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Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit alpha isoform)

 PP2BA_HUMAN             Reviewed;         521 AA.
Q08209; A1A441; A8K3B7; A8W6Z7; A8W6Z8; B5BUA2; Q8TAW9;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 189.
RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;
EC=3.1.3.16;
AltName: Full=CAM-PRP catalytic subunit;
AltName: Full=Calmodulin-dependent calcineurin A subunit alpha isoform;
Name=PPP3CA; Synonyms=CALNA, CNA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=8392375; DOI=10.1016/0167-4889(93)90117-8;
Muramatsu T., Kincaid R.L.;
"Molecular cloning of a full-length cDNA encoding the catalytic
subunit of human calmodulin-dependent protein phosphatase (calcineurin
A alpha).";
Biochim. Biophys. Acta 1178:117-120(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND ALTERNATIVE
SPLICING.
PubMed=20590401; DOI=10.3109/10826084.2010.482449;
Chiocco M.J., Zhu X., Walther D., Pletnikova O., Troncoso J.C.,
Uhl G.R., Liu Q.R.;
"Fine mapping of calcineurin (PPP3CA) gene reveals novel alternative
splicing patterns, association of 5'UTR trinucleotide repeat with
addiction vulnerability, and differential isoform expression in
Alzheimer's disease.";
Subst. Use Misuse 45:1809-1826(2010).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
PubMed=21647268;
Landreville S., Lupien C.B., Vigneault F., Gaudreault M., Mathieu M.,
Rousseau A.P., Guerin S.L., Salesse C.;
"Identification of differentially expressed genes in uveal melanoma
using suppressive subtractive hybridization.";
Mol. Vis. 17:1324-1333(2011).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
INTERACTION WITH MYOZ1 AND MYOZ2.
PubMed=11114196; DOI=10.1073/pnas.260501097;
Frey N., Richardson J.A., Olson E.N.;
"Calsarcins, a novel family of sarcomeric calcineurin-binding
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000).
[11]
INTERACTION WITH MYOZ3.
PubMed=11842093; DOI=10.1074/jbc.M200712200;
Frey N., Olson E.N.;
"Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin
family, interacts with multiple Z-disc proteins.";
J. Biol. Chem. 277:13998-14004(2002).
[12]
INTERACTION WITH CRTC2.
PubMed=15454081; DOI=10.1016/j.cell.2004.09.015;
Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G.,
Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H.,
Okamoto M., Montminy M.;
"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive
coincidence detector.";
Cell 119:61-74(2004).
[13]
FUNCTION.
PubMed=15671020; DOI=10.1074/jbc.M411494200;
Wang Y., Shibasaki F., Mizuno K.;
"Calcium signal-induced cofilin dephosphorylation is mediated by
Slingshot via calcineurin.";
J. Biol. Chem. 280:12683-12689(2005).
[14]
INTERACTION WITH SYNPO2.
PubMed=17923693; DOI=10.1128/MCB.00950-07;
Faul C., Dhume A., Schecter A.D., Mundel P.;
"Protein kinase A, Ca2+/calmodulin-dependent kinase II, and
calcineurin regulate the intracellular trafficking of myopodin between
the Z-disc and the nucleus of cardiac myocytes.";
Mol. Cell. Biol. 27:8215-8227(2007).
[15]
INTERACTION WITH DMN1L, AND FUNCTION.
PubMed=18838687; DOI=10.1073/pnas.0808249105;
Cereghetti G.M., Stangherlin A., Martins de Brito O., Chang C.R.,
Blackstone C., Bernardi P., Scorrano L.;
"Dephosphorylation by calcineurin regulates translocation of Drp1 to
mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 105:15803-15808(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=8524402; DOI=10.1038/378641a0;
Kissinger C.R., Parge H.E., Knighton D.R., Lewis C.T., Pelletier L.A.,
Tempczyk A., Kalish V.J., Tucker K.D., Showalter R.E., Moomaw E.W.,
Gastinel L.N., Habuka N., Chen X., Maldonado F., Barker J.E.,
Bacquet R., Villafranca J.E.;
"Crystal structures of human calcineurin and the human FKBP12-FK506-
calcineurin complex.";
Nature 378:641-644(1995).
[20]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-380 IN COMPLEX WITH
SUBSTRATE PEPTIDE, FUNCTION, AND METAL-BINDING SITES.
PubMed=17498738; DOI=10.1016/j.jmb.2007.04.032;
Li H., Zhang L., Rao A., Harrison S.C., Hogan P.G.;
"Structure of calcineurin in complex with PVIVIT peptide: portrait of
a low-affinity signalling interaction.";
J. Mol. Biol. 369:1296-1306(2007).
-!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein
phosphatase. Many of the substrates contain a PxIxIT motif. This
subunit may have a role in the calmodulin activation of
calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.
{ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:17498738,
ECO:0000269|PubMed:18838687}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
Note=Binds 1 Fe(3+) ion per subunit.;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- SUBUNIT: Interacts with CIB1; the interaction increases upon
cardiomyocytes hypertrophy (By similarity). Interacts with CHP1
and CHP2 (By similarity). Composed of two components (A and B),
the A component is the catalytic subunit and the B component
confers calcium sensitivity. Interacts with CRTC2, MYOZ1, MYOZ2
and MYOZ3. Interacts with DNM1L; the interaction dephosphorylates
DNM1L and regulates its translocation to mitochondria. Interacts
with CMYA5; this interaction represses calcineurin activity in
muscle (By similarity). Interacts (constitutively active form)
with SYNPO2 (PubMed:17923693). {ECO:0000250,
ECO:0000269|PubMed:17923693}.
-!- INTERACTION:
P24588:AKAP5; NbExp=6; IntAct=EBI-15637215, EBI-703640;
R4GN89:C16orf74; NbExp=3; IntAct=EBI-352922, EBI-10225238;
Q8VHW5:Cacng8 (xeno); NbExp=2; IntAct=EBI-352922, EBI-9086576;
P62993:GRB2; NbExp=3; IntAct=EBI-352922, EBI-401755;
O36972:Mal-047 (xeno); NbExp=2; IntAct=EBI-15637215, EBI-16039701;
O95644:NFATC1; NbExp=4; IntAct=EBI-15637215, EBI-6907210;
Q13469:NFATC2; NbExp=2; IntAct=EBI-15637215, EBI-716258;
P63098:PPP3R1; NbExp=7; IntAct=EBI-15637215, EBI-915984;
P54578:USP14; NbExp=3; IntAct=EBI-352922, EBI-1048016;
P46939:UTRN; NbExp=3; IntAct=EBI-15637215, EBI-295856;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cell membrane,
sarcolemma {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes
with ACTN1 and MYOZ2 at the Z line in heart and skeletal muscle.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q08209-1; Sequence=Displayed;
Name=2;
IsoId=Q08209-2; Sequence=VSP_018562;
Name=3;
IsoId=Q08209-3; Sequence=VSP_043378, VSP_018562;
Name=4;
IsoId=Q08209-4; Sequence=VSP_047755;
Name=5;
IsoId=Q08209-5; Sequence=VSP_054467;
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Calcineurin entry;
URL="https://en.wikipedia.org/wiki/Calcineurin";
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EMBL; L14778; AAA02631.1; -; mRNA.
EMBL; EU192652; ABW74484.1; -; mRNA.
EMBL; EU192653; ABW74485.1; -; mRNA.
EMBL; AY904364; AAY17314.1; -; mRNA.
EMBL; AK290532; BAF83221.1; -; mRNA.
EMBL; AL353950; CAB89253.1; -; mRNA.
EMBL; AB451338; BAG70152.1; -; mRNA.
EMBL; AB451487; BAG70301.1; -; mRNA.
EMBL; AC092671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471057; EAX06125.1; -; Genomic_DNA.
EMBL; CH471057; EAX06124.1; -; Genomic_DNA.
EMBL; BC025714; AAH25714.1; -; mRNA.
CCDS; CCDS34037.1; -. [Q08209-1]
CCDS; CCDS47113.1; -. [Q08209-3]
CCDS; CCDS47114.1; -. [Q08209-2]
PIR; S35067; S35067.
RefSeq; NP_000935.1; NM_000944.4. [Q08209-1]
RefSeq; NP_001124163.1; NM_001130691.1. [Q08209-2]
RefSeq; NP_001124164.1; NM_001130692.1. [Q08209-3]
UniGene; Hs.435512; -.
PDB; 1AUI; X-ray; 2.10 A; A=1-521.
PDB; 1M63; X-ray; 2.80 A; A/E=1-372.
PDB; 1MF8; X-ray; 3.10 A; A=20-392.
PDB; 2JOG; NMR; -; A=21-347.
PDB; 2JZI; NMR; -; B=391-414.
PDB; 2P6B; X-ray; 2.30 A; A/C=1-380.
PDB; 2R28; X-ray; 1.86 A; C/D=389-413.
PDB; 2W73; X-ray; 1.45 A; K/L/M/O=395-411.
PDB; 3LL8; X-ray; 2.00 A; A/C=14-370.
PDB; 4F0Z; X-ray; 1.70 A; A=1-370.
PDB; 4Q5U; X-ray; 1.95 A; C=391-414.
