ID PP1G_HUMAN STANDARD; PRT; 323 AA. AC P36873; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE Serine/threonine protein phosphatase PP1-gamma catalytic subunit DE (EC 3.1.3.16) (PP-1G) (Protein phosphatase 1C catalytic subunit). GN Name=PPP1CC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORMS GAMMA-1 AND GAMMA-2). RX MEDLINE=93349989; PubMed=8394140; DOI=10.1016/0167-4889(93)90014-G; RA Barker H.M., Craig S.P., Spurr N.K., Cohen P.T.W.; RT "Sequence of human protein serine/threonine phosphatase 1 gamma and RT localization of the gene (PPP1CC) encoding it to chromosome bands RT 12q24.1-q24.2."; RL Biochim. Biophys. Acta 1178:228-233(1993). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORM GAMMA-1). RC TISSUE=Placenta; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [3] RP NUCLEOTIDE SEQUENCE OF 5-323 (ISOFORM GAMMA-1). RC TISSUE=Skeletal muscle; RX MEDLINE=94154385; PubMed=8111128; RA Norman S.A., Mott D.M.; RT "Molecular cloning and chromosomal localization of a human skeletal RT muscle PP-1 gamma 1 cDNA."; RL Mamm. Genome 5:41-45(1994). RN [4] RP INTERACTION WITH MICROCYSTIN, AND MUTAGENESIS OF CYS-273. RX PubMed=7556599; RA MacKintosh R.W., Dalby K.N., Campbell D.G., Cohen P.T., Cohen P.T.W., RA MacKintosh C.; RT "The cyanobacterial toxin microcystin binds covalently to cysteine-273 RT on protein phosphatase 1."; RL FEBS Lett. 371:236-240(1995). RN [5] RP INTERACTION WITH PPP1R3D. RX MEDLINE=98074939; PubMed=9414128; DOI=10.1016/S0014-5793(97)01385-9; RA Armstrong C.G., Browne G.J., Cohen P., Cohen P.T.W.; RT "PPP1R6, a novel member of the family of glycogen-targetting subunits RT of protein phosphatase 1."; RL FEBS Lett. 418:210-214(1998). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX MEDLINE=96107380; PubMed=7500362; RA Egloff M.-P., Cohen P.T.W., Reinemer P., Barford D.; RT "Crystal structure of the catalytic subunit of human protein RT phosphatase 1 and its complex with tungstate."; RL J. Mol. Biol. 254:942-959(1995). CC -!- FUNCTION: Protein phosphatase 1 (PP1) is essential for cell CC division, and participates in the regulation of glycogen CC metabolism, muscle contractility and protein synthesis. Involved CC in regulation of ionic conductances and long-term synaptic CC plasticity. May play an important role in dephosphorylating CC substrates such as the postsynaptic density-associated CC Ca(2+)/calmodulin dependent protein kinase II. CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein + CC phosphate. CC -!- COFACTOR: Binds 1 iron ion and 1 manganese ion per subunit. CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or CC PPP1CC, which is folded into its native form by inhibitor 2 and CC glycogen synthetase kinase 3, and then complexed to one or several CC targeting or regulatory subunits. PPP1R12A and PPP1R12B mediate CC binding to myosin. PPP1R3A, PPP1R3B, PPP1R3C and PPP1R3D mediate CC binding to glycogen. Interacts with cyanobacterial toxin CC microcystin; disulfide-linked. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Gamma-1; CC IsoId=P36873-1; Sequence=Displayed; CC Name=Gamma-2; CC IsoId=P36873-2; Sequence=VSP_005094; CC -!- MISCELLANEOUS: Microcystin toxin is bound to Cys-273 through a CC thioether bond. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily. CC -!- DATABASE: NAME=Protein Spotlight; NOTE=Issue 32 of March 2003; CC WWW="http://www.expasy.org/spotlight/back_issues/sptlt032.shtml". 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 EMBL; X74008; CAA52169.1; -. DR EMBL; BC014073; AAH14073.1; -. DR EMBL; L07395; AAA19823.1; -. DR PIR; S35699; S35699. DR PIR; S35700; S35700. DR PDB; 1IT6; X-ray; A/B=1-323. DR PDB; 1JK7; X-ray; A=1-323. DR IntAct; P36873; -. DR Ensembl; ENSG00000186298; Homo sapiens. DR Genew; HGNC:9283; PPP1CC. DR H-InvDB; HIX0019358; -. DR MIM; 176914; -. DR InterPro; IPR004843; M-pesterase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR ProDom; PD000252; T_phtase_apaH; 1. DR SMART; SM00156; PP2Ac; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. KW 3D-structure; Alternative splicing; Carbohydrate metabolism; KW Cell cycle; Cell division; Glycogen metabolism; Hydrolase; Iron; KW Manganese; Metal-binding; Multigene family; Protein phosphatase. FT SITE 273 273 Inhibition by microcystin toxin binding. FT METAL 64 64 Iron. FT METAL 66 66 Iron. FT METAL 92 92 Iron and manganese. FT METAL 124 124 Manganese. FT ACT_SITE 125 125 Proton donor. FT METAL 173 173 Manganese. FT METAL 248 248 Manganese. FT VARSPLIC 315 323 GMITKQAKK -> VASGLNPSIQKASNYRNNTVLYE (in FT isoform Gamma-2). FT /FTId=VSP_005094. FT MUTAGEN 273 273 C->A,S,L: Abolishes interaction with FT microcystin toxin. FT HELIX 9 18 FT TURN 19 21 FT TURN 24 25 FT HELIX 32 48 FT STRAND 52 55 FT STRAND 59 62 FT STRAND 64 64 FT TURN 66 67 FT HELIX 69 79 FT TURN 82 83 FT STRAND 87 89 FT HELIX 100 113 FT TURN 115 117 FT STRAND 118 120 FT TURN 124 125 FT HELIX 128 131 FT TURN 132 133 FT HELIX 136 143 FT HELIX 146 156 FT TURN 157 158 FT STRAND 162 165 FT TURN 166 168 FT STRAND 169 172 FT TURN 178 179 FT HELIX 183 187 FT TURN 188 188 FT HELIX 200 206 FT STRAND 208 209 FT TURN 211 212 FT STRAND 216 218 FT TURN 220 221 FT STRAND 225 227 FT HELIX 229 239 FT TURN 240 240 FT STRAND 243 246 FT TURN 252 253 FT STRAND 255 258 FT TURN 259 262 FT STRAND 263 267 FT TURN 270 271 FT HELIX 272 274 FT TURN 275 275 FT STRAND 280 285 FT TURN 287 288 FT STRAND 291 296 SQ SEQUENCE 323 AA; 36984 MW; 0EEEF0E842188536 CRC64; MADLDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE KKKPNATRPV TPPRGMITKQ AKK //