DECR2_HUMAN
ID DECR2_HUMAN Reviewed; 292 AA.
AC Q9NUI1; Q6ZRS7; Q96ET0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing];
DE Short=pDCR;
DE EC=1.3.1.124 {ECO:0000269|PubMed:11514237, ECO:0000269|PubMed:22745130};
DE AltName: Full=2,4-dienoyl-CoA reductase 2;
DE AltName: Full=Short chain dehydrogenase/reductase family 17C member 1;
GN Name=DECR2; Synonyms=PDCR, SDR17C1;
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 [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=11514237; DOI=10.1016/s1388-1981(01)00141-x;
RA De Nys K., Meyhi E., Mannaerts G.P., Fransen M., Van Veldhoven P.P.;
RT "Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase.";
RL Biochim. Biophys. Acta 1533:66-72(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Lung;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-151 AND LYS-291, AND
RP IDENTIFICATION BY MASS 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 2-278 IN COMPLEX WITH HEXADIENOYL
RP COA AND NADP, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP MUTAGENESIS OF ASP-86; ASP-137; ASP-186 AND ASP-268, AND FUNCTION.
RX PubMed=22745130; DOI=10.1074/jbc.m112.385351;
RA Hua T., Wu D., Ding W., Wang J., Shaw N., Liu Z.J.;
RT "Studies of human 2,4-dienoyl CoA reductase shed new light on peroxisomal
RT beta-oxidation of unsaturated fatty acids.";
RL J. Biol. Chem. 287:28956-28965(2012).
CC -!- FUNCTION: Auxiliary enzyme of beta-oxidation. Participates in the
CC degradation of unsaturated fatty enoyl-CoA esters having double bonds
CC in both even- and odd-numbered positions in peroxisome. Catalyzes the
CC NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
CC Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also
CC towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA, suggesting that it does
CC not constitute a rate limiting step in the peroxisomal degradation of
CC docosahexaenoic acid. {ECO:0000269|PubMed:11514237,
CC ECO:0000269|PubMed:22745130}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)-
CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:61892, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85099,
CC ChEBI:CHEBI:85493; EC=1.3.1.124;
CC Evidence={ECO:0000269|PubMed:11514237, ECO:0000269|PubMed:22745130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E,4E)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)-
CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:45912, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85101,
CC ChEBI:CHEBI:85493; EC=1.3.1.124;
CC Evidence={ECO:0000269|PubMed:11514237, ECO:0000269|PubMed:22745130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,4Z,7Z,10Z,13Z,16Z,19Z)-docosaheptaenoyl-CoA + H(+) + NADPH
CC = (3E,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:44920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77559, ChEBI:CHEBI:84791;
CC Evidence={ECO:0000269|PubMed:11514237};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=59 uM for 2,4-hexadienoyl-CoA {ECO:0000269|PubMed:11514237};
CC KM=6 uM for 2,4-decadienoyl-CoA {ECO:0000269|PubMed:11514237};
CC KM=102 uM for 2,4,7,10,13,16,19-docosaheptaenoyl-CoA
CC {ECO:0000269|PubMed:11514237};
CC KM=71.6 uM for 2,4-hexadienoyl CoA {ECO:0000269|PubMed:22745130};
CC KM=2.4 uM for 2,4-decadienoyl CoA {ECO:0000269|PubMed:22745130};
CC Vmax=1.75 umol/min/mg enzyme toward 2,4-hexadienoyl CoA
CC {ECO:0000269|PubMed:22745130};
CC Vmax=1.37 umol/min/mg enzyme toward 2,4-decadienoyl CoA
CC {ECO:0000269|PubMed:22745130};
CC -!- SUBUNIT: Monomer, dimer and oligomer. {ECO:0000269|PubMed:22745130}.
