PP1G_HUMAN
ID PP1G_HUMAN Reviewed; 323 AA.
AC P36873;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 241.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-gamma catalytic subunit;
DE Short=PP-1G;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 1C catalytic subunit;
GN Name=PPP1CC;
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] (ISOFORMS 1 AND 2).
RX 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 12q24.1-
RT q24.2.";
RL Biochim. Biophys. Acta 1178:228-233(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [3]
RP PROTEIN SEQUENCE OF 2-15; 44-60; 99-122; 151-168 AND 247-260, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 2-15; 27-36; 44-60; 99-111; 133-141; 151-187 AND
RP 239-260, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Bilsland A.E., Keith W.N.;
RL Submitted (JAN-2010) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-323 (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=8111128; DOI=10.1007/bf00360567;
RA Norman S.A., Mott D.M.;
RT "Molecular cloning and chromosomal localization of a human skeletal muscle
RT PP-1 gamma 1 cDNA.";
RL Mamm. Genome 5:41-45(1994).
RN [6]
RP INTERACTION WITH MICROCYSTIN, AND MUTAGENESIS OF CYS-273.
RX PubMed=7556599; DOI=10.1016/0014-5793(95)00888-g;
RA MacKintosh R.W., Dalby K.N., Campbell D.G., Cohen P.T.W., Cohen P.,
RA MacKintosh C.;
RT "The cyanobacterial toxin microcystin binds covalently to cysteine-273 on
RT protein phosphatase 1.";
RL FEBS Lett. 371:236-240(1995).
RN [7]
RP INTERACTION WITH PPP1R3D.
RX 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-targeting subunits of
RT protein phosphatase 1.";
RL FEBS Lett. 418:210-214(1997).
RN [8]
RP SUBCELLULAR LOCATION, INTERACTION WITH PPP1R8, AND MUTAGENESIS OF HIS-125.
RX PubMed=11739654; DOI=10.1242/jcs.114.23.4219;
RA Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.;
RT "Dynamic targeting of protein phosphatase 1 within the nuclei of living
RT mammalian cells.";
RL J. Cell Sci. 114:4219-4228(2001).
RN [9]
RP INTERACTION WITH PPP1R15A.
RX PubMed=11564868; DOI=10.1128/mcb.21.20.6841-6850.2001;
RA Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.;
RT "Growth arrest and DNA damage-inducible protein GADD34 assembles a novel
RT signaling complex containing protein phosphatase 1 and inhibitor 1.";
RL Mol. Cell. Biol. 21:6841-6850(2001).
RN [10]
RP INTERACTION WITH PPP1R7.
RX PubMed=12226088; DOI=10.1074/jbc.m206838200;
RA Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W.,
RA Bollen M.;
RT "Binding of the concave surface of the Sds22 superhelix to the alpha
RT 4/alpha 5/alpha 6-triangle of protein phosphatase-1.";
RL J. Biol. Chem. 277:47331-47337(2002).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=12529430; DOI=10.1091/mbc.e02-07-0376;
RA Trinkle-Mulcahy L., Andrews P.D., Wickramasinghe S., Sleeman J.,
RA Prescott A., Lam Y.W., Lyon C., Swedlow J.R., Lamond A.I.;
RT "Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout
RT the mammalian cell cycle.";
RL Mol. Biol. Cell 14:107-117(2003).
RN [12]
RP INTERACTION WITH NEK2, AND PHOSPHORYLATION.
RX PubMed=15659832; DOI=10.1196/annals.1329.059;
RA Fardilha M., Wu W., Sa R., Fidalgo S., Sousa C., Mota C.,
RA da Cruz e Silva O.A., da Cruz e Silva E.F.;
RT "Alternatively spliced protein variants as potential therapeutic targets
RT for male infertility and contraception.";
RL Ann. N. Y. Acad. Sci. 1030:468-478(2004).
RN [13]
RP ACTIVITY REGULATION.
RX PubMed=15705855; DOI=10.1126/science.1101902;
RA Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D.,
RA Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.;
RT "A selective inhibitor of eIF2alpha dephosphorylation protects cells from
RT ER stress.";
RL Science 307:935-939(2005).
RN [14]
RP INTERACTION WITH CDCA2.
RX PubMed=16492807; DOI=10.1083/jcb.200508154;
RA Trinkle-Mulcahy L., Andersen J., Lam Y.W., Moorhead G., Mann M.,
RA Lamond A.I.;
RT "Repo-Man recruits PP1 gamma to chromatin and is essential for cell
RT viability.";
RL J. Cell Biol. 172:679-692(2006).
RN [15]
RP INTERACTION WITH NEK2.
