ID G1NFJ1_MELGA Unreviewed; 470 AA. AC G1NFJ1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 2. DT 19-JAN-2022, entry version 66. 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. 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; MESFCCL; -. 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: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 SUPFAM; SSF56300; SSF56300; 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 Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}; KW Reference proteome {ECO:0000313|Proteomes:UP000001645}. FT DOMAIN 97..102 FT /note="SER_THR_PHOSPHATASE" FT /evidence="ECO:0000259|PROSITE:PS00125" FT REGION 430..470 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 442..470 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 470 AA; 53050 MW; AFF2C6FBAAAF1FCA CRC64; 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 ICSDDELGTE EDGFDGATAA ARKEVIRNKI RAIGKMARVF SVLREESESV LTLKGLTPTG MLPSGVLSGG KQTLQSATVE AIEADEAIKG FSPQHKITSF EEAKGLDRIN ERMPPRRDVP SDANLNSINK AISTETNGTD SNGSNSSNIQ //