TECR_HUMAN
ID TECR_HUMAN Reviewed; 308 AA.
AC Q9NZ01; B2RD55; O75350; Q6IBB2; Q9BWK3; Q9Y6P0;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Very-long-chain enoyl-CoA reductase {ECO:0000305};
DE EC=1.3.1.93 {ECO:0000269|PubMed:12482854};
DE AltName: Full=Synaptic glycoprotein SC2;
DE AltName: Full=Trans-2,3-enoyl-CoA reductase;
DE Short=TER;
GN Name=TECR; Synonyms=GPSN2, SC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hair follicle dermal papilla;
RA Seo H.C., Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y.,
RA Hwang S.Y., Im S.U., Jung E.J., Kim J.C.;
RT "A catalog of genes in human dermal papilla cells as identified by
RT expressed sequence tags.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Cervix, Ovary, and Prostate;
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP INTERACTION WITH ELOVL1 AND LASS2.
RX PubMed=20937905; DOI=10.1073/pnas.1005572107;
RA Ohno Y., Suto S., Yamanaka M., Mizutani Y., Mitsutake S., Igarashi Y.,
RA Sassa T., Kihara A.;
RT "ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid
RT synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18439-18444(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25049234; DOI=10.1074/jbc.m114.571869;
RA Wakashima T., Abe K., Kihara A.;
RT "Dual functions of the trans-2-enoyl-CoA reductase TER in the sphingosine
RT 1-phosphate metabolic pathway and in fatty acid elongation.";
RL J. Biol. Chem. 289:24736-24748(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP STRUCTURE BY NMR OF 1-81.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminal ubiquitin-like domain in human
RT synaptic glycoprotein SC2.";
RL Submitted (MAR-2007) to the PDB data bank.
RN [14]
RP VARIANT MRT14 LEU-182.
RX PubMed=21212097; DOI=10.1093/hmg/ddq569;
RA Caliskan M., Chong J.X., Uricchio L., Anderson R., Chen P., Sougnez C.,
RA Garimella K., Gabriel S.B., dePristo M.A., Shakir K., Matern D., Das S.,
RA Waggoner D., Nicolae D.L., Ober C.;
RT "Exome sequencing reveals a novel mutation for autosomal recessive non-
RT syndromic mental retardation in the TECR gene on chromosome 19p13.";
RL Hum. Mol. Genet. 20:1285-1289(2011).
RN [15]
RP CHARACTERIZATION OF VARIANT MRT14 LEU-182, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24220030; DOI=10.1074/jbc.m113.493221;
RA Abe K., Ohno Y., Sassa T., Taguchi R., Caliskan M., Ober C., Kihara A.;
RT "Mutation for nonsyndromic mental retardation in the trans-2-enoyl-CoA
RT reductase TER gene involved in fatty acid elongation impairs the enzyme
RT activity and stability, leading to change in sphingolipid profile.";
RL J. Biol. Chem. 288:36741-36749(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 (PubMed:25049234). Catalyzes the last of the four reactions of
CC the long-chain fatty acids elongation cycle (PubMed:12482854). 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 (PubMed:12482854). This enzyme reduces the trans-2,3-enoyl-
CC CoA fatty acid intermediate to an acyl-CoA that can be further
CC elongated by entering a new cycle of elongation (PubMed:12482854).
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 (PubMed:12482854).
CC Catalyzes the saturation step of the sphingosine 1-phosphate metabolic
CC pathway, the conversion of trans-2-hexadecenoyl-CoA to palmitoyl-CoA
CC (PubMed:25049234). {ECO:0000269|PubMed:12482854,
CC ECO:0000269|PubMed:25049234}.
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:0000269|PubMed:12482854};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14475;
CC Evidence={ECO:0000305|PubMed:12482854};
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:0000269|PubMed:12482854};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39332;
CC Evidence={ECO:0000305|PubMed:12482854};
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:0000269|PubMed:12482854};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39468;
CC Evidence={ECO:0000305|PubMed:12482854};
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:0000269|PubMed:12482854};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39320;
CC Evidence={ECO:0000305|PubMed:12482854};
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:0000269|PubMed:24220030, ECO:0000269|PubMed:25049234};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36144;
CC Evidence={ECO:0000305|PubMed:24220030, ECO:0000305|PubMed:25049234};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:12482854, ECO:0000269|PubMed:24220030,
CC ECO:0000269|PubMed:25049234}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:25049234}.
CC -!- SUBUNIT: Interacts with ELOVL1 and LASS2.
CC {ECO:0000269|PubMed:20937905}.