RX PubMed=17283141; DOI=10.1158/0008-5472.can-06-3071;
RA Mi J., Guo C., Brautigan D.L., Larner J.M.;
RT "Protein phosphatase-1alpha regulates centrosome splitting through Nek2.";
RL Cancer Res. 67:1082-1089(2007).
RN [16]
RP FUNCTION IN DEPHOSPHORYLATION OF RPS6KB1, ACTIVITY REGULATION, INTERACTION
RP WITH URI1, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17936702; DOI=10.1016/j.molcel.2007.08.010;
RA Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M.,
RA Aebersold R., Hess D., Krek W.;
RT "S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes
RT activates a negative feedback program that counters S6K1 survival
RT signaling.";
RL Mol. Cell 28:28-40(2007).
RN [17]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NOM1.
RX PubMed=17965019; DOI=10.1074/jbc.m706708200;
RA Gunawardena S.R., Ruis B.L., Meyer J.A., Kapoor M., Conklin K.F.;
RT "NOM1 targets protein phosphatase I to the nucleolus.";
RL J. Biol. Chem. 283:398-404(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP CAUTION.
RX PubMed=19377461; DOI=10.1038/nature07954;
RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
RA Kitagawa H., Kato S.;
RT "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced
RT granulopoiesis.";
RL Nature 459:455-459(2009).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP CAUTION, AND RETRACTION NOTICE OF PUBMED:24275569.
RX PubMed=24336203; DOI=10.1038/nature12896;
RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
RA Kitagawa H., Kato S.;
RT "Retraction: GlcNAcylation of a histone methyltransferase in retinoic-acid-
RT induced granulopoiesis.";
RL Nature 505:574-574(2014).
RN [25]
RP IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, AND
RP INTERACTION WITH PPP1R8.
RX PubMed=20516061; DOI=10.1074/jbc.m110.109801;
RA Lee J.H., You J., Dobrota E., Skalnik D.G.;
RT "Identification and characterization of a novel human PP1 phosphatase
RT complex.";
RL J. Biol. Chem. 285:24466-24476(2010).
RN [26]
RP INTERACTION WITH RRP1B, AND SUBCELLULAR LOCATION.
RX PubMed=20926688; DOI=10.1091/mbc.e10-04-0287;
RA Chamousset D., De Wever V., Moorhead G.B., Chen Y., Boisvert F.M.,
RA Lamond A.I., Trinkle-Mulcahy L.;
RT "RRP1B targets PP1 to mammalian cell nucleoli and is associated with pre-
RT 60S ribosomal subunits.";
RL Mol. Biol. Cell 21:4212-4226(2010).
RN [27]
RP FUNCTION IN CIRCADIAN CLOCK.
RX PubMed=21712997; DOI=10.1371/journal.pone.0021325;
RA Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.;
RT "Protein phosphatase 1 (PP1) is a post-translational regulator of the
RT mammalian circadian clock.";
RL PLoS ONE 6:E21325-E21325(2011).
RN [28]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DYNLT4.
RX PubMed=23789093; DOI=10.1242/bio.20131065;
RA Korrodi-Gregorio L., Vieira S.I., Esteves S.L., Silva J.V., Freitas M.J.,
RA Brauns A.K., Luers G., Abrantes J., Esteves P.J., da Cruz e Silva O.A.,
RA Fardilha M., da Cruz e Silva E.F.;
RT "TCTEX1D4, a novel protein phosphatase 1 interactor: connecting the
RT phosphatase to the microtubule network.";
RL Biol. Open 2:453-465(2013).
RN [29]
RP INTERACTION WITH PPP1R2B.
RX PubMed=23506001; DOI=10.1186/1471-2121-14-15;
RA Korrodi-Gregorio L., Ferreira M., Vintem A.P., Wu W., Muller T., Marcus K.,
RA Vijayaraghavan S., Brautigan D.L., da Cruz E Silva O.A., Fardilha M.,
RA da Cruz E Silva E.F.;
RT "Identification and characterization of two distinct PPP1R2 isoforms in
RT human spermatozoa.";
RL BMC Cell Biol. 14:15-15(2013).
RN [30]
RP INTERACTION WITH PPP1CA, PEAK1 AND SHC1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=23846654; DOI=10.1038/nature12308;
RA Zheng Y., Zhang C., Croucher D.R., Soliman M.A., St-Denis N.,
RA Pasculescu A., Taylor L., Tate S.A., Hardy W.R., Colwill K., Dai A.Y.,
RA Bagshaw R., Dennis J.W., Gingras A.C., Daly R.J., Pawson T.;
RT "Temporal regulation of EGF signalling networks by the scaffold protein
RT Shc1.";
RL Nature 499:166-171(2013).
