PPP5_MOUSE
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 03-AUG-2022, entry version 191.
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, Pancreas,
RC 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}.
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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; 32.
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; Q60676; -.
DR PeptideAtlas; Q60676; -.
DR PRIDE; Q60676; -.
DR ProteomicsDB; 289815; -.
DR Antibodypedia; 31446; 704 antibodies from 32 providers.
DR DNASU; 19060; -.
DR Ensembl; ENSMUST00000003183; ENSMUSP00000003183; ENSMUSG00000003099.
DR GeneID; 19060; -.
DR KEGG; mmu:19060; -.
DR UCSC; uc009fiq.2; mouse.
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; 671536at2759; -.
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; 2 hits in 76 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 261 other tissues.
DR ExpressionAtlas; Q60676; baseline and differential.
DR Genevisible; Q60676; MM.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; 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:0006470; P:protein dephosphorylation; 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; 1.25.40.10; -; 1.
DR Gene3D; 3.60.21.10; -; 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; IPR011236; Ser/Thr_PPase_5.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45668:SF5; PTHR45668:SF5; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08321; PPP5; 1.
DR Pfam; PF00515; TPR_1; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
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
