PP2BC_HUMAN
ID PP2BC_HUMAN Reviewed; 512 AA.
AC P48454; B4DRT5; Q9BSS6; Q9H4M5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform;
DE EC=3.1.3.16 {ECO:0000269|PubMed:19154138};
DE AltName: Full=CAM-PRP catalytic subunit;
DE AltName: Full=Calcineurin, testis-specific catalytic subunit;
DE AltName: Full=Calmodulin-dependent calcineurin A subunit gamma isoform;
GN Name=PPP3CC; Synonyms=CALNA3, CNA3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=1339277; DOI=10.1016/0006-291x(92)92379-c;
RA Muramatsu T., Kincaid R.L.;
RT "Molecular cloning and chromosomal mapping of the human gene for the
RT testis-specific catalytic subunit of calmodulin-dependent protein
RT phosphatase (calcineurin A).";
RL Biochem. Biophys. Res. Commun. 188:265-271(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Endothelial cell;
RA Bako E., Aydonian A., Verin A.D., Garcia J.G.N.;
RT "Isoform specific expression of calcineurin in endothelial cells.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymphoma;
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 [7]
RP FUNCTION, INTERACTION WITH CALCINEURIN B, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=19154138; DOI=10.1021/bi8019355;
RA Kilka S., Erdmann F., Migdoll A., Fischer G., Weiwad M.;
RT "The proline-rich N-terminal sequence of calcineurin Abeta determines
RT substrate binding.";
RL Biochemistry 48:1900-1910(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP INTERACTION WITH SPATA33.
RX PubMed=34446558; DOI=10.1073/pnas.2106673118;
RA Miyata H., Oura S., Morohoshi A., Shimada K., Mashiko D., Oyama Y.,
RA Kaneda Y., Matsumura T., Abbasi F., Ikawa M.;
RT "SPATA33 localizes calcineurin to the mitochondria and regulates sperm
RT motility in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase
CC which plays an essential role in the transduction of intracellular
CC Ca(2+)-mediated signals. Dephosphorylates and activates transcription
CC factor NFATC1. Dephosphorylates and inactivates transcription factor
CC ELK1. Dephosphorylates DARPP32. {ECO:0000269|PubMed:19154138}.
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:19154138};
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:19154138};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.27 uM for NFATC1 {ECO:0000269|PubMed:19154138};
CC KM=0.94 uM for DARPP32 {ECO:0000269|PubMed:19154138};
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:19154138). There are
CC three catalytic subunits, each encoded by a separate gene (PPP3CA,
CC PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded
CC by separate genes (PPP3R1 and PPP3R2). In response to an increase in
CC Ca(2+) intracellular levels, forms a complex composed of
CC PPP3CC/calcineurin A, calcineurin B and calmodulin (By similarity).
CC Interacts (via calmodulin-binding domain) with calmodulin; the
CC interaction depends on calmodulin binding to Ca(2+) (By similarity).
CC Interacts with UNC119 (By similarity). Interacts with SPATA33 (via
CC PQIIIT motif) (PubMed:34446558). Interacts with VDAC2 in a SPATA33-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:P16298,
CC ECO:0000250|UniProtKB:P48455, ECO:0000269|PubMed:19154138,
CC ECO:0000269|PubMed:34446558}.
CC -!- INTERACTION:
CC P48454; P49418: AMPH; NbExp=3; IntAct=EBI-2827192, EBI-7121510;
CC P48454; P05067: APP; NbExp=3; IntAct=EBI-2827192, EBI-77613;
CC P48454; P63098: PPP3R1; NbExp=4; IntAct=EBI-2827192, EBI-915984;
CC P48454; Q96N06: SPATA33; NbExp=3; IntAct=EBI-2827192, EBI-17572815;
CC P48454; Q13432: UNC119; NbExp=3; IntAct=EBI-2827192, EBI-711260;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P48455}.
CC Note=Localizes in the mitochondria in a SPATA33-dependent manner.
CC {ECO:0000250|UniProtKB:P48455}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P48454-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48454-2; Sequence=VSP_037946;
CC Name=3;
CC IsoId=P48454-3; Sequence=VSP_045211;
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:1339277}.
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-305 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; S46622; AAB23769.1; -; mRNA.
DR EMBL; AY007249; AAG02563.1; -; mRNA.
DR EMBL; AK299415; BAG61397.1; -; mRNA.
DR EMBL; AC037459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63677.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63679.1; -; Genomic_DNA.
DR EMBL; BC004864; AAH04864.1; -; mRNA.
DR CCDS; CCDS34859.1; -. [P48454-1]
DR CCDS; CCDS59093.1; -. [P48454-3]
DR CCDS; CCDS59094.1; -. [P48454-2]
DR PIR; JC1283; JC1283.
DR RefSeq; NP_001230903.1; NM_001243974.1. [P48454-3]
DR RefSeq; NP_001230904.1; NM_001243975.1. [P48454-2]
DR RefSeq; NP_005596.2; NM_005605.4. [P48454-1]
DR AlphaFoldDB; P48454; -.
DR SMR; P48454; -.
DR BioGRID; 111525; 69.
DR ComplexPortal; CPX-1001; Calcineurin-Calmodulin complex, gamma-R1 variant.
DR ComplexPortal; CPX-1050; Calcineurin-Calmodulin complex, gamma-R2 variant.
DR ComplexPortal; CPX-1112; Calcineurin-Calmodulin-AKAP5 complex, gamma-R1 variant.
DR ComplexPortal; CPX-1118; Calcineurin-Calmodulin-AKAP5 complex, gamma-R2 variant.
DR IntAct; P48454; 40.
DR MINT; P48454; -.
DR STRING; 9606.ENSP00000380878; -.
DR BindingDB; P48454; -.
