PP2BB_MOUSE
ID PP2BB_MOUSE Reviewed; 525 AA.
AC P48453; Q6NZR4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:P16298};
DE AltName: Full=CAM-PRP catalytic subunit;
DE AltName: Full=Calmodulin-dependent calcineurin A subunit beta isoform;
DE Short=CNA beta {ECO:0000250|UniProtKB:P16298};
GN Name=Ppp3cb; Synonyms=Calnb;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-525 (ISOFORM 2).
RX PubMed=1659808; DOI=10.1016/s0006-291x(05)81410-x;
RA Giri P.R., Higuchi S., Kincaid R.L.;
RT "Chromosomal mapping of the human genes for the calmodulin-dependent
RT protein phosphatase (calcineurin) catalytic subunit.";
RL Biochem. Biophys. Res. Commun. 181:252-258(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 320-416 (ISOFORMS 1 AND 2).
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=10200317; DOI=10.1073/pnas.96.8.4650;
RA Zhuo M., Zhang W., Son H., Mansuy I., Sobel R.A., Seidman J., Kandel E.R.;
RT "A selective role of calcineurin aalpha in synaptic depotentiation in
RT hippocampus.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4650-4655(1999).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12773574; DOI=10.1128/mcb.23.12.4331-4343.2003;
RA Parsons S.A., Wilkins B.J., Bueno O.F., Molkentin J.D.;
RT "Altered skeletal muscle phenotypes in calcineurin Aalpha and Abeta gene-
RT targeted mice.";
RL Mol. Cell. Biol. 23:4331-4343(2003).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15509543; DOI=10.1016/s0002-9440(10)63430-x;
RA Gooch J.L., Toro J.J., Guler R.L., Barnes J.L.;
RT "Calcineurin A-alpha but not A-beta is required for normal kidney
RT development and function.";
RL Am. J. Pathol. 165:1755-1765(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, and Spleen;
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=21435446; DOI=10.1016/j.ajpath.2010.12.054;
RA Reddy R.N., Pena J.A., Roberts B.R., Williams S.R., Price S.R., Gooch J.L.;
RT "Rescue of calcineurin Aalpha(-/-) mice reveals a novel role for the alpha
RT isoform in the salivary gland.";
RL Am. J. Pathol. 178:1605-1613(2011).
RN [9]
RP FUNCTION, AND INTERACTION WITH MAP3K14 AND TRAF3.
RX PubMed=26029823; DOI=10.1038/srep10758;
RA Shinzawa M., Konno H., Qin J., Akiyama N., Miyauchi M., Ohashi H.,
RA Miyamoto-Sato E., Yanagawa H., Akiyama T., Inoue J.;
RT "Catalytic subunits of the phosphatase calcineurin interact with NF-kappaB-
RT inducing kinase (NIK) and attenuate NIK-dependent gene expression.";
RL Sci. Rep. 5:10758-10758(2015).
RN [10]
RP INTERACTION WITH SORL1, AND TISSUE SPECIFICITY.
RX PubMed=25967121; DOI=10.1681/asn.2014070728;
RA Borschewski A., Himmerkus N., Boldt C., Blankenstein K.I., McCormick J.A.,
RA Lazelle R., Willnow T.E., Jankowski V., Plain A., Bleich M., Ellison D.H.,
RA Bachmann S., Mutig K.;
RT "Calcineurin and sorting-related receptor with A-type repeats interact to
RT regulate the renal Na(+)-K(+)-2Cl(-) cotransporter.";
RL J. Am. Soc. Nephrol. 27:107-119(2016).
RN [11]
RP INTERACTION WITH UNC119.
RX PubMed=31696965; DOI=10.15252/embj.2018101409;
RA Chaya T., Tsutsumi R., Varner L.R., Maeda Y., Yoshida S., Furukawa T.;
RT "Cul3-Klhl18 ubiquitin ligase modulates rod transducin translocation during
RT light-dark adaptation.";
RL EMBO J. 2019:E101409-E101409(2019).
CC -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase
CC which plays an essential role in the transduction of intracellular
CC Ca(2+)-mediated signals (By similarity). Dephosphorylates and activates
CC transcription factor NFATC1 (By similarity). Dephosphorylates and
CC inactivates transcription factor ELK1 (By similarity). Dephosphorylates
CC DARPP32 (By similarity). Negatively regulates MAP3K14/NIK signaling via
CC inhibition of nuclear translocation of the transcription factors RELA
CC and RELB (PubMed:26029823). May play a role in skeletal muscle fiber
CC type specification (PubMed:12773574). {ECO:0000250|UniProtKB:P16298,
CC ECO:0000269|PubMed:12773574, ECO:0000269|PubMed:26029823}.
