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   02-SEP-2026, entry version 201.
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:1328240, PubMed:15967565,
CC       PubMed:16411749, PubMed:1715244). 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). Dephosphorylates KLHL3,
CC       promoting the interaction between KLHL3 and WNK4 and subsequent
CC       degradation of WNK4 (By similarity). Negatively regulates SLC9A1
CC       activity (By similarity). {ECO:0000250|UniProtKB:P63328,
CC       ECO:0000250|UniProtKB:P63329, ECO:0000250|UniProtKB:Q08209,
CC       ECO:0000269|PubMed:1328240, ECO:0000269|PubMed:15967565,
CC       ECO:0000269|PubMed:16411749, ECO:0000269|PubMed:1715244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = 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=O-phospho-L-threonyl-[protein] + H2O = 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:1715244, PubMed:7543369).
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 CLMB
CC       (via PxIxIT motif, when phosphorylated on 'Thr-44'); leading to
CC       enhanced recruitment of PPP3CA to the plasma membrane and modulation of
CC       calcineurin signaling (By similarity). Interacts (via N-terminus) with
CC       MAP3K14/NIK (via C-terminus and kinase domain) (By similarity).
CC       Interacts with TRAF3 (By similarity). Interacts with SPATA33 (via
CC       PQIIIT motif) (By similarity). {ECO:0000250|UniProtKB:P63328,
CC       ECO:0000250|UniProtKB:P63329, ECO:0000250|UniProtKB:Q08209,
CC       ECO:0000269|PubMed:1715244, 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:1328240, PubMed:1715244). 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_005207693.5. [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   AlphaFoldDB; P48452; -.
DR   BMRB; P48452; -.
DR   SMR; P48452; -.
DR   BioGRID; 159961; 2.
DR   CORUM; P48452; -.
DR   FunCoup; P48452; 2619.
DR   IntAct; P48452; 1.
DR   MINT; P48452; -.
DR   STRING; 9913.ENSBTAP00000068601; -.
DR   iPTMnet; P48452; -.
DR   PaxDb; 9913-ENSBTAP00000068601; -.
DR   Ensembl; ENSBTAT00000021305.7; ENSBTAP00000021305.5; ENSBTAG00000016005.7. [P48452-2]
DR   GeneID; 286852; -.
DR   KEGG; bta:286852; -.
DR   CTD; 5530; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016005; -.
DR   VGNC; VGNC:33265; PPP3CA.
DR   eggNOG; KOG0375; Eukaryota.
DR   GeneTree; ENSGT00940000156306; -.
DR   HOGENOM; CLU_004962_6_0_1; -.
DR   InParanoid; P48452; -.
DR   OMA; YPAACNF; -.
DR   OrthoDB; 5593063at2759; -.
DR   BRENDA; 3.1.3.16; 908.
DR   Reactome; R-BTA-2025928; Calcineurin activates NFAT.
DR   Reactome; R-BTA-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-BTA-4086398; Ca2+ pathway.
DR   Reactome; R-BTA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR   EvolutionaryTrace; P48452; -.
DR   Proteomes; UP000009136; Chromosome 6.
DR   Bgee; ENSBTAG00000016005; Expressed in occipital lobe and 106 other cell types or tissues.
DR   ExpressionAtlas; P48452; baseline.
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:0005886; C:plasma membrane; ISS:UniProtKB.
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:0004722; F:protein serine/threonine phosphatase activity; EXP:UniProtKB.
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   FunFam; 3.60.21.10:FF:000002; Serine/threonine-protein phosphatase; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP.
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; SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR   PDBsum; 1TCO; -.
DR   PDBsum; 2F2O; -.
DR   PDBsum; 2F2P; -.
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        475..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..521
FT                   /note="Low complexity"
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
//