ID G1NFJ1_MELGA Unreviewed; 501 AA. AC G1NFJ1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 02-JUN-2021, entry version 64. DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273}; DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273}; GN Name=PPP3CA {ECO:0000313|Ensembl:ENSMGAP00000011783}; OS Meleagris gallopavo (Wild turkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Meleagridinae; Meleagris. OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000011783, ECO:0000313|Proteomes:UP000001645}; RN [1] {ECO:0000313|Ensembl:ENSMGAP00000011783, ECO:0000313|Proteomes:UP000001645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475; RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A., RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K., RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C., RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A., RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P., RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T., RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M., RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D., RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C., RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J., RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P., RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X., RA Zhang Y., Reed K.M.; RT "Multi-platform next-generation sequencing of the domestic turkey RT (Meleagris gallopavo): genome assembly and analysis."; RL PLoS Biol. 8:E1000475-E1000475(2010). RN [2] {ECO:0000313|Ensembl:ENSMGAP00000011783} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. 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:0000256|ARBA:ARBA00001512}; 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:0000256|ARBA:ARBA00001482, CC ECO:0000256|RuleBase:RU004273}; CC -!- COFACTOR: CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; CC Evidence={ECO:0000256|ARBA:ARBA00001965}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SIMILARITY: Belongs to the PPP phosphatase family. CC {ECO:0000256|RuleBase:RU004273}. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily. CC {ECO:0000256|ARBA:ARBA00009905}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR Ensembl; ENSMGAT00000012664; ENSMGAP00000011783; ENSMGAG00000011269. DR GeneTree; ENSGT00940000156306; -. DR InParanoid; G1NFJ1; -. DR OMA; KPHGGHT; -. DR TreeFam; TF105557; -. DR Proteomes; UP000001645; Chromosome 4. DR GO; GO:0005955; C:calcineurin complex; IEA:Ensembl. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0030018; C:Z disc; IEA:Ensembl. DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IEA:Ensembl. DR GO; GO:0016018; F:cyclosporin A binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046983; F:protein dimerization activity; IEA:Ensembl. DR GO; GO:0106306; F:protein serine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0106307; F:protein threonine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IEA:Ensembl. DR GO; GO:0006816; P:calcium ion transport; IEA:Ensembl. DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl. DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0033555; P:multicellular organismal response to stress; IEA:Ensembl. DR GO; GO:0035562; P:negative regulation of chromatin binding; IEA:Ensembl. DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:Ensembl. DR GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IEA:Ensembl. DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IEA:Ensembl. DR GO; GO:1903244; P:positive regulation of cardiac muscle hypertrophy in response to stress; IEA:Ensembl. DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl. DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl. DR GO; GO:1905205; P:positive regulation of connective tissue replacement; IEA:Ensembl. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl. DR GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl. DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl. DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl. DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl. DR GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl. 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 PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. PE 3: Inferred from homology; KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}; KW Reference proteome {ECO:0000313|Proteomes:UP000001645}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 128..133 FT /note="SER_THR_PHOSPHATASE" FT /evidence="ECO:0000259|PROSITE:PS00125" FT REGION 461..501 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 473..501 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 501 AA; 56501 MW; 69E20846C67AF74F CRC64; AVPFPPSHRL TAKEVFDNDG KPRVDILKAH LMKEGRLEES VALRIITEGA SILRQEKNLL DIDAPVTVCG DIHGQFFDLM KLFEVGGSPA NTRYLFLGDY VDRGYFSIEC VLYLWALKIL YPKTLFLLRG NHECRHLTEY FTFKQECKIK YSERVYDACM DAFDCLPLAA LMNQQFLCVH GGLSPEINTL DDIRKLDRFK EPPAYGPMCD ILWSDPLEDF GNEKTQEHFT HNTVRGCSYF YSYPAVCEFL QHNNLLSILR AHEAQDAGYR MYRKSQTTGF PSLITIFSAP NYLDVYNNKA AVLKYENNVM NIRQFNCSPH PYWLPNFMDV FTWSLPFVGE KVTEMLVNVL NICSDDELGT EEDGFDGATA AARKEVIRNK IRAIGKMARV FSVLREESES VLTLKGLTPT GMLPSGVLSG GKQTLQSATV EAIEADEAIK GFSPQHKITS FEEAKGLDRI NERMPPRRDV PSDANLNSIN KAISTETNGT DSNGSNSSNI Q //