PP2BA_BOVIN
ID PP2BA_BOVIN Reviewed; 521 AA.
AC P48452; Q08DM4; Q309F2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Protein phosphatase 3 catalytic subunit alpha {ECO:0000250|UniProtKB:Q08209};
DE EC=3.1.3.16 {ECO:0000269|PubMed:1328240, ECO:0000269|PubMed:15967565, ECO:0000269|PubMed:16411749, ECO:0000269|PubMed:1715244};
DE AltName: Full=CAM-PRP catalytic subunit;
DE AltName: Full=Calcineurin A alpha {ECO:0000250|UniProtKB:Q08209};
DE AltName: Full=Calmodulin-dependent calcineurin A subunit alpha isoform {ECO:0000250|UniProtKB:P63328};
DE Short=CNA alpha {ECO:0000250|UniProtKB:P63328};
DE AltName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform {ECO:0000250|UniProtKB:Q08209};
GN Name=PPP3CA {ECO:0000250|UniProtKB:Q08209};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND X-RAY CRYSTALLOGRAPHY (2.50
RP ANGSTROMS) OF 18-392 IN COMPLEX WITH PPP3R1; IRON AND ZINC.
RC TISSUE=Brain;
RX PubMed=7543369; DOI=10.1016/0092-8674(95)90439-5;
RA Griffith J.P., Kim J.L., Kim E.E., Sintchak M.D., Thomson J.A.,
RA Fitzgibbon M.J., Fleming M.A., Caron P.R., Hsiao K., Navia M.A.;
RT "X-ray structure of calcineurin inhibited by the immunophilin-
RT immunosuppressant FKBP12-FK506 complex.";
RL Cell 82:507-522(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Heart muscle;
RX PubMed=15967565; DOI=10.1016/j.biochi.2005.04.010;
RA Selvakumar P., Lakshmikuttyamma A., Anderson D.H., Sharma R.K.;
RT "Molecular cloning, expression, purification and characterization of
RT calcineurin from bovine cardiac muscle.";
RL Biochimie 87:975-983(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, IDENTIFICATION IN A
RP COMPLEX WITH PPP3R1 AND CALMODULIN, AND TISSUE SPECIFICITY.
RX PubMed=1715244; DOI=10.1016/0092-8674(91)90124-h;
RA Liu J., Farmer J.D. Jr., Lane W.S., Friedman J., Weissman I.,
RA Schreiber S.L.;
RT "Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506
RT complexes.";
RL Cell 66:807-815(1991).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=1328240; DOI=10.1016/s0021-9258(19)36654-2;
RA Gaestel M., Benndorf R., Hayess K., Priemer E., Engel K.;
RT "Dephosphorylation of the small heat shock protein hsp25 by
RT calcium/calmodulin-dependent (type 2B) protein phosphatase.";
RL J. Biol. Chem. 267:21607-21611(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 389-413, FUNCTION, CATALYTIC
RP ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=16411749; DOI=10.1021/bi0521801;
RA Ye Q., Li X., Wong A., Wei Q., Jia Z.;
RT "Structure of calmodulin bound to a calcineurin peptide: a new way of
RT making an old binding mode.";
RL Biochemistry 45:738-745(2006).
CC -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase
CC which plays an essential role in the transduction of intracellular
CC Ca(2+)-mediated signals (PubMed:15967565, PubMed:1715244,
CC PubMed:1328240, PubMed:16411749). Many of the substrates contain a
CC PxIxIT motif and/or a LxVP motif (By similarity). In response to
CC increased Ca(2+) levels, dephosphorylates and activates phosphatase
CC SSH1 which results in cofilin dephosphorylation (By similarity). In
CC response to increased Ca(2+) levels following mitochondrial
CC depolarization, dephosphorylates DNM1L inducing DNM1L translocation to
CC the mitochondrion (By similarity). Positively regulates the
CC CACNA1B/CAV2.2-mediated Ca(2+) release probability at hippocampal
CC neuronal soma and synaptic terminals (By similarity). Dephosphorylates
CC heat shock protein HSPB1 (PubMed:1328240). Dephosphorylates and
CC activates transcription factor NFATC1 (By similarity). Dephosphorylates
CC and inactivates transcription factor ELK1 (By similarity).