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:0000250|UniProtKB:P16298};
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:0000250|UniProtKB:P16298};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000250|UniProtKB:P16298};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250|UniProtKB:P16298};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P16298};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P16298};
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)-bound calmodulin following an
CC increase in intracellular Ca(2+). At low Ca(2+) concentrations, the
CC catalytic subunit (also known as calcineurin A) is inactive and is
CC bound to the regulatory subunit (also known as calcineurin B) in which
CC only two high-affinity binding sites are occupied by Ca(2+). In
CC response to elevated calcium levels, the occupancy of the low-affinity
CC sites on calcineurin B by Ca(2+) causes a conformational change of the
CC C-terminal regulatory domain of calcineurin A, resulting in the
CC exposure of the calmodulin-binding domain and in the partial activation
CC of calcineurin A. 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.
CC {ECO:0000250|UniProtKB:P16298}.
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). There are three catalytic
CC subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC)
CC and two regulatory subunits which are also encoded by separate genes
CC (PPP3R1 and PPP3R2). In response to an increase in Ca(2+) intracellular
CC levels, forms a complex composed of PPP3CB/calcineurin A, calcineurin B
CC and calmodulin. Interacts (via calcineurin B binding domain) with
CC regulatory subunit PPP3R1/calcineurin B. Interacts (via calmodulin-
CC binding domain) with calmodulin; the interaction depends on calmodulin
CC binding to Ca(2+). Interacts with SLC12A1 (By similarity). Interacts
CC with SORL1 (PubMed:25967121). Interacts with UNC119 (PubMed:31696965).
CC Interacts with MAP3K14/NIK (via C-terminus and kinase domain)
CC (PubMed:26029823). Interacts with TRAF3 (PubMed:26029823). Interacts
CC with SPATA33 (via PQIIIT motif) (By similarity).
CC {ECO:0000250|UniProtKB:P16298, ECO:0000250|UniProtKB:P20651,
CC ECO:0000269|PubMed:25967121, ECO:0000269|PubMed:26029823,
CC ECO:0000269|PubMed:31696965}.
CC -!- INTERACTION:
CC P48453; D3YVF0: Akap5; NbExp=3; IntAct=EBI-642618, EBI-7091108;
CC P48453; Q9WVC7: Akap6; Xeno; NbExp=2; IntAct=EBI-642618, EBI-7559840;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16298}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=2B2;
CC IsoId=P48453-1; Sequence=Displayed;
CC Name=1; Synonyms=2B1;
CC IsoId=P48453-2; Sequence=VSP_011856;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, in the thick ascending limb
CC epithelium and in the collecting duct, but not in the distal convoluted
CC tubule (at protein level) (PubMed:25967121, PubMed:15509543). Expressed
CC in the brain and the bicep, tricep, soleus and gastrocnemius muscles
CC (at protein level) (PubMed:12773574). Expressed in the salivary gland
CC (at protein level) (PubMed:21435446). Expressed in hippocampal neuron
CC nuclei and adjacent white matter tracts in the CA1 region of the
CC hippocampus (at protein level) (PubMed:10200317).
CC {ECO:0000269|PubMed:10200317, ECO:0000269|PubMed:12773574,
CC ECO:0000269|PubMed:15509543, ECO:0000269|PubMed:21435446,
CC ECO:0000269|PubMed:25967121}.
CC -!- DOMAIN: The poly-Pro domain may confer substrate specificity.
CC {ECO:0000250|UniProtKB:P16298}.
CC -!- DOMAIN: The autoinhibitory domain prevents access to the catalytic
CC site. {ECO:0000250|UniProtKB:P16298}.
CC -!- DOMAIN: The autoinhibitory segment prevents access to the substrate
CC binding site. {ECO:0000250|UniProtKB:P16298}.
CC -!- DOMAIN: Possible isomerization of Pro-318 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 -!- DISRUPTION PHENOTYPE: Knockout mice show reduced body weight,
CC independent of changes in muscle weight (PubMed:12773574). Reduced slow
CC and intermediate program type muscle fibers in the biceps, triceps and
CC soleus (PubMed:12773574). Increased expression of fast program type
CC muscle fibers in the soleus muscle (PubMed:12773574).
CC {ECO:0000269|PubMed:12773574}.
CC -!- MISCELLANEOUS: Unlike for protein substrates, PPP3CB activity towards
CC synthetic phosphatase substrate p-nitrophenyl phosphate (pNPP) is
CC increased in presence of the immunosuppressant complex FKBP12-FK506.
CC {ECO:0000250|UniProtKB:P16298}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC {ECO:0000305}.
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DR EMBL; BC066000; AAH66000.1; -; mRNA.
DR EMBL; M81483; AAA37411.1; -; mRNA.
DR CCDS; CCDS26846.1; -. [P48453-1]
DR PIR; JT0976; JT0976.
DR RefSeq; NP_001297355.1; NM_001310426.1.
DR RefSeq; NP_001297356.1; NM_001310427.1.
DR RefSeq; NP_032940.1; NM_008914.3. [P48453-1]
DR AlphaFoldDB; P48453; -.