CC -!- INTERACTION:
CC Q9NZ01; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-2877718, EBI-11343438;
CC Q9NZ01; P11912: CD79A; NbExp=3; IntAct=EBI-2877718, EBI-7797864;
CC Q9NZ01; O00501: CLDN5; NbExp=3; IntAct=EBI-2877718, EBI-18400628;
CC Q9NZ01; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-2877718, EBI-17233035;
CC Q9NZ01; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2877718, EBI-6942903;
CC Q9NZ01; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-2877718, EBI-18535450;
CC Q9NZ01; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2877718, EBI-781551;
CC Q9NZ01; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2877718, EBI-18304435;
CC Q9NZ01; O00258: GET1; NbExp=3; IntAct=EBI-2877718, EBI-18908258;
CC Q9NZ01; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-2877718, EBI-17231387;
CC Q9NZ01; B0YJ81: HACD1; NbExp=3; IntAct=EBI-2877718, EBI-12051643;
CC Q9NZ01; Q6Y1H2: HACD2; NbExp=7; IntAct=EBI-2877718, EBI-530257;
CC Q9NZ01; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-2877718, EBI-10266796;
CC Q9NZ01; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-2877718, EBI-373355;
CC Q9NZ01; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-2877718, EBI-6163737;
CC Q9NZ01; P15941-11: MUC1; NbExp=3; IntAct=EBI-2877718, EBI-17263240;
CC Q9NZ01; O15173: PGRMC2; NbExp=3; IntAct=EBI-2877718, EBI-1050125;
CC Q9NZ01; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-2877718, EBI-10192441;
CC Q9NZ01; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2877718, EBI-18159983;
CC Q9NZ01; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-2877718, EBI-5235586;
CC Q9NZ01; Q86WV6: STING1; NbExp=3; IntAct=EBI-2877718, EBI-2800345;
CC Q9NZ01; P27105: STOM; NbExp=3; IntAct=EBI-2877718, EBI-1211440;
CC Q9NZ01; Q00059: TFAM; NbExp=3; IntAct=EBI-2877718, EBI-1049924;
CC Q9NZ01; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-2877718, EBI-1055364;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12482854, ECO:0000269|PubMed:24220030}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZ01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZ01-2; Sequence=VSP_005957;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues tested. Highly expressed
CC in skeletal muscle. {ECO:0000269|PubMed:12482854}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q64232}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 14
CC (MRT14) [MIM:614020]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:21212097, ECO:0000269|PubMed:24220030}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
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DR EMBL; AF038958; AAC39872.1; -; mRNA.
DR EMBL; AF038959; AAC39873.1; -; mRNA.
DR EMBL; AF222742; AAF32373.1; -; mRNA.
DR EMBL; AK315412; BAG37802.1; -; mRNA.
DR EMBL; BT007179; AAP35843.1; -; mRNA.
DR EMBL; CR456892; CAG33173.1; -; mRNA.
DR EMBL; BC000174; AAH00174.2; -; mRNA.
DR EMBL; BC002425; AAH02425.1; -; mRNA.
DR EMBL; BC005952; AAH05952.1; -; mRNA.
DR EMBL; BC007801; AAH07801.1; -; mRNA.
DR EMBL; BC013881; AAH13881.1; -; mRNA.
DR CCDS; CCDS12313.1; -. [Q9NZ01-1]
DR PIR; T50638; T50638.
DR PIR; T50639; T50639.
DR RefSeq; NP_001308099.1; NM_001321170.1.
DR RefSeq; NP_612510.1; NM_138501.5. [Q9NZ01-1]
DR PDB; 2DZJ; NMR; -; A=1-81.
DR PDBsum; 2DZJ; -.
DR AlphaFoldDB; Q9NZ01; -.
DR BMRB; Q9NZ01; -.
DR SMR; Q9NZ01; -.
DR BioGRID; 114900; 221.
DR IntAct; Q9NZ01; 108.
DR MINT; Q9NZ01; -.
DR STRING; 9606.ENSP00000215567; -.
DR SwissLipids; SLP:000000436; -.
DR GlyGen; Q9NZ01; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NZ01; -.
DR PhosphoSitePlus; Q9NZ01; -.
DR SwissPalm; Q9NZ01; -.
DR BioMuta; TECR; -.
DR DMDM; 20177939; -.
DR EPD; Q9NZ01; -.
DR jPOST; Q9NZ01; -.
DR MassIVE; Q9NZ01; -.
DR MaxQB; Q9NZ01; -.
DR PaxDb; Q9NZ01; -.
DR PeptideAtlas; Q9NZ01; -.
DR PRIDE; Q9NZ01; -.
