ID   ANM1_RAT                Reviewed;         353 AA.
AC   Q63009;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Protein arginine N-methyltransferase 1 {ECO:0000305};
DE            EC=2.1.1.319 {ECO:0000269|PubMed:19405910};
DE   AltName: Full=Histone-arginine N-methyltransferase PRMT1;
GN   Name=Prmt1 {ECO:0000312|RGD:62020}; Synonyms=Hrmt1l2;
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], AND INTERACTION WITH BTG1; BTG2 AND IFNAR1.
RX   PubMed=8663146; DOI=10.1074/jbc.271.25.15034;
RA   Lin W.-J., Gary J.D., Yang M.C., Clarke S., Herschman H.R.;
RT   "The mammalian immediate-early TIS21 protein and the leukemia-associated
RT   BTG1 protein interact with a protein-arginine N-methyltransferase.";
RL   J. Biol. Chem. 271:15034-15044(1996).
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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15837430; DOI=10.1016/j.bbagen.2005.02.015;
RA   Lim Y., Kwon Y.H., Won N.H., Min B.H., Park I.S., Paik W.K., Kim S.;
RT   "Multimerization of expressed protein-arginine methyltransferases during
RT   the growth and differentiation of rat liver.";
RL   Biochim. Biophys. Acta 1723:240-247(2005).
RN   [4]
RP   FUNCTION.
RX   PubMed=18492485; DOI=10.1016/j.bbrc.2008.05.051;
RA   Iwasaki H.;
RT   "Involvement of PRMT1 in hnRNPQ activation and internalization of insulin
RT   receptor.";
RL   Biochem. Biophys. Res. Commun. 372:314-319(2008).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19405910; DOI=10.1042/bj20090268;
RA   Lakowski T.M., Frankel A.;
RT   "Kinetic analysis of human protein arginine N-methyltransferase 2:
RT   formation of monomethyl- and asymmetric dimethyl-arginine residues on
RT   histone H4.";
RL   Biochem. J. 421:253-261(2009).
RN   [6]
RP   FUNCTION, INTERACTION WITH MAP3K5, AND MUTAGENESIS OF GLY-80.
RX   PubMed=22095282; DOI=10.1038/cdd.2011.168;
RA   Cho J.H., Lee M.K., Yoon K.W., Lee J., Cho S.G., Choi E.J.;
RT   "Arginine methylation-dependent regulation of ASK1 signaling by PRMT1.";
RL   Cell Death Differ. 19:859-870(2012).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH
RP   S-ADENOSYL-L-HOMOCYSTEINE AND PEPTIDE SUBSTRATE, SUBUNIT, FUNCTION, ACTIVE
RP   SITE, AND MUTAGENESIS OF GLU-144 AND GLU-153.
RX   PubMed=12737817; DOI=10.1016/s0969-2126(03)00071-6;
RA   Zhang X., Cheng X.;
RT   "Structure of the predominant protein arginine methyltransferase PRMT1 and
RT   analysis of its binding to substrate peptides.";
RL   Structure 11:509-520(2003).
CC   -!- FUNCTION: Arginine methyltransferase that methylates (mono and
CC       asymmetric dimethylation) the guanidino nitrogens of arginyl residues
CC       present in proteins such as ESR1, histone H2, H3 and H4, FMR1, ILF3,
CC       HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15,
CC       FOXO1, CHTOP and MAP3K5/ASK1 (PubMed:12737817, PubMed:15837430,
CC       PubMed:18492485, PubMed:22095282, PubMed:19405910). Constitutes the
CC       main enzyme that mediates monomethylation and asymmetric dimethylation
CC       of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific
CC       tag for epigenetic transcriptional activation (By similarity). May be
CC       involved in the regulation of TAF15 transcriptional activity, act as an
CC       activator of estrogen receptor (ER)-mediated transactivation, play a
CC       key role in neurite outgrowth and act as a negative regulator of
CC       megakaryocytic differentiation, by modulating p38 MAPK pathway (By
CC       similarity). Methylates RBM15, promoting ubiquitination and degradation
CC       of RBM15 (By similarity). Methylates FOXO1 and retains it in the
CC       nucleus increasing its transcriptional activity (By similarity).
CC       Methylates CHTOP and this methylation is critical for its 5-
CC       hydroxymethylcytosine (5hmC)-binding activity (By similarity).
