.
DR BioCyc; ARA:AT3G55360-MON; -.
DR BioCyc; MetaCyc:AT3G55360-MON; -.
DR BRENDA; 1.3.1.93; 399.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9M2U2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2U2; baseline and differential.
DR Genevisible; Q9M2U2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0009923; C:fatty acid elongase complex; TAS:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009922; F:fatty acid elongase activity; IMP:TAIR.
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:0042335; P:cuticle development; IMP:TAIR.
DR GO; GO:0006665; P:sphingolipid metabolic process; IMP:TAIR.
DR GO; GO:0010091; P:trichome branching; IMP:TAIR.
DR GO; GO:1905499; P:trichome papilla formation; IMP:TAIR.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0010025; P:wax biosynthetic process; IMP:TAIR.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039357; SRD5A/TECR.
DR PANTHER; PTHR10556; PTHR10556; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 1: Evidence at protein level;
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..310
FT /note="Very-long-chain enoyl-CoA reductase"
FT /id="PRO_0000420423"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 310 AA; 35724 MW; 5B1A7D6A021605ED CRC64;
MKVTVVSRSG REVLKAPLDL PDSATVADLQ EAFHKRAKKF YPSRQRLTLP VTPGSKDKPV
VLNSKKSLKE YCDGNNNSLT VVFKDLGAQV SYRTLFFFEY LGPLLIYPVF YYFPVYKFLG
YGEDCVIHPV QTYAMYYWCF HYFKRILETF FVHRFSHATS PIGNVFRNCA YYWSFGAYIA
YYVNHPLYTP VSDLQMKIGF GFGLVCQVAN FYCHILLKNL RDPSGAGGYQ IPRGFLFNIV
TCANYTTEIY QWLGFNIATQ TIAGYVFLAV AALIMTNWAL GKHSRLRKIF DGKDGKPKYP
RRWVILPPFL
