ID PPP5_MOUSE Reviewed; 499 AA. AC Q60676; G5E819; O35299; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 16-OCT-2013, sequence version 3. DT 27-MAR-2024, entry version 200. DE RecName: Full=Serine/threonine-protein phosphatase 5; DE Short=PP5; DE EC=3.1.3.16 {ECO:0000269|PubMed:21994940}; DE AltName: Full=Protein phosphatase T; DE Short=PPT; GN Name=Ppp5c; 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 [MRNA]. RA Ollendorff V., Donoghue D.J.; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-155. RX PubMed=7972012; DOI=10.1073/pnas.91.23.11075; RA Chinkers M.; RT "Targeting of a distinctive protein-serine phosphatase to the protein RT kinase-like domain of the atrial natriuretic peptide receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 91:11075-11079(1994). RN [6] RP IDENTIFICATION IN A COMPLEX WITH HSP90AA1 AND NR3C1. RX PubMed=9195923; DOI=10.1074/jbc.272.26.16224; RA Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., RA Chinkers M., Pratt W.B.; RT "Protein phosphatase 5 is a major component of glucocorticoid RT receptor.hsp90 complexes with properties of an FK506-binding RT immunophilin."; RL J. Biol. Chem. 272:16224-16230(1997). RN [7] RP INTERACTION WITH CPNE1. RX PubMed=12522145; DOI=10.1074/jbc.m212632200; RA Tomsig J.L., Snyder S.L., Creutz C.E.; RT "Identification of targets for calcium signaling through the copine family RT of proteins. Characterization of a coiled-coil copine-binding motif."; RL J. Biol. Chem. 278:10048-10054(2003). RN [8] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=16790549; DOI=10.1073/pnas.0604138103; RA Partch C.L., Shields K.F., Thompson C.L., Selby C.P., Sancar A.; RT "Posttranslational regulation of the mammalian circadian clock by RT cryptochrome and protein phosphatase 5."; RL Proc. Natl. Acad. Sci. U.S.A. 103:10467-10472(2006). RN [9] RP FUNCTION IN DNA DAMAGE RESPONSE, AND DISRUPTION PHENOTYPE. RX PubMed=17376776; DOI=10.1074/jbc.c700019200; RA Yong W., Bao S., Chen H., Li D., Sanchez E.R., Shou W.; RT "Mice lacking protein phosphatase 5 are defective in ataxia telangiectasia RT mutated (ATM)-mediated cell cycle arrest."; RL J. Biol. Chem. 282:14690-14694(2007). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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 [11] RP FUNCTION IN DEPHOSPHORYLATION OF NR3C1 AND PPARG, INTERACTION WITH NR3C1 RP AND PPARG, AND SUBCELLULAR LOCATION. RX PubMed=21994940; DOI=10.1074/jbc.m111.311662; RA Hinds T.D. Jr., Stechschulte L.A., Cash H.A., Whisler D., Banerjee A., RA Yong W., Khuder S.S., Kaw M.K., Shou W., Najjar S.M., Sanchez E.R.; RT "Protein phosphatase 5 mediates lipid metabolism through reciprocal control RT of glucocorticoid receptor and peroxisome proliferator-activated receptor-? RT (PPAR?)."; RL J. Biol. Chem. 286:42911-42922(2011). RN [12] RP FUNCTION IN GLUCOSE HOMEOSTASIS, AND DISRUPTION PHENOTYPE. RX PubMed=22526606; DOI=10.1007/s00125-012-2541-1; RA Grankvist N., Amable L., Honkanen R.E., Sjoeholm A., Ortsaeter H.; RT "Serine/threonine protein phosphatase 5 regulates glucose homeostasis in RT vivo and apoptosis signalling in mouse pancreatic islets and clonal MIN6 RT cells."; RL Diabetologia 55:2005-2015(2012). CC -!- FUNCTION: Serine/threonine-protein phosphatase that dephosphorylates a CC myriad of proteins involved in different signaling pathways including CC the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors CC NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT CC (PubMed:17376776, PubMed:21994940, PubMed:22526606). Implicated in wide CC ranging cellular processes, including apoptosis, differentiation, DNA CC damage response, cell survival, regulation of ion channels or circadian CC rhythms, in response to steroid and thyroid hormones, calcium, fatty CC acids, TGF-beta as well as oxidative and genotoxic stresses (By CC similarity). Participates in the control of DNA damage response CC