CC       Methylates MAP3K5/ASK1 at 'Arg-85' and 'Arg-87' which promotes
CC       association of MAP3K5 with thioredoxin and negatively regulates MAP3K5
CC       association with TRAF2, inhibiting MAP3K5 stimulation and MAP3K5-
CC       induced activation of JNK (PubMed:22095282). Methylates H4R3 in genes
CC       involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent
CC       manner (By similarity). Plays a role in regulating alternative splicing
CC       in the heart (By similarity). Methylates NPRL2 at 'Arg-78' leading to
CC       inhibition of its GTPase activator activity and then the GATOR1 complex
CC       and consequently inducing timely mTORC1 activation under methionine-
CC       sufficient conditions (By similarity). {ECO:0000250|UniProtKB:Q99873,
CC       ECO:0000250|UniProtKB:Q9JIF0, ECO:0000269|PubMed:12737817,
CC       ECO:0000269|PubMed:15837430, ECO:0000269|PubMed:18492485,
CC       ECO:0000269|PubMed:19405910, ECO:0000269|PubMed:22095282}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC         COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC         Evidence={ECO:0000269|PubMed:19405910};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097;
CC         Evidence={ECO:0000305|PubMed:19405910};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC         N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:48100, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11990,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:65280;
CC         Evidence={ECO:0000269|PubMed:19405910};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48101;
CC         Evidence={ECO:0000305|PubMed:19405910};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-methionine
CC         = H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + S-adenosyl-
CC         L-homocysteine; Xref=Rhea:RHEA:48104, Rhea:RHEA-COMP:11990,
CC         Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61897, ChEBI:CHEBI:65280;
CC         Evidence={ECO:0000269|PubMed:19405910};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48105;
CC         Evidence={ECO:0000305|PubMed:19405910};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1 uM for AdoMet {ECO:0000269|PubMed:19405910};
CC         KM=4.2 uM for histone H4 {ECO:0000269|PubMed:19405910};
CC         Vmax=1.2 nmol/min/mg enzyme toward AdoMet
CC         {ECO:0000269|PubMed:19405910};
CC         Vmax=1.24 nmol/min/mg enzyme toward histone H4
CC         {ECO:0000269|PubMed:19405910};
CC   -!- SUBUNIT: Homodimer and heterodimer with PRMT8. Homooctamer; individual
CC       homodimers associates to form a homooctamer. Interacts with NFATC2IP.
CC       Interacts with ILF3 and SUPT5H. Individual homodimers can associate to
CC       form a homohexamer. Interacts with FOXO1; the interaction methylates
CC       FOXO1, retaining it in the nucleus and increasing its transcriptional
CC       activity. Methylation of FOXO1 is increased with oxidative stress.
CC       Interacts with CHTOP; the interaction methylates CHTOP, enabling its
CC       interaction with the 5FMC complex (By similarity). Interacts with BTG1,
CC       BTG2 and IFNAR1. Interacts with and probably methylates ATXN2L (By
CC       similarity). Component of the methylosome, a 20S complex containing at
CC       least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50, PRMT1 and ERH (By
CC       similarity). Interacts with DHX9 (via RGG region) (By similarity).
CC       Interacts (via N-terminus) with HABP4 (By similarity). Interacts with
CC       MAP3K5/ASK1; the interaction results in MAP3K5 methylation by PRMT1
CC       which inhibits MAP3K5 activation (PubMed:22095282). Interacts with
CC       TRIM48; the interaction results in ubiquitination of PRMT1 by TRIM48,
CC       leading to PRMT1 proteasomal degradation and activation of MAP3K5 (By
CC       similarity). Interacts with GATOR1 complex; this interaction is S-
CC       adenosyl-L-methionine (SAM) dependent and is perturbated by BMT2/SAMTOR
CC       in a SAM-sensitive manner (By similarity).
CC       {ECO:0000250|UniProtKB:Q99873, ECO:0000269|PubMed:12737817,
CC       ECO:0000269|PubMed:22095282, ECO:0000269|PubMed:8663146}.
CC   -!- INTERACTION:
CC       Q63009; Q9JIL3: Ilf3; NbExp=2; IntAct=EBI-78708, EBI-78714;
CC       Q63009; Q63009: Prmt1; NbExp=2; IntAct=EBI-78708, EBI-78708;
CC       Q63009; P62633: CNBP; Xeno; NbExp=2; IntAct=EBI-78708, EBI-1047529;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9JIF0}. Nucleus,
CC       nucleoplasm {ECO:0000250|UniProtKB:Q9JIF0}. Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:15837430}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q99873}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:Q99873}. Note=Mostly found in the cytoplasm.