RN [31]
RP FUNCTION, INTERACTION WITH FOXP3, AND INDUCTION.
RX PubMed=23396208; DOI=10.1038/nm.3085;
RA Nie H., Zheng Y., Li R., Guo T.B., He D., Fang L., Liu X., Xiao L.,
RA Chen X., Wan B., Chin Y.E., Zhang J.Z.;
RT "Phosphorylation of FOXP3 controls regulatory T cell function and is
RT inhibited by TNF-alpha in rheumatoid arthritis.";
RL Nat. Med. 19:322-328(2013).
RN [32]
RP INTERACTION WITH MKI67.
RX PubMed=24867636; DOI=10.7554/elife.01641;
RA Booth D.G., Takagi M., Sanchez-Pulido L., Petfalski E., Vargiu G.,
RA Samejima K., Imamoto N., Ponting C.P., Tollervey D., Earnshaw W.C.,
RA Vagnarelli P.;
RT "Ki-67 is a PP1-interacting protein that organises the mitotic chromosome
RT periphery.";
RL Elife 3:E01641-E01641(2014).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=7500362; DOI=10.1006/jmbi.1995.0667;
RA Egloff M.-P., Cohen P.T.W., Reinemer P., Barford D.;
RT "Crystal structure of the catalytic subunit of human protein phosphatase 1
RT and its complex with tungstate.";
RL J. Mol. Biol. 254:942-959(1995).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE, AND
RP COFACTOR.
RX PubMed=11535607; DOI=10.1074/jbc.m107656200;
RA Maynes J.T., Bateman K.S., Cherney M.M., Das A.K., Luu H.A., Holmes C.F.,
RA James M.N.;
RT "Crystal structure of the tumor-promoter okadaic acid bound to protein
RT phosphatase-1.";
RL J. Biol. Chem. 276:44078-44082(2001).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-298 IN COMPLEX WITH MANGANESE,
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=15280359; DOI=10.1074/jbc.m407184200;
RA Maynes J.T., Perreault K.R., Cherney M.M., Luu H.A., James M.N.,
RA Holmes C.F.;
RT "Crystal structure and mutagenesis of a protein phosphatase-1:calcineurin
RT hybrid elucidate the role of the beta12-beta13 loop in inhibitor binding.";
RL J. Biol. Chem. 279:43198-43206(2004).
CC -!- FUNCTION: Protein phosphatase that associates with over 200 regulatory
CC proteins to form highly specific holoenzymes which dephosphorylate
CC hundreds of biological targets. Protein phosphatase 1 (PP1) is
CC essential for cell division, and participates in the regulation of
CC glycogen metabolism, muscle contractility and protein synthesis.
CC Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances
CC and long-term synaptic plasticity. May play an important role in
CC dephosphorylating substrates such as the postsynaptic density-
CC associated Ca(2+)/calmodulin dependent protein kinase II. Component of
CC the PTW/PP1 phosphatase complex, which plays a role in the control of
CC chromatin structure and cell cycle progression during the transition
CC from mitosis into interphase. In balance with CSNK1D and CSNK1E,
CC determines the circadian period length, through the regulation of the
CC speed and rhythmicity of PER1 and PER2 phosphorylation. May
CC dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418'
CC residue of FOXP3 in regulatory T-cells (Treg) from patients with
CC rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg
CC cells functionally defective (PubMed:23396208).
CC {ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:20516061,
CC ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208}.
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:15280359};
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:15280359};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11535607, ECO:0000269|PubMed:15280359};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:11535607,
CC ECO:0000269|PubMed:15280359};
CC -!- ACTIVITY REGULATION: Inactivated by binding to URI1. The phosphatase
CC activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically
CC inhibited by Salubrinal, a drug that protects cells from endoplasmic
CC reticulum stress. {ECO:0000269|PubMed:15705855,
CC ECO:0000269|PubMed:17936702}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC which is folded into its native form by inhibitor 2 and glycogen
CC synthetase kinase 3, and then complexed to one or several targeting or
CC regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to
CC myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C,
CC PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts
CC with cyanobacterial toxin microcystin; disulfide-linked. Interacts with
CC PPP1R3B and PPP1R7. Isoform 2 interacts with SPZ1 (By similarity).
CC Interacts with CDCA2. PPP1R15A and PPP1R15B mediate binding to EIF2S1.