PDB; 5C1V; X-ray; 3.35 A; A/B=2-346.
PDB; 5SVE; X-ray; 2.60 A; A=1-370.
PDBsum; 1AUI; -.
PDBsum; 1M63; -.
PDBsum; 1MF8; -.
PDBsum; 2JOG; -.
PDBsum; 2JZI; -.
PDBsum; 2P6B; -.
PDBsum; 2R28; -.
PDBsum; 2W73; -.
PDBsum; 3LL8; -.
PDBsum; 4F0Z; -.
PDBsum; 4Q5U; -.
PDBsum; 5C1V; -.
PDBsum; 5SVE; -.
DisProt; DP00092; -.
ProteinModelPortal; Q08209; -.
SMR; Q08209; -.
BioGrid; 111522; 68.
CORUM; Q08209; -.
DIP; DIP-6095N; -.
ELM; Q08209; -.
IntAct; Q08209; 24.
MINT; MINT-1037516; -.
STRING; 9606.ENSP00000378323; -.
BindingDB; Q08209; -.
ChEMBL; CHEMBL4445; -.
DrugBank; DB08231; MYRISTIC ACID.
DEPOD; Q08209; -.
iPTMnet; Q08209; -.
PhosphoSitePlus; Q08209; -.
SwissPalm; Q08209; -.
BioMuta; PPP3CA; -.
DMDM; 1352673; -.
EPD; Q08209; -.
MaxQB; Q08209; -.
PaxDb; Q08209; -.
PeptideAtlas; Q08209; -.
PRIDE; Q08209; -.
DNASU; 5530; -.
Ensembl; ENST00000323055; ENSP00000320580; ENSG00000138814. [Q08209-3]
Ensembl; ENST00000394853; ENSP00000378322; ENSG00000138814. [Q08209-2]
Ensembl; ENST00000394854; ENSP00000378323; ENSG00000138814. [Q08209-1]
Ensembl; ENST00000512215; ENSP00000422781; ENSG00000138814. [Q08209-4]
GeneID; 5530; -.
KEGG; hsa:5530; -.
UCSC; uc003hvu.3; human. [Q08209-1]
CTD; 5530; -.
DisGeNET; 5530; -.
EuPathDB; HostDB:ENSG00000138814.16; -.
GeneCards; PPP3CA; -.
HGNC; HGNC:9314; PPP3CA.
HPA; CAB018581; -.
HPA; HPA012778; -.
MIM; 114105; gene.
neXtProt; NX_Q08209; -.
OpenTargets; ENSG00000138814; -.
PharmGKB; PA33678; -.
eggNOG; KOG0375; Eukaryota.
eggNOG; COG0639; LUCA.
GeneTree; ENSGT00530000063087; -.
HOGENOM; HOG000172699; -.
HOVERGEN; HBG002819; -.
InParanoid; Q08209; -.
KO; K04348; -.
OMA; LWSLKIW; -.
OrthoDB; EOG091G094R; -.
PhylomeDB; Q08209; -.
TreeFam; TF105557; -.
Reactome; R-HSA-180024; DARPP-32 events.
Reactome; R-HSA-2025928; Calcineurin activates NFAT.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
SIGNOR; Q08209; -.
ChiTaRS; PPP3CA; human.
EvolutionaryTrace; Q08209; -.
GeneWiki; PPP3CA; -.
GenomeRNAi; 5530; -.
PMAP-CutDB; Q08209; -.
PRO; PR:Q08209; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138814; -.
CleanEx; HS_PPP3CA; -.
ExpressionAtlas; Q08209; baseline and differential.
Genevisible; Q08209; HS.
GO; GO:0005955; C:calcineurin complex; IDA:CAFA.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IDA:UniProtKB.
GO; GO:0016018; F:cyclosporin A binding; IDA:CAFA.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; NAS:UniProtKB.
GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IDA:BHF-UCL.
GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IDA:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0016311; P:dephosphorylation; TAS:UniProtKB.
GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
GO; GO:0033555; P:multicellular organismal response to stress; IEA:Ensembl.
GO; GO:0035562; P:negative regulation of chromatin binding; IEA:Ensembl.
GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:Ensembl.
GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IEA:Ensembl.
GO; GO:1903244; P:positive regulation of cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
GO; GO:1905205; P:positive regulation of connective tissue replacement; IEA:Ensembl.
GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
GO; GO:0051533; P:positive regulation of NFAT protein import into nucleus; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
Pfam; PF00149; Metallophos; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
SUPFAM; SSF56300; SSF56300; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Calmodulin-binding;
Cell membrane; Complete proteome; Hydrolase; Iron; Membrane;
Metal-binding; Nitration; Nucleus; Phosphoprotein;
Protein phosphatase; Reference proteome; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 521 Serine/threonine-protein phosphatase 2B
catalytic subunit alpha isoform.