CC Dephosphorylates DARPP32 (By similarity). May dephosphorylate CRTC2 at
CC 'Ser-171' resulting in CRTC2 dissociation from 14-3-3 proteins (By
CC similarity). Required for postnatal development of the nephrogenic zone
CC and superficial glomeruli in the kidneys, cell cycle homeostasis in the
CC nephrogenic zone, and ultimately normal kidney function (By
CC similarity). Plays a role in intracellular AQP2 processing and
CC localization to the apical membrane in the kidney, may thereby be
CC required for efficient kidney filtration (By similarity). Required for
CC secretion of salivary enzymes amylase, peroxidase, lysozyme and sialic
CC acid via formation of secretory vesicles in the submandibular glands
CC (By similarity). Required for calcineurin activity and homosynaptic
CC depotentiation in the hippocampus (By similarity). Required for normal
CC differentiation and survival of keratinocytes and therefore required
CC for epidermis superstructure formation (By similarity). Positively
CC regulates osteoblastic bone formation, via promotion of osteoblast
CC differentiation (By similarity). Positively regulates osteoclast
CC differentiation, potentially via NFATC1 signaling (By similarity). May
CC play a role in skeletal muscle fiber type specification, potentially
CC via NFATC1 signaling (By similarity). Negatively regulates MAP3K14/NIK
CC signaling via inhibition of nuclear translocation of the transcription
CC factors RELA and RELB (By similarity). Required for antigen-specific T-
CC cell proliferation response (By similarity).
CC {ECO:0000250|UniProtKB:P63328, ECO:0000250|UniProtKB:P63329,
CC ECO:0000250|UniProtKB:Q08209, ECO:0000269|PubMed:1328240,
CC ECO:0000269|PubMed:15967565, ECO:0000269|PubMed:16411749,
CC ECO:0000269|PubMed:1715244}.
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; Evidence={ECO:0000269|PubMed:1328240,
CC ECO:0000269|PubMed:15967565, ECO:0000269|PubMed:16411749,
CC ECO:0000269|PubMed:1715244};
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; Evidence={ECO:0000269|PubMed:1328240,
CC ECO:0000269|PubMed:15967565, ECO:0000269|PubMed:16411749,
CC ECO:0000269|PubMed:1715244};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:7543369};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:7543369};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:7543369};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:7543369};
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)-bound calmodulin following an
CC increase in intracellular Ca(2+) (PubMed:16411749). At low Ca(2+)
CC concentrations, the catalytic subunit (also known as calcineurin A) is
CC inactive and is bound to the regulatory subunit (also known as
CC calcineurin B) in which only two high-affinity binding sites are
CC occupied by Ca(2+) (By similarity). In response to elevated calcium
CC levels, the occupancy of the low-affinity sites on calcineurin B by
CC Ca(2+) causes a conformational change of the C-terminal regulatory
CC domain of calcineurin A, resulting in the exposure of the calmodulin-
CC binding domain and in the partial activation of calcineurin A
CC (PubMed:16411749). The subsequent binding of Ca(2+)-bound calmodulin
CC leads to the displacement of the autoinhibitory domain from the active
CC site and possibly of the autoinhibitory segment from the substrate
CC binding site which fully activates calcineurin A (By similarity).
CC Inhibited by immunosuppressant drug FK506 (tacrolimus) in complex with
CC FKBP12 and also by immunosuppressant drug cyclosporin A (CsA) in
CC complex with PPIA/cyclophilin A; the inhibition is Ca(2+)-dependent
CC (PubMed:1715244). {ECO:0000250|UniProtKB:P16298,
CC ECO:0000269|PubMed:16411749, ECO:0000269|PubMed:1715244}.
CC -!- SUBUNIT: Forms a complex composed of a calmodulin-dependent catalytic
CC subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding
CC subunit (also known as calcineurin B) (PubMed:7543369, PubMed:1715244).
CC There are three catalytic subunits, each encoded by a separate gene
CC (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also
CC encoded by separate genes (PPP3R1 and PPP3R2). In response to an
CC increase in Ca(2+) intracellular levels, forms a complex composed of
CC PPP3CA/calcineurin A, calcineurin B and calmodulin (PubMed:1715244).