CC       Colocalizes with CHTOP within the nucleus. Low levels detected also in
CC       the chromatin fraction (By similarity). Upon methionine stimulation,
CC       localizes to the lysosome in an NPRL2-dependent manner (By similarity).
CC       {ECO:0000250|UniProtKB:Q99873, ECO:0000250|UniProtKB:Q9JIF0}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- PTM: Polyubiquitinated at Lys-127 by the SCF(FBXL17) complex, leading
CC       to its subsequent degradation (By similarity). Ubiquitination is
CC       regulated by acetylation at Lys-210 and Lys-215 (By similarity).
CC       Polyubiquitinated by E3 ubiquitin-protein ligase TRIM48, leading to
CC       suppression of MAP3K5/ASK1 methylation and subsequent MAP3K5 activation
CC       (By similarity). {ECO:0000250|UniProtKB:Q99873,
CC       ECO:0000250|UniProtKB:Q9JIF0}.
CC   -!- PTM: Acetylation at Lys-210 and Lys-215 regulates ubiquitination by the
CC       SCF(FBXL17) complex. Acetylated at Lys-215 by p300/EP300. Deacetylated
CC       at Lys-210 and Lys-215 by SIRT1. {ECO:0000250|UniProtKB:Q9JIF0}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Protein arginine N-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR   EMBL; U60882; AAC52622.1; -; mRNA.
DR   EMBL; BC078815; AAH78815.1; -; mRNA.
DR   RefSeq; NP_077339.1; NM_024363.1.
DR   PDB; 1OR8; X-ray; 2.35 A; A=14-353.
DR   PDB; 1ORH; X-ray; 2.64 A; A=1-353.
DR   PDB; 1ORI; X-ray; 2.50 A; A=11-353.
DR   PDB; 3Q7E; X-ray; 2.20 A; A=14-353.
DR   PDBsum; 1OR8; -.
DR   PDBsum; 1ORH; -.
DR   PDBsum; 1ORI; -.
DR   PDBsum; 3Q7E; -.
DR   AlphaFoldDB; Q63009; -.
DR   SMR; Q63009; -.
DR   BioGRID; 248825; 4.
DR   IntAct; Q63009; 6.
DR   MINT; Q63009; -.
DR   STRING; 10116.ENSRNOP00000063624; -.
DR   BindingDB; Q63009; -.
DR   ChEMBL; CHEMBL1275220; -.
DR   iPTMnet; Q63009; -.
DR   PhosphoSitePlus; Q63009; -.
DR   jPOST; Q63009; -.
DR   PaxDb; 10116-ENSRNOP00000063624; -.
DR   Ensembl; ENSRNOT00055009066; ENSRNOP00055006909; ENSRNOG00055005632.
DR   Ensembl; ENSRNOT00060013117; ENSRNOP00060009946; ENSRNOG00060007875.
DR   Ensembl; ENSRNOT00065048584; ENSRNOP00065039836; ENSRNOG00065028078.
DR   GeneID; 60421; -.
DR   KEGG; rno:60421; -.
DR   UCSC; RGD:62020; rat.
DR   AGR; RGD:62020; -.
DR   CTD; 3276; -.
DR   RGD; 62020; Prmt1.
DR   VEuPathDB; HostDB:ENSRNOG00000026109; -.
DR   eggNOG; KOG1499; Eukaryota.
DR   HOGENOM; CLU_017375_1_1_1; -.
DR   InParanoid; Q63009; -.
DR   OrthoDB; 197898at2759; -.
DR   BRENDA; 2.1.1.319; 5301.
DR   Reactome; R-RNO-3214858; RMTs methylate histone arginines.
DR   Reactome; R-RNO-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR   SABIO-RK; Q63009; -.
DR   EvolutionaryTrace; Q63009; -.
DR   PRO; PR:Q63009; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000026109; Expressed in ovary and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0044020; F:histone H4R3 methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0042054; F:histone methyltransferase activity; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR   GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; ISO:RGD.
DR   GO; GO:0008170; F:N-methyltransferase activity; ISO:RGD.
DR   GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:RGD.
DR   GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:MGI.
DR   GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:MGI.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; TAS:RGD.
DR   GO; GO:0030519; F:snoRNP binding; IDA:RGD.