mechanisms such as checkpoint activation and DNA damage repair through, CC for instance, the regulation ATM/ATR-signaling and dephosphorylation of CC PRKDC and TP53BP1 (PubMed:17376776). Inhibits ASK1/MAP3K5-mediated CC apoptosis induced by oxidative stress (By similarity). Plays a positive CC role in adipogenesis, mainly through the dephosphorylation and CC activation of PPARG transactivation function (PubMed:21994940). Also CC dephosphorylates and inhibits the anti-adipogenic effect of NR3C1 CC (PubMed:21994940). Regulates the circadian rhythms, through the CC dephosphorylation and activation of CSNK1E. May modulate TGF-beta CC signaling pathway by the regulation of SMAD3 phosphorylation and CC protein expression levels. Dephosphorylates and may play a role in the CC regulation of TAU/MAPT (By similarity). Through their CC dephosphorylation, may play a role in the regulation of ions channels CC such as KCNH2 (By similarity). Dephosphorylate FNIP1, disrupting CC interaction with HSP90AA1/Hsp90 (By similarity). CC {ECO:0000250|UniProtKB:P53041, ECO:0000250|UniProtKB:P53042, CC ECO:0000269|PubMed:17376776, ECO:0000269|PubMed:21994940, CC ECO:0000269|PubMed:22526606}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC Evidence={ECO:0000269|PubMed:21994940}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; CC Evidence={ECO:0000269|PubMed:21994940}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC Evidence={ECO:0000269|PubMed:21994940}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005; CC Evidence={ECO:0000269|PubMed:21994940}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 Mg(2+) or Mn(2+) cations per subunit. {ECO:0000250}; CC -!- ACTIVITY REGULATION: Autoinhibited. In the autoinhibited state, the TPR CC domain interacts with the catalytic region and prevents substrate CC access to the catalytic pocket. Allosterically activated by various CC polyunsaturated fatty acids, free long-chain fatty-acids and long-chain CC fatty acyl-CoA esters, arachidonic acid being the most effective CC activator. HSP90A and probably RAC1, GNA12 and GNA13 can also release CC the autoinhibition by the TPR repeat. Activation by RAC1, GNA12 and CC GNA13 is synergistic with the one produced by fatty acids binding. CC Inhibited by okadaic acid. CC -!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and CC HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and CC client protein TSC2 (By similarity). Probably forms a complex composed CC of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and CC client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not CC contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Part of CC a complex with HSP90/HSP90AA1 and steroid receptors (PubMed:9195923). CC Interacts (via TPR repeats) with HSP90AA1 (via TPR repeat-binding CC motif) or HSPA1A/HSPA1B; the interaction is direct and activates the CC phosphatase activity (By similarity). Dissociates from HSPA1A/HSPA1B CC and HSP90AA1 in response to arachidonic acid (By similarity). Interacts CC with CPNE1 (via VWFA domain) (PubMed:12522145). Interacts with CDC16, CC CDC27 (By similarity). Interacts with KLHDC10 (via the 6 Kelch CC repeats); inhibits the phosphatase activity on MAP3K5 (By similarity). CC Interacts with ATM and ATR; both interactions are induced by DNA damage CC and enhance ATM and ATR kinase activity (By similarity). Interacts with CC RAD17; reduced by DNA damage (By similarity). Interacts with nuclear CC receptors such as NR3C1/GCR and PPARG (activated by agonist); regulates CC their transactivation activities (PubMed:9195923, PubMed:21994940). CC Interacts (via TPR repeats) with S100 proteins S100A1, S100A2, S100A6, CC S100B and S100P; the interactions are calcium-dependent, strongly CC activate PPP5C phosphatase activity and compete with HSP90AA1 and CC MAP3K5 interactions (By similarity). Interacts with SMAD2 and SMAD3 but CC not with