CC Interacts (via calcineurin B binding domain) with regulatory subunit
CC PPP3R1/calcineurin B (PubMed:7543369). Interacts (via calmodulin-
CC binding domain) with CALM1/calmodulin; the interaction depends on
CC calmodulin binding to Ca(2+) (PubMed:1715244). Forms a complex composed
CC of MYOZ2 and ACTN1 (By similarity). Within the complex interacts with
CC MYOZ2 (By similarity). Interacts with MYOZ1 (By similarity). Interacts
CC with MYOZ3 (By similarity).Interacts with CIB1; the interaction
CC increases upon cardiomyocyte hypertrophy (By similarity). Interacts
CC with CHP1 and CHP2 (By similarity). Interacts with CRTC1. Interacts
CC with CRTC2 (By similarity). Interacts with DNM1L; the interaction
CC dephosphorylates DNM1L and promotes its translocation to mitochondria
CC (By similarity). Interacts with CMYA5; this interaction represses
CC calcineurin activity in muscle (By similarity). Interacts
CC (constitutively active form) with SYNPO2 (By similarity). Interacts
CC with scaffold protein AKAP5 (via IAIIIT motif); the interaction
CC recruits PPP3CA to the plasma membrane following L-type Ca(2+)-channel
CC activation (By similarity). Interacts with NFATC2 (By similarity).
CC Interacts with RCAN3 (By similarity). Interacts with PPIA (By
CC similarity). Interacts with UNC119 (By similarity). Interacts with
CC C16orf74 (via PxIxIT motif, when phosphorylated on 'Thr-75') (By
CC similarity). Interacts (via N-terminus) with MAP3K14/NIK (via C-
CC terminus and kinase domain) (By similarity). Interacts with TRAF3 (By
CC similarity). Interacts with SPATA33 (via PQIIIT motif) (By similarity).
CC {ECO:0000250|UniProtKB:P63328, ECO:0000250|UniProtKB:P63329,
CC ECO:0000250|UniProtKB:Q08209, ECO:0000269|PubMed:1715244,
CC ECO:0000269|PubMed:7543369}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q08209}. Cell
CC membrane {ECO:0000250|UniProtKB:Q08209}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q08209}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P63329}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:P63329}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q08209}. Note=Colocalizes with ACTN1 and MYOZ2
CC at the Z line in heart and skeletal muscle (By similarity). Recruited
CC to the cell membrane by scaffold protein AKAP5 following L-type Ca(2+)-
CC channel activation (By similarity). {ECO:0000250|UniProtKB:P63329,
CC ECO:0000250|UniProtKB:Q08209}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48452-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48452-2; Sequence=VSP_018561;
CC -!- TISSUE SPECIFICITY: Expressed in brain and thymus (at protein level)
CC (PubMed:1715244, PubMed:1328240). Isoform 1: Expressed in brain.
CC Isoform 2: Expressed in cardiac muscle. {ECO:0000269|PubMed:1328240,
CC ECO:0000269|PubMed:15967565, ECO:0000269|PubMed:1715244}.
CC -!- DOMAIN: The autoinhibitory domain prevents access to the catalytic
CC site. {ECO:0000250|UniProtKB:P63328}.
CC -!- DOMAIN: The autoinhibitory segment prevents access to the substrate
CC binding site. {ECO:0000250|UniProtKB:P63328}.
CC -!- DOMAIN: Possible isomerization of Pro-309 within the SAPNY motif
CC triggers a conformation switch which affects the organization and thus
CC accessibility of the active site and the substrate binding region
CC (PxIxIF motif). The trans- to cis-transition may favor calcineurin A
CC activation and substrate binding. The reverse cis- to trans-transition
CC may be enhanced by peptidyl-prolyl isomerases such as PPIA.
CC {ECO:0000250|UniProtKB:Q08209}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC {ECO:0000305}.
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DR EMBL; U33868; AAC48473.1; -; mRNA.
DR EMBL; DQ231569; ABB22788.1; -; mRNA.
DR EMBL; BC123668; AAI23669.1; -; mRNA.
DR PIR; A56968; A56968.
DR RefSeq; NP_777212.1; NM_174787.2. [P48452-1]
DR RefSeq; XP_005207750.1; XM_005207693.3. [P48452-2]
DR PDB; 1TCO; X-ray; 2.50 A; A=18-392.
DR PDB; 2F2O; X-ray; 2.17 A; A/B=389-413.
DR PDB; 2F2P; X-ray; 2.60 A; A/B=389-413.
DR PDBsum; 1TCO; -.
DR PDBsum; 2F2O; -.
DR PDBsum; 2F2P; -.
DR AlphaFoldDB; P48452; -.
DR BMRB; P48452; -.
DR SMR; P48452; -.
DR BioGRID; 159961; 2.
DR IntAct; P48452; 1.
DR MINT; P48452; -.
DR STRING; 9913.ENSBTAP00000021305; -.
DR iPTMnet; P48452; -.