/FTId=PRO_0000058822.
REGION 2 301 Catalytic.
REGION 247 253 Calcineurin B binding-site 1.
{ECO:0000255}.
REGION 296 301 Calcineurin B binding-site 2.
{ECO:0000255}.
REGION 392 414 Calmodulin-binding. {ECO:0000255}.
REGION 465 487 Inhibitory domain.
ACT_SITE 151 151 Proton donor. {ECO:0000250}.
METAL 90 90 Iron.
METAL 92 92 Iron.
METAL 118 118 Iron.
METAL 118 118 Zinc.
METAL 150 150 Zinc.
METAL 199 199 Zinc.
METAL 281 281 Zinc.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 224 224 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P63328}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000250|UniProtKB:P63329}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 20 86 Missing (in isoform 5).
{ECO:0000303|PubMed:21647268}.
/FTId=VSP_054467.
VAR_SEQ 87 318 Missing (in isoform 4).
{ECO:0000303|PubMed:20590401}.
/FTId=VSP_047755.
VAR_SEQ 318 359 Missing (in isoform 3).
{ECO:0000303|PubMed:20590401}.
/FTId=VSP_043378.
VAR_SEQ 448 457 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:20590401}.
/FTId=VSP_018562.
STRAND 13 15 {ECO:0000244|PDB:5SVE}.
HELIX 31 34 {ECO:0000244|PDB:4F0Z}.
HELIX 43 51 {ECO:0000244|PDB:4F0Z}.
HELIX 58 73 {ECO:0000244|PDB:4F0Z}.
STRAND 77 81 {ECO:0000244|PDB:4F0Z}.
STRAND 83 88 {ECO:0000244|PDB:4F0Z}.
HELIX 95 105 {ECO:0000244|PDB:4F0Z}.
TURN 108 110 {ECO:0000244|PDB:3LL8}.
STRAND 113 115 {ECO:0000244|PDB:4F0Z}.
STRAND 120 123 {ECO:0000244|PDB:4F0Z}.
HELIX 126 139 {ECO:0000244|PDB:4F0Z}.
TURN 141 143 {ECO:0000244|PDB:4F0Z}.
STRAND 144 146 {ECO:0000244|PDB:4F0Z}.
HELIX 154 159 {ECO:0000244|PDB:4F0Z}.
HELIX 162 169 {ECO:0000244|PDB:4F0Z}.
HELIX 172 183 {ECO:0000244|PDB:4F0Z}.
STRAND 188 191 {ECO:0000244|PDB:4F0Z}.
TURN 192 194 {ECO:0000244|PDB:4F0Z}.
STRAND 195 200 {ECO:0000244|PDB:4F0Z}.
STRAND 206 208 {ECO:0000244|PDB:2JOG}.
HELIX 210 213 {ECO:0000244|PDB:4F0Z}.
STRAND 218 220 {ECO:0000244|PDB:4F0Z}.
STRAND 223 225 {ECO:0000244|PDB:4F0Z}.
HELIX 226 232 {ECO:0000244|PDB:4F0Z}.
TURN 237 240 {ECO:0000244|PDB:4F0Z}.
STRAND 247 250 {ECO:0000244|PDB:4F0Z}.
TURN 252 254 {ECO:0000244|PDB:4F0Z}.
STRAND 255 260 {ECO:0000244|PDB:4F0Z}.
HELIX 262 271 {ECO:0000244|PDB:4F0Z}.
STRAND 276 279 {ECO:0000244|PDB:4F0Z}.
STRAND 287 290 {ECO:0000244|PDB:4F0Z}.
TURN 295 297 {ECO:0000244|PDB:4F0Z}.
STRAND 298 306 {ECO:0000244|PDB:4F0Z}.
HELIX 311 313 {ECO:0000244|PDB:4F0Z}.
STRAND 319 325 {ECO:0000244|PDB:4F0Z}.
STRAND 328 334 {ECO:0000244|PDB:4F0Z}.
HELIX 344 346 {ECO:0000244|PDB:4F0Z}.
HELIX 349 369 {ECO:0000244|PDB:4F0Z}.
HELIX 396 409 {ECO:0000244|PDB:2W73}.
HELIX 470 477 {ECO:0000244|PDB:1AUI}.
HELIX 478 481 {ECO:0000244|PDB:1AUI}.
SEQUENCE 521 AA; 58688 MW; 16480D62DDBF1F40 CRC64;
MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEESV
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 KALTSETNGT DSNGSNSSNI Q


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