DR ProteomicsDB; 83310; -. [Q9NZ01-1]
DR ProteomicsDB; 83311; -. [Q9NZ01-2]
DR Antibodypedia; 26742; 141 antibodies from 23 providers.
DR DNASU; 9524; -.
DR Ensembl; ENST00000215567.10; ENSP00000215567.4; ENSG00000099797.15. [Q9NZ01-1]
DR GeneID; 9524; -.
DR KEGG; hsa:9524; -.
DR MANE-Select; ENST00000215567.10; ENSP00000215567.4; NM_138501.6; NP_612510.1.
DR UCSC; uc002mza.4; human. [Q9NZ01-1]
DR CTD; 9524; -.
DR DisGeNET; 9524; -.
DR GeneCards; TECR; -.
DR HGNC; HGNC:4551; TECR.
DR HPA; ENSG00000099797; Low tissue specificity.
DR MalaCards; TECR; -.
DR MIM; 610057; gene.
DR MIM; 614020; phenotype.
DR neXtProt; NX_Q9NZ01; -.
DR OpenTargets; ENSG00000099797; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA28946; -.
DR VEuPathDB; HostDB:ENSG00000099797; -.
DR eggNOG; KOG1639; Eukaryota.
DR GeneTree; ENSGT00950000182886; -.
DR HOGENOM; CLU_059260_1_0_1; -.
DR InParanoid; Q9NZ01; -.
DR OMA; TVFVIEY; -.
DR OrthoDB; 720263at2759; -.
DR PhylomeDB; Q9NZ01; -.
DR TreeFam; TF300908; -.
DR BioCyc; MetaCyc:ENSG00000099797-MON; -.
DR BRENDA; 1.3.1.93; 2681.
DR PathwayCommons; Q9NZ01; -.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SignaLink; Q9NZ01; -.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 9524; 70 hits in 1076 CRISPR screens.
DR ChiTaRS; TECR; human.
DR EvolutionaryTrace; Q9NZ01; -.
DR GeneWiki; TECR; -.
DR GenomeRNAi; 9524; -.
DR Pharos; Q9NZ01; Tbio.
DR PRO; PR:Q9NZ01; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NZ01; protein.
DR Bgee; ENSG00000099797; Expressed in lower esophagus mucosa and 124 other tissues.
DR ExpressionAtlas; Q9NZ01; baseline and differential.
DR Genevisible; Q9NZ01; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0102758; F:very-long-chain enoyl-CoA reductase activity; IMP:UniProtKB.
DR GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; TAS:Reactome.
DR GO; GO:0030497; P:fatty acid elongation; IDA:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR GO; GO:0006665; P:sphingolipid metabolic process; IMP:UniProtKB.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IDA: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 3D-structure; Acetylation; Alternative splicing; Disease variant;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Glycoprotein; Intellectual disability; Lipid biosynthesis;
KW Lipid metabolism; Membrane; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..308
FT /note="Very-long-chain enoyl-CoA reductase"
FT /id="PRO_0000213683"
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:0007744|PubMed:19608861"
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"
FT VAR_SEQ 20..170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9653160"
FT /id="VSP_005957"
FT VARIANT 182
FT /note="P -> L (in MRT14; reduced enzyme activity; reduced
FT protein stability; no effect on subcellular localization;
FT dbSNP:rs199469705)"
FT /evidence="ECO:0000269|PubMed:21212097,
FT ECO:0000269|PubMed:24220030"
FT /id="VAR_065918"
FT CONFLICT 72..75
FT /note="TTAT -> PRAH (in Ref. 1; AAC39872)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="Y -> C (in Ref. 1; AAC39872/AAC39873)"
FT /evidence="ECO:0000305"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:2DZJ"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:2DZJ"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:2DZJ"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2DZJ"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:2DZJ"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2DZJ"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2DZJ"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:2DZJ"
SQ SEQUENCE 308 AA; 36034 MW; 120AD0883820784D CRC64;
MKHYEVEILD AKTREKLCFL DKVEPHATIA EIKNLFTKTH PQWYPARQSL RLDPKGKSLK
DEDVLQKLPV GTTATLYFRD LGAQISWVTV FLTEYAGPLF IYLLFYFRVP FIYGHKYDFT
SSRHTVVHLA CICHSFHYIK RLLETLFVHR FSHGTMPLRN IFKNCTYYWG FAAWMAYYIN
HPLYTPPTYG AQQVKLALAI FVICQLGNFS IHMALRDLRP AGSKTRKIPY PTKNPFTWLF
LLVSCPNYTY EVGSWIGFAI MTQCLPVALF SLVGFTQMTI WAKGKHRSYL KEFRDYPPLR
MPIIPFLL