DR PaxDb; P48452; -.
DR PRIDE; P48452; -.
DR Ensembl; ENSBTAT00000021305; ENSBTAP00000021305; ENSBTAG00000016005. [P48452-1]
DR Ensembl; ENSBTAT00000056385; ENSBTAP00000047848; ENSBTAG00000016005. [P48452-2]
DR GeneID; 286852; -.
DR KEGG; bta:286852; -.
DR CTD; 5530; -.
DR VEuPathDB; HostDB:ENSBTAG00000016005; -.
DR eggNOG; KOG0375; Eukaryota.
DR GeneTree; ENSGT00940000156306; -.
DR HOGENOM; CLU_004962_6_0_1; -.
DR InParanoid; P48452; -.
DR OMA; MESFCCL; -.
DR OrthoDB; 463522at2759; -.
DR TreeFam; TF105557; -.
DR BRENDA; 3.1.3.16; 908.
DR EvolutionaryTrace; P48452; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000016005; Expressed in occipital lobe and 106 other tissues.
DR ExpressionAtlas; P48452; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005955; C:calcineurin complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; TAS:UniProtKB.
DR GO; GO:0008544; P:epidermis development; ISS:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0023057; P:negative regulation of signaling; ISS:UniProtKB.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:UniProtKB.
DR GO; GO:0090193; P:positive regulation of glomerulus development; ISS:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0046878; P:positive regulation of saliva secretion; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0061006; P:regulation of cell proliferation involved in kidney morphogenesis; ISS:UniProtKB.
DR GO; GO:0097205; P:renal filtration; ISS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISS:UniProtKB.
DR CDD; cd07416; MPP_PP2B; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041751; MPP_PP2B.
DR InterPro; IPR043360; PP2B.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45673; PTHR45673; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calmodulin-binding;
KW Cell membrane; Cell projection; Cytoplasm; Hydrolase; Iron; Membrane;
KW Metal-binding; Nitration; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Synapse; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT CHAIN 2..521
FT /note="Protein phosphatase 3 catalytic subunit alpha"
FT /id="PRO_0000058821"
FT REGION 56..340
FT /note="Catalytic"
FT /evidence="ECO:0000305"
FT REGION 327..336
FT /note="Interaction with PxIxIF motif in substrate"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT REGION 341..369
FT /note="Calcineurin B binding"
FT /evidence="ECO:0000269|PubMed:16411749"
FT REGION 392..406
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000269|PubMed:16411749"
FT REGION 407..414
FT /note="Autoinhibitory segment"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT REGION 465..487
FT /note="Auto-inhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT REGION 475..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 307..311
FT /note="SAPNY motif"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT COMPBIAS 493..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:7543369,
FT ECO:0007744|PDB:1TCO"
FT BINDING 92
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:7543369,
FT ECO:0007744|PDB:1TCO"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:7543369,
FT ECO:0007744|PDB:1TCO"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:7543369,
FT ECO:0007744|PDB:1TCO"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:7543369,
FT ECO:0007744|PDB:1TCO"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:7543369,
FT ECO:0007744|PDB:1TCO"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:7543369,
FT ECO:0007744|PDB:1TCO"
FT SITE 352
FT /note="Interaction with PxVP motif in substrate"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT MOD_RES 224
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P63328"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63329"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT VAR_SEQ 448..457
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15967565"
FT /id="VSP_018561"
FT CONFLICT 367
FT /note="N -> D (in Ref. 2; ABB22788)"
FT /evidence="ECO:0000305"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 58..74
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:1TCO"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:1TCO"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1TCO"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1TCO"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 295..305
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 349..369
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:2F2O"
FT HELIX 397..409
FT /evidence="ECO:0007829|PDB:2F2O"
SQ SEQUENCE 521 AA; 58672 MW; F3F153F22AB56BDF CRC64;
MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEETV
ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK LFEVGGSPAN TRYLFLGDYV
DRGYFSIECV LYLWALKILY PKTLFLLRGN HECRHLTEYF TFKQECKIKY SERVYDACMD
AFDCLPLAAL MNQQFLCVHG GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG
NEKTQEHFTH NTVRGCSYFY SYPAVCEFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP
SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK
VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI RAIGKMARVF SVLREESESV
LTLKGLTPTG MLPSGVLSGG KQTLQSATVE AIEADEAIKG FSPQHKITSF EEAKGLDRIN
ERMPPRRDAM PSDANLNSIN KALASETNGT DSNGSNSSNI Q