DR SMR; P48453; -.
DR BioGRID; 202345; 26.
DR ComplexPortal; CPX-1006; Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant.
DR ComplexPortal; CPX-1008; Calcineurin-Calmodulin complex, beta-R2 variant.
DR ComplexPortal; CPX-1011; Calcineurin-Calmodulin complex, beta-R1 variant.
DR ComplexPortal; CPX-1117; Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant.
DR IntAct; P48453; 13.
DR MINT; P48453; -.
DR STRING; 10090.ENSMUSP00000125722; -.
DR iPTMnet; P48453; -.
DR PhosphoSitePlus; P48453; -.
DR SwissPalm; P48453; -.
DR EPD; P48453; -.
DR jPOST; P48453; -.
DR MaxQB; P48453; -.
DR PaxDb; P48453; -.
DR PRIDE; P48453; -.
DR ProteomicsDB; 289870; -. [P48453-1]
DR ProteomicsDB; 289871; -. [P48453-2]
DR Antibodypedia; 1918; 214 antibodies from 35 providers.
DR DNASU; 19056; -.
DR Ensembl; ENSMUST00000159027; ENSMUSP00000125722; ENSMUSG00000021816. [P48453-1]
DR GeneID; 19056; -.
DR KEGG; mmu:19056; -.
DR UCSC; uc007sjx.2; mouse. [P48453-1]
DR CTD; 5532; -.
DR MGI; MGI:107163; Ppp3cb.
DR VEuPathDB; HostDB:ENSMUSG00000021816; -.
DR eggNOG; KOG0375; Eukaryota.
DR GeneTree; ENSGT00940000154115; -.
DR InParanoid; P48453; -.
DR OMA; TNRRIMN; -.
DR OrthoDB; 463522at2759; -.
DR PhylomeDB; P48453; -.
DR TreeFam; TF105557; -.
DR Reactome; R-MMU-2025928; Calcineurin activates NFAT.
DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR Reactome; R-MMU-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR BioGRID-ORCS; 19056; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ppp3cb; mouse.
DR PRO; PR:P48453; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P48453; protein.
DR Bgee; ENSMUSG00000021816; Expressed in subiculum and 255 other tissues.
DR ExpressionAtlas; P48453; baseline and differential.
DR Genevisible; P48453; MM.
DR GO; GO:0005955; C:calcineurin complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IC:ComplexPortal.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IMP:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046983; F:protein dimerization activity; ISO:MGI.
DR GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097720; P:calcineurin-mediated signaling; ISS:UniProtKB.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; ISO:MGI.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IDA:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; IMP:MGI.
DR GO; GO:0001946; P:lymphangiogenesis; IGI:MGI.
DR GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; IC:ComplexPortal.
DR GO; GO:0023057; P:negative regulation of signaling; IMP:UniProtKB.
DR GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IC:ComplexPortal.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IC:ComplexPortal.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IC:ComplexPortal.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IC:ComplexPortal.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:0034097; P:response to cytokine; IMP:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; IMP:MGI.
DR GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IMP:MGI.
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 Acetylation; Alternative splicing; Calmodulin-binding; Cytoplasm;
KW Hydrolase; Iron; Metal-binding; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT CHAIN 2..525
FT /note="Serine/threonine-protein phosphatase 2B catalytic
FT subunit beta isoform"
FT /id="PRO_0000058826"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..356
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT REGION 357..379
FT /note="Calcineurin B binding"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT REGION 402..416
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT REGION 417..424
FT /note="Autoinhibitory segment"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT REGION 475..497
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT MOTIF 316..320
FT /note="SAPNY motif"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 387..406
FT /note="MTEGEDQFDVGSAAARKEII -> GSEEDGFDGATAAARKEVI (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:1328240"
FT /id="VSP_011856"
FT CONFLICT 481
FT /note="E -> G (in Ref. 2; AAA37411)"
FT /evidence="ECO:0000305"
FT CONFLICT 523..524
FT /note="SA -> TP (in Ref. 2; AAA37411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 59173 MW; 5E73BA3100BE2337 CRC64;
MAAPEPARAA PPPPPPPPPP LGADRVVKAV PFPPTHRLTS EEVFDMDGIP RVDVLKNHLV
KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI HGQFFDLMKL FEVGGSPANT
RYLFLGDYVD RGYFSIECVL YLWVLKILYP STLFLLRGNH ECRHLTEYFT FKQECKIKYS
ERVYEACMEA FDSLPLAALL NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL
WSDPSEDFGN EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY
RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY WLPNFMDVFT
WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDVGSAA ARKEIIRNKI RAIGKMARVF
SVLREESESV LTLKGLTPTG MLPSGVLAGG RQTLQSATVE AIEAEKAIRG FSPPHRICSF
EEAKGLDRIN ERMPPRKDAV QQDGFNSLNT AHTTENHGTG NHSAQ