DR DrugCentral; P48454; -.
DR DEPOD; PPP3CC; -.
DR iPTMnet; P48454; -.
DR PhosphoSitePlus; P48454; -.
DR BioMuta; PPP3CC; -.
DR DMDM; 257051041; -.
DR EPD; P48454; -.
DR jPOST; P48454; -.
DR MassIVE; P48454; -.
DR MaxQB; P48454; -.
DR PaxDb; P48454; -.
DR PeptideAtlas; P48454; -.
DR PRIDE; P48454; -.
DR ProteomicsDB; 4973; -.
DR ProteomicsDB; 55894; -. [P48454-1]
DR ProteomicsDB; 55895; -. [P48454-2]
DR Antibodypedia; 9535; 232 antibodies from 30 providers.
DR DNASU; 5533; -.
DR Ensembl; ENST00000240139.10; ENSP00000240139.5; ENSG00000120910.15. [P48454-1]
DR Ensembl; ENST00000289963.12; ENSP00000289963.8; ENSG00000120910.15. [P48454-2]
DR Ensembl; ENST00000397775.7; ENSP00000380878.3; ENSG00000120910.15. [P48454-3]
DR GeneID; 5533; -.
DR KEGG; hsa:5533; -.
DR MANE-Select; ENST00000240139.10; ENSP00000240139.5; NM_005605.5; NP_005596.2.
DR UCSC; uc003xbs.4; human. [P48454-1]
DR CTD; 5533; -.
DR DisGeNET; 5533; -.
DR GeneCards; PPP3CC; -.
DR HGNC; HGNC:9316; PPP3CC.
DR HPA; ENSG00000120910; Low tissue specificity.
DR MIM; 114107; gene.
DR neXtProt; NX_P48454; -.
DR OpenTargets; ENSG00000120910; -.
DR PharmGKB; PA33680; -.
DR VEuPathDB; HostDB:ENSG00000120910; -.
DR eggNOG; KOG0375; Eukaryota.
DR GeneTree; ENSGT00940000154115; -.
DR InParanoid; P48454; -.
DR OMA; NMITIEA; -.
DR OrthoDB; 463522at2759; -.
DR PhylomeDB; P48454; -.
DR TreeFam; TF105557; -.
DR PathwayCommons; P48454; -.
DR Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-HSA-180024; DARPP-32 events.
DR SignaLink; P48454; -.
DR SIGNOR; P48454; -.
DR BioGRID-ORCS; 5533; 6 hits in 1081 CRISPR screens.
DR ChiTaRS; PPP3CC; human.
DR GeneWiki; PPP3CC; -.
DR GenomeRNAi; 5533; -.
DR Pharos; P48454; Tbio.
DR PRO; PR:P48454; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P48454; protein.
DR Bgee; ENSG00000120910; Expressed in gastrocnemius and 197 other tissues.
DR ExpressionAtlas; P48454; baseline and differential.
DR Genevisible; P48454; HS.
DR GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IC:ComplexPortal.
DR GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; IDA:MGI.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
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:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IDA:UniProtKB.
DR GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; IC:ComplexPortal.
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:1900244; P:positive regulation of synaptic vesicle endocytosis; IEA:Ensembl.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IC:ComplexPortal.
DR GO; GO:0006470; P:protein dephosphorylation; IDA: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 Alternative splicing; Calmodulin-binding; Hydrolase; Iron; Metal-binding;
KW Mitochondrion; Phosphoprotein; Protein phosphatase; Reference proteome;
KW Zinc.
FT CHAIN 1..512
FT /note="Serine/threonine-protein phosphatase 2B catalytic
FT subunit gamma isoform"
FT /id="PRO_0000058828"
FT REGION 52..343
FT /note="Catalytic"
FT /evidence="ECO:0000305"
FT REGION 344..366
FT /note="Calcineurin B binding"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT REGION 386..400
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT REGION 401..408
FT /note="Autoinhibitory segment"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT REGION 459..481
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT REGION 471..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 303..307
FT /note="SAPNY motif"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT BINDING 86
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT BINDING 114
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 380
FT /note="E -> EDHYIPSYQK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045211"
FT VAR_SEQ 442..451
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1339277, ECO:0000303|Ref.2"
FT /id="VSP_037946"
FT VARIANT 501
FT /note="A -> V (in dbSNP:rs28764007)"
FT /id="VAR_061758"
FT CONFLICT 485..486
FT /note="HA -> YP (in Ref. 1; AAB23769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 58129 MW; 1C3AA7996660D575 CRC64;
MSGRRFHLST TDRVIKAVPF PPTQRLTFKE VFENGKPKVD VLKNHLVKEG RLEEEVALKI
INDGAAILRQ EKTMIEVDAP ITVCGDIHGQ FFDLMKLFEV GGSPSNTRYL FLGDYVDRGY
FSIECVLYLW SLKINHPKTL FLLRGNHECR HLTDYFTFKQ ECRIKYSEQV YDACMETFDC
LPLAALLNQQ FLCVHGGMSP EITSLDDIRK LDRFTEPPAF GPVCDLLWSD PSEDYGNEKT
LEHYTHNTVR GCSYFYSYPA VCEFLQNNNL LSIIRAHEAQ DAGYRMYRKS QATGFPSLIT
IFSAPNYLDV YNNKAAVLKY ENNVMNIRQF NCSPHPYWLP NFMDVFTWSL PFVGEKVTEM
LVNVLNICSD DELISDDEAE GSTTVRKEII RNKIRAIGKM ARVFSILRQE SESVLTLKGL
TPTGTLPLGV LSGGKQTIET ATVEAVEARE AIRGFSLQHK IRSFEEARGL DRINERMPPR
KDSIHAGGPM KSVTSAHSHA AHRSDQGKKA HS