SMAD1; decreases SMAD3 phosphorylation and protein levels (By CC similarity). Interacts (via TPR repeats) with CRY1 and CRY2; the CC interaction with CRY2 down-regulates the phosphatase activity on CSNK1E CC (By similarity). Interacts (via TPR repeats) with the active form of CC RAC1, GNA12 or GNA13; these interactions activate the phosphatase CC activity and translocate PPP5C to the cell membrane (By similarity). CC Interacts with FLCN (By similarity). {ECO:0000250|UniProtKB:P53041, CC ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:21994940, CC ECO:0000269|PubMed:9195923}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21994940}. Cytoplasm CC {ECO:0000269|PubMed:21994940}. Cell membrane CC {ECO:0000250|UniProtKB:P53041}. Note=Predominantly nuclear. But also CC present in the cytoplasm. Translocates from the cytoplasm to the plasma CC membrane in a RAC1-dependent manner. {ECO:0000250|UniProtKB:P53041}. CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level) and brain, CC enriched in suprachiasmatic nuclei. {ECO:0000269|PubMed:16790549}. CC -!- INDUCTION: Does not show circadian oscillation. CC {ECO:0000269|PubMed:16790549}. CC -!- PTM: Activated by at least two different proteolytic cleavages CC producing a 56 kDa and a 50 kDa form. {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Animals are fertile with a growth rate equivalent CC to that of wild-type. Males weigh less, exhibit reduced fasting CC glycaemia and improved glucose tolerance, but retain normal insulin CC sensitivity. {ECO:0000269|PubMed:17376776, CC ECO:0000269|PubMed:22526606}. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T) CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF018262; AAB70573.1; -; mRNA. DR EMBL; AC148976; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466654; EDL42060.1; -; Genomic_DNA. DR EMBL; BC003744; AAH03744.1; -; mRNA. DR EMBL; U12204; AAB18613.1; -; mRNA. DR CCDS; CCDS20859.1; -. DR RefSeq; NP_035285.2; NM_011155.2. DR AlphaFoldDB; Q60676; -. DR SMR; Q60676; -. DR BioGRID; 202349; 114. DR IntAct; Q60676; 2. DR MINT; Q60676; -. DR STRING; 10090.ENSMUSP00000003183; -. DR iPTMnet; Q60676; -. DR PhosphoSitePlus; Q60676; -. DR SwissPalm; Q60676; -. DR EPD; Q60676; -. DR jPOST; Q60676; -. DR MaxQB; Q60676; -. DR PaxDb; 10090-ENSMUSP00000003183; -. DR PeptideAtlas; Q60676; -. DR ProteomicsDB; 289815; -. DR Pumba; Q60676; -. DR Antibodypedia; 31446; 769 antibodies from 32 providers. DR DNASU; 19060; -. DR Ensembl; ENSMUST00000003183.12; ENSMUSP00000003183.6; ENSMUSG00000003099.12. DR GeneID; 19060; -. DR KEGG; mmu:19060; -. DR UCSC; uc009fiq.2; mouse. DR AGR; MGI:102666; -. DR CTD; 5536; -. DR MGI; MGI:102666; Ppp5c. DR VEuPathDB; HostDB:ENSMUSG00000003099; -. DR eggNOG; KOG0376; Eukaryota. DR GeneTree; ENSGT00940000158785; -. DR InParanoid; Q60676; -. DR OMA; NHFFMSR; -. DR OrthoDB; 1107740at2759; -. DR PhylomeDB; Q60676; -. DR TreeFam; TF105562; -. DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway. DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-MMU-8939211; ESR-mediated signaling. DR BioGRID-ORCS; 19060; 4 hits in 83 CRISPR screens. DR ChiTaRS; Ppp5c; mouse. DR PRO; PR:Q60676; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q60676; Protein. DR Bgee; ENSMUSG00000003099; Expressed in retinal neural layer and 264 other cell types or tissues. DR ExpressionAtlas; Q60676; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0043204; C:perikaryon; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0101031; C:protein folding chaperone complex; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:1990635; C:proximal dendrite; ISO:MGI. DR GO; GO:0043531; F:ADP binding; ISO:MGI. DR GO; GO:0005524; F:ATP binding; ISO:MGI. DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI. DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI. DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008017; F:microtubule binding; ISO:MGI. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0016791; F:phosphatase activity; ISO:MGI. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IMP:MGI. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0003723; F:RNA binding; IDA:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI. DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; ISS:UniProtKB. DR GO; GO:2000324; P:positive regulation of glucocorticoid receptor signaling pathway; ISO:MGI. DR GO; GO:1904550; P:response to arachidonic acid; ISO:MGI. DR GO; GO:0010288; P:response to lead ion; ISO:MGI. DR GO; GO:0043278; P:response to morphine; IMP:MGI. DR CDD; cd07417; MPP_PP5_C; 1. DR Gene3D; 3.60.21.10; -; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR041753; PP5_C. DR InterPro; IPR013235; PPP_dom. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR001440; TPR_1. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1. DR PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1. DR Pfam; PF00149; Metallophos; 1. DR Pfam; PF08321; PPP5; 1. DR Pfam; PF00515; TPR_1; 1. DR PIRSF; PIRSF033096; PPPtase_5; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00156; PP2Ac; 1. DR SMART; SM00028; TPR; 3. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. DR PROSITE; PS50005; TPR; 3. DR PROSITE; PS50293; TPR_REGION; 1. DR Genevisible; Q60676; MM. PE 1: Evidence at protein level; KW Acetylation; Cell membrane; Cytoplasm; Hydrolase; Magnesium; Manganese; KW Membrane; Metal-binding; Nucleus; Protein phosphatase; Reference proteome; KW Repeat; TPR repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P53041" FT CHAIN 2..499 FT /note="Serine/threonine-protein phosphatase 5" FT /id="PRO_0000058895" FT REPEAT 28..61 FT /note="TPR 1" FT REPEAT 62..95 FT /note="TPR 2" FT REPEAT 96..129 FT /note="TPR 3" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 184..499 FT /note="Catalytic" FT REGION 495..499 FT /note="Required for autoinhibition" FT /evidence="ECO:0000250|UniProtKB:P53042" FT COMPBIAS 9..24 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 304 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P53041" FT BINDING 242 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P53041" FT BINDING 244 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P53041" FT BINDING 244 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P53041" FT BINDING 271 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P53041" FT BINDING 271 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P53041" FT BINDING 275 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P53041" FT BINDING 303..304 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P53041" FT BINDING 303 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P53041" FT BINDING 352 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P53041" FT BINDING 400 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P53041" FT BINDING 427 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P53041" FT BINDING 427 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P53041" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P53041" FT CONFLICT 24 FT /note="T -> A (in Ref. 1; AAB70573 and 4; AAH03744)" FT /evidence="ECO:0000305" FT CONFLICT 155 FT /note="D -> G (in Ref. 5; AAB18613)" FT /evidence="ECO:0000305" SQ SEQUENCE 499 AA; 56877 MW; 92C5509374FD6721 CRC64; MAMAEGERTE CAETPRDEPP ADGTLKRAEE LKTQANDYFK AKDYENAIKF YSQAIELNPG NAIYYGNRSL AYLRTECYGY ALGDATRAIE LDKKYIKGYY RRAASNMALG KFRAALRDYE TVVKVKPNDK DAKMKYQECS KIVKQKAFER AIAGDEHRRS VVDSLDIESM TIEDEYSGPK LEDGKVTITF MKDLMQWYKD QKKLHRKCAY QILVQVKEVL CKLSTLVETT LKETEKITVC GDTHGQFYDL LNIFELNGLP SETNPYIFNG DFVDRGSFSV EVILTLFGFK LLYPDHFHLL RGNHETDNMN QIYGFEGEVK AKYTAQMYEL FSEVFEWLPL AQCINGKVLI MHGGLFSEDG VTLDDIRKIE RNRQPPDSGP MCDLLWSDPQ PQNGRSVSKR GVSCQFGPDV TKAFLEENQL DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN YCDQMGNKAS YIHLQGSDLR PQFHQFTAVP HPNVKPMAYA NTLLQLGMM //