CC -!- INTERACTION:
CC Q9NUI1; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-3937367, EBI-725606;
CC Q9NUI1; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-3937367, EBI-9057006;
CC Q9NUI1; P51784: USP11; NbExp=3; IntAct=EBI-3937367, EBI-306876;
CC Q9NUI1; O14972: VPS26C; NbExp=3; IntAct=EBI-3937367, EBI-7207091;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q9Z2M4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NUI1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NUI1-2; Sequence=VSP_013630, VSP_013631, VSP_013632;
CC Name=3;
CC IsoId=Q9NUI1-3; Sequence=VSP_013629;
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. 2,4-dienoyl-CoA reductase subfamily. {ECO:0000305}.
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DR EMBL; AJ293009; CAC05664.1; -; mRNA.
DR EMBL; AE006463; AAK61231.1; -; Genomic_DNA.
DR EMBL; AK128012; BAC87232.1; -; mRNA.
DR EMBL; AL023881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010740; AAH10740.1; -; mRNA.
DR EMBL; BC011968; AAH11968.1; -; mRNA.
DR CCDS; CCDS10409.1; -. [Q9NUI1-1]
DR RefSeq; NP_065715.1; NM_020664.3. [Q9NUI1-1]
DR PDB; 4FC6; X-ray; 2.10 A; A/B/C/D=2-278.
DR PDB; 4FC7; X-ray; 1.84 A; A/B/C/D=2-278.
DR PDBsum; 4FC6; -.
DR PDBsum; 4FC7; -.
DR AlphaFoldDB; Q9NUI1; -.
DR SMR; Q9NUI1; -.
DR BioGRID; 117525; 58.
DR IntAct; Q9NUI1; 20.
DR STRING; 9606.ENSP00000219481; -.
DR SwissLipids; SLP:000001050; -.
DR GlyGen; Q9NUI1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NUI1; -.
DR MetOSite; Q9NUI1; -.
DR PhosphoSitePlus; Q9NUI1; -.
DR BioMuta; DECR2; -.
DR DMDM; 84029527; -.
DR EPD; Q9NUI1; -.
DR jPOST; Q9NUI1; -.
DR MassIVE; Q9NUI1; -.
DR MaxQB; Q9NUI1; -.
DR PaxDb; Q9NUI1; -.
DR PeptideAtlas; Q9NUI1; -.
DR PRIDE; Q9NUI1; -.
DR ProteomicsDB; 82673; -. [Q9NUI1-1]
DR ProteomicsDB; 82674; -. [Q9NUI1-2]
DR ProteomicsDB; 82675; -. [Q9NUI1-3]
DR Antibodypedia; 34897; 152 antibodies from 27 providers.
DR DNASU; 26063; -.
DR Ensembl; ENST00000219481.10; ENSP00000219481.5; ENSG00000242612.7. [Q9NUI1-1]
DR Ensembl; ENST00000439661.5; ENSP00000399697.1; ENSG00000242612.7. [Q9NUI1-2]
DR Ensembl; ENST00000613476.3; ENSP00000481547.1; ENSG00000274296.3. [Q9NUI1-1]
DR Ensembl; ENST00000631856.1; ENSP00000488824.1; ENSG00000274296.3. [Q9NUI1-2]
DR GeneID; 26063; -.
DR KEGG; hsa:26063; -.
DR MANE-Select; ENST00000219481.10; ENSP00000219481.5; NM_020664.4; NP_065715.1.
DR UCSC; uc002chb.4; human. [Q9NUI1-1]
DR CTD; 26063; -.
DR GeneCards; DECR2; -.
DR HGNC; HGNC:2754; DECR2.
DR HPA; ENSG00000242612; Tissue enriched (liver).
DR MIM; 615839; gene.
DR neXtProt; NX_Q9NUI1; -.
DR OpenTargets; ENSG00000242612; -.
DR PharmGKB; PA27235; -.
DR VEuPathDB; HostDB:ENSG00000242612; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000153801; -.
DR HOGENOM; CLU_1309747_0_0_1; -.
DR InParanoid; Q9NUI1; -.
DR OMA; GSICSAQ; -.
DR OrthoDB; 1105725at2759; -.
DR PhylomeDB; Q9NUI1; -.
DR TreeFam; TF315256; -.
DR BRENDA; 1.3.1.124; 2681.
DR BRENDA; 1.3.1.34; 2681.
DR PathwayCommons; Q9NUI1; -.
DR Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SABIO-RK; Q9NUI1; -.
DR SignaLink; Q9NUI1; -.
DR BioGRID-ORCS; 26063; 19 hits in 1079 CRISPR screens.
DR ChiTaRS; DECR2; human.
DR GeneWiki; DECR2; -.
DR GenomeRNAi; 26063; -.
DR Pharos; Q9NUI1; Tbio.
DR PRO; PR:Q9NUI1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NUI1; protein.
DR Bgee; ENSG00000242612; Expressed in right lobe of liver and 93 other tissues.
DR ExpressionAtlas; Q9NUI1; baseline and differential.
DR Genevisible; Q9NUI1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005778; C:peroxisomal membrane; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR045017; DECR2-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43296; PTHR43296; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Fatty acid metabolism;
KW Lipid metabolism; NADP; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..292
FT /note="Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-
FT CoA-producing]"
FT /id="PRO_0000054559"
FT MOTIF 290..292
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250"
FT BINDING 35..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:22745130"
FT BINDING 60..64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:22745130"
FT BINDING 60
FT /ligand="substrate"
FT BINDING 86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:22745130"
FT BINDING 88
FT /ligand="substrate"
FT BINDING 118
FT /ligand="substrate"
FT BINDING 126..128
FT /ligand="substrate"
FT BINDING 182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:22745130"
FT BINDING 208..214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:22745130"
FT BINDING 219
FT /ligand="substrate"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 151
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013629"
FT VAR_SEQ 50
FT /note="R -> RASEDQMGHCSSSGTCLAGVATFMVIVGKQPPNQKSRETKEQGRQIP
FT FVCVR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013630"
FT VAR_SEQ 114..160
FT /note="AAGNFLCPAGALSFNAFKTVMDIDTSGTFNVSRVLYEKFFRDHGGVI -> S
FT SSSCGLPFCRCGRELPVPRWRLVLQRLQDRDGHRYQRHLQCVSCAL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013631"
FT VAR_SEQ 161..292
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013632"
FT MUTAGEN 86
FT /note="D->A: Reduces enzyme activity by 98%."
FT /evidence="ECO:0000269|PubMed:22745130"
FT MUTAGEN 137
FT /note="D->A: Reduces enzyme activity by 97%."
FT /evidence="ECO:0000269|PubMed:22745130"
FT MUTAGEN 186
FT /note="D->A: Reduces enzyme activity by about 95%."
FT /evidence="ECO:0000269|PubMed:22745130"
FT MUTAGEN 268
FT /note="D->A: Reduces enzyme activity by 97%."
FT /evidence="ECO:0000269|PubMed:22745130"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:4FC7"
FT TURN 23..28
FT /evidence="ECO:0007829|PDB:4FC7"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:4FC7"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:4FC7"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:4FC7"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 62..76
FT /evidence="ECO:0007829|PDB:4FC7"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 90..104
FT /evidence="ECO:0007829|PDB:4FC7"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:4FC7"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 176..196
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:4FC7"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:4FC7"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:4FC7"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:4FC7"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:4FC7"
SQ SEQUENCE 292 AA; 30778 MW; 9E7CD2995CE598D6 CRC64;
MAQPPPDVEG DDCLPAYRHL FCPDLLRDKV AFITGGGSGI GFRIAEIFMR HGCHTVIASR
SLPRVLTAAR KLAGATGRRC LPLSMDVRAP PAVMAAVDQA LKEFGRIDIL INCAAGNFLC
PAGALSFNAF KTVMDIDTSG TFNVSRVLYE KFFRDHGGVI VNITATLGNR GQALQVHAGS
AKAAVDAMTR HLAVEWGPQN IRVNSLAPGP ISGTEGLRRL GGPQASLSTK VTASPLQRLG
NKTEIAHSVL YLASPLASYV TGAVLVADGG AWLTFPNGVK GLPDFASFSA KL