CC Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with
CC IKFZ1; the interaction targets PPP1CC to pericentromeric
CC heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it
CC from degradation. Interacts with PPP1R42; the interaction is direct (By
CC similarity). Interacts with NOM1 and PPP1R8. Component of the PTW/PP1
CC phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA
CC or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with isoform 1
CC and isoform 4 NEK2. Interacts with URI1; the interaction is
CC phosphorylation-dependent and occurs in a growth factor-dependent
CC manner. Interacts with FOXP3. Interacts with TMEM225 (via RVxF motif)
CC (By similarity). Interacts with MKI67 (PubMed:24867636). Interacts with
CC RRP1B; this targets PPP1CC to the nucleolus (PubMed:20926688).
CC Interacts with PPP1R2B (PubMed:23506001). Found in a complex with
CC PPP1CA, PPP1CC, SHC1 and PEAK1 (PubMed:23846654). Interacts with DYNLT4
CC (PubMed:23789093). {ECO:0000250|UniProtKB:P63087,
CC ECO:0000269|PubMed:11535607, ECO:0000269|PubMed:11564868,
CC ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:12226088,
CC ECO:0000269|PubMed:15280359, ECO:0000269|PubMed:15659832,
CC ECO:0000269|PubMed:16492807, ECO:0000269|PubMed:17283141,
CC ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:17965019,
CC ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:20926688,
CC ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:23506001,
CC ECO:0000269|PubMed:23789093, ECO:0000269|PubMed:23846654,
CC ECO:0000269|PubMed:24867636, ECO:0000269|PubMed:7556599,
CC ECO:0000269|PubMed:9414128}.
CC -!- INTERACTION:
CC P36873; P38398: BRCA1; NbExp=2; IntAct=EBI-356283, EBI-349905;
CC P36873; O95400: CD2BP2; NbExp=3; IntAct=EBI-356283, EBI-768015;
CC P36873; Q96S65: CSRNP1; NbExp=3; IntAct=EBI-356283, EBI-4311573;
CC P36873; Q9H175: CSRNP2; NbExp=7; IntAct=EBI-356283, EBI-5235958;
CC P36873; P03372: ESR1; NbExp=3; IntAct=EBI-356283, EBI-78473;
CC P36873; Q8IWU2: LMTK2; NbExp=5; IntAct=EBI-356283, EBI-2008933;
CC P36873; Q8N912: NRAC; NbExp=3; IntAct=EBI-356283, EBI-12051377;
CC P36873; O15294: OGT; NbExp=11; IntAct=EBI-356283, EBI-539828;
CC P36873; O60927: PPP1R11; NbExp=6; IntAct=EBI-356283, EBI-1048104;
CC P36873; Q5SWA1: PPP1R15B; NbExp=4; IntAct=EBI-356283, EBI-2815482;
CC P36873; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-356283, EBI-710402;
CC P36873; P41236: PPP1R2; NbExp=7; IntAct=EBI-356283, EBI-1056517;
CC P36873; Q6NXS1: PPP1R2B; NbExp=5; IntAct=EBI-356283, EBI-10251630;
CC P36873; O14990: PPP1R2C; NbExp=3; IntAct=EBI-356283, EBI-12404293;
CC P36873; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-356283, EBI-12000762;
CC P36873; Q86XI6: PPP1R3B; NbExp=3; IntAct=EBI-356283, EBI-3918864;
CC P36873; Q9UQK1: PPP1R3C; NbExp=4; IntAct=EBI-356283, EBI-2506727;
CC P36873; Q15435: PPP1R7; NbExp=5; IntAct=EBI-356283, EBI-1024281;
CC P36873; Q12972-2: PPP1R8; NbExp=3; IntAct=EBI-356283, EBI-12252736;
CC P36873; Q96SB3: PPP1R9B; NbExp=5; IntAct=EBI-356283, EBI-351275;
CC P36873; Q14684: RRP1B; NbExp=9; IntAct=EBI-356283, EBI-372051;
CC P36873; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-356283, EBI-11952721;
CC P36873; Q13625: TP53BP2; NbExp=8; IntAct=EBI-356283, EBI-77642;
CC P36873; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-356283, EBI-10175039;
CC P36873; Q4KMQ1-2: TPRN; NbExp=3; IntAct=EBI-356283, EBI-11978969;
CC P36873; O94763: URI1; NbExp=17; IntAct=EBI-356283, EBI-357067;
CC P36873; O94763-1: URI1; NbExp=8; IntAct=EBI-356283, EBI-12590720;
CC P36873; O95405: ZFYVE9; NbExp=5; IntAct=EBI-356283, EBI-296817;
CC P36873; Q9UEG4: ZNF629; NbExp=3; IntAct=EBI-356283, EBI-9977294;
CC P36873; O08785: Clock; Xeno; NbExp=2; IntAct=EBI-356283, EBI-79859;
CC P36873-1; Q5JR98: DYNLT4; NbExp=2; IntAct=EBI-356289, EBI-4311709;
CC P36873-1; P51955: NEK2; NbExp=2; IntAct=EBI-356289, EBI-633182;
CC P36873-1; Q5JTV8-3: TOR1AIP1; NbExp=4; IntAct=EBI-356289, EBI-21448143;
CC P36873-1; P04637: TP53; NbExp=2; IntAct=EBI-356289, EBI-366083;
CC P36873-2; Q5JQC9: AKAP4; NbExp=4; IntAct=EBI-3964623, EBI-16628643;
CC P36873-2; Q5JR98: DYNLT4; NbExp=3; IntAct=EBI-3964623, EBI-4311709;
CC P36873-2; Q7Z5V6: PPP1R32; NbExp=4; IntAct=EBI-3964623, EBI-4311771;
CC P36873-2; Q96S59: RANBP9; NbExp=3; IntAct=EBI-3964623, EBI-636085;
CC P36873-2; A1DRY3; NbExp=2; IntAct=EBI-3964623, EBI-4311408;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11739654}. Nucleus.