DR   GO; GO:0048738; P:cardiac muscle tissue development; ISS:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR   GO; GO:0046329; P:negative regulation of JNK cascade; ISS:UniProtKB.
DR   GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR   GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IDA:MGI.
DR   GO; GO:0035247; P:peptidyl-arginine omega-N-methylation; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:BHF-UCL.
DR   GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:BHF-UCL.
DR   GO; GO:0045727; P:positive regulation of translation; ISO:RGD.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   GO; GO:0006479; P:protein methylation; IDA:MGI.
DR   GO; GO:0030510; P:regulation of BMP signaling pathway; ISO:RGD.
DR   GO; GO:0045652; P:regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11006:SF54; PROTEIN ARGININE N-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
DR   Genevisible; Q63009; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Lysosome; Membrane;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Ubl conjugation.
FT   CHAIN           1..353
FT                   /note="Protein arginine N-methyltransferase 1"
FT                   /id="PRO_0000212323"
FT   DOMAIN          32..353
FT                   /note="SAM-dependent MTase PRMT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000269|PubMed:12737817"
FT   ACT_SITE        153
FT                   /evidence="ECO:0000269|PubMed:12737817"
FT   BINDING         45
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:12737817"
FT   BINDING         54
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:12737817"
FT   BINDING         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:12737817"
FT   BINDING         100
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:12737817"
FT   BINDING         129
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:12737817"
FT   MOD_RES         116
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIF0"
FT   MOD_RES         210
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIF0"
FT   MOD_RES         215
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIF0"
FT   MOD_RES         286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99873"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99873"
FT   CROSSLNK        127
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIF0"
FT   MUTAGEN         80
FT                   /note="G->R: Abolishes catalytic activity. Disrupts
FT                   interaction of MAP3K5/ASK1 with thioredoxin. Abolishes
FT                   inhibition of MAP3K5 and activation of JNK1. No effect on
FT                   interaction with MAP3K5."
FT                   /evidence="ECO:0000269|PubMed:22095282"
FT   MUTAGEN         144
FT                   /note="E->D: Reduces catalytic activity 10-fold, and causes
FT                   higher order oligomers of the protein."
FT                   /evidence="ECO:0000269|PubMed:12737817"
FT   MUTAGEN         144
FT                   /note="E->Q: Reduces catalytic activity 3000-fold, and
FT                   causes higher order oligomers of the protein."
FT                   /evidence="ECO:0000269|PubMed:12737817"
FT   MUTAGEN         153
FT                   /note="E->D: Reduces catalytic activity to 0.03%, but does
FT                   not affect oligomerization."
FT                   /evidence="ECO:0000269|PubMed:12737817"
FT   MUTAGEN         153
FT                   /note="E->Q: Completely abolishes catalytic activity, but
FT                   does not affect oligomerization."
FT                   /evidence="ECO:0000269|PubMed:12737817"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:1ORH"
FT   HELIX           43..50
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   HELIX           52..63
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          73..78
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   HELIX           83..90
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          94..100
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   HELIX           104..114
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   TURN            118..120
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          121..126
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   TURN            128..130
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          138..143
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          147..152
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   HELIX           156..166
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          167..175
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          177..185
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   HELIX           188..194
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   HELIX           196..199
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   HELIX           207..209
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   HELIX           210..214
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          218..220
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   HELIX           224..226
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          227..238
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   TURN            239..241
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   HELIX           244..247
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          248..257
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          259..273
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          277..279
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          282..284
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          296..307
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          312..321
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          323..325
FT                   /evidence="ECO:0007829|PDB:1ORI"
FT   STRAND          329..338
FT                   /evidence="ECO:0007829|PDB:3Q7E"
FT   STRAND          343..352
FT                   /evidence="ECO:0007829|PDB:3Q7E"
SQ   SEQUENCE   353 AA;  40522 MW;  EDBB0587784C527E CRC64;
     MAAAEAANCI MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK DEVRTLTYRN
     SMFHNRHLFK DKVVLDVGSG TGILCMFAAK AGARKVIGIE CSSISDYAVK IVKANKLDHV
     VTIIKGKVEE VELPVEKVDI IISEWMGYCL FYESMLNTVL HARDKWLAPD GLIFPDRATL
     YVTAIEDRQY KDYKIHWWEN VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY
     TVKVEDLTFT SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY
     MEDYLTVKTG EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY RMR
//