CC Nucleus, nucleolus {ECO:0000269|PubMed:11739654,
CC ECO:0000269|PubMed:20926688, ECO:0000269|PubMed:23789093}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:11739654}. Nucleus speckle
CC {ECO:0000269|PubMed:11739654}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:12529430}. Cleavage furrow
CC {ECO:0000269|PubMed:12529430}. Midbody {ECO:0000269|PubMed:12529430}.
CC Mitochondrion {ECO:0000269|PubMed:17936702}. Cytoplasm, cytoskeleton,
CC microtubule organizing center {ECO:0000269|PubMed:23789093}.
CC Note=Colocalizes with SPZ1 in the nucleus (By similarity). Colocalizes
CC with URI1 at mitochondrion (PubMed:17936702). Rapidly exchanges between
CC the nucleolar, nucleoplasmic and cytoplasmic compartments
CC (PubMed:11739654). Highly mobile in cells and can be relocalized
CC through interaction with targeting subunits (PubMed:17965019). In the
CC presence of PPP1R8 relocalizes from the nucleolus to nuclear speckles
CC (PubMed:11739654). Shows a dynamic targeting to specific sites
CC throughout the cell cycle (PubMed:12529430). Highly concentrated in
CC nucleoli of interphase cells and localizes at kinetochores early in
CC mitosis (PubMed:12529430). Relocalization to chromosome-containing
CC regions occurs at the transition from early to late anaphase
CC (PubMed:12529430). Also accumulates at the cleavage furrow and midbody
CC by telophase (PubMed:12529430). Colocalizes with DYNLT4 in the
CC microtubule organizing center (MTOC)(PubMed:23789093).
CC {ECO:0000250|UniProtKB:P63087, ECO:0000269|PubMed:11739654,
CC ECO:0000269|PubMed:12529430, ECO:0000269|PubMed:17936702,
CC ECO:0000269|PubMed:17965019, ECO:0000269|PubMed:23789093}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PPPCC1, Gamma-1;
CC IsoId=P36873-1; Sequence=Displayed;
CC Name=2; Synonyms=PPPCC2, Gamma-2;
CC IsoId=P36873-2; Sequence=VSP_005094;
CC -!- INDUCTION: Up-regulated in synovial fluid mononuclear cells and
CC peripheral blood mononuclear cells from patients with rheumatoid
CC arthritis. {ECO:0000269|PubMed:23396208}.
CC -!- PTM: Phosphorylated by NEK2. {ECO:0000269|PubMed:15659832}.
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 {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be part of the MLL5-L complex, at
CC least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and
CC OGT (PubMed:19377461). However, the corresponding article has been
CC retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461,
CC ECO:0000269|PubMed:24336203}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget - Issue
CC 32 of March 2003;
CC URL="https://web.expasy.org/spotlight/back_issues/032";
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DR EMBL; X74008; CAA52169.1; -; mRNA.
DR EMBL; BC014073; AAH14073.1; -; mRNA.
DR EMBL; L07395; AAA19823.1; -; mRNA.
DR CCDS; CCDS58279.1; -. [P36873-2]
DR CCDS; CCDS9150.1; -. [P36873-1]
DR PIR; S35699; S35699.
DR PIR; S35700; S35700.
DR RefSeq; NP_001231903.1; NM_001244974.1. [P36873-2]
DR RefSeq; NP_002701.1; NM_002710.3. [P36873-1]
DR PDB; 1IT6; X-ray; 2.00 A; A/B=1-323.
DR PDB; 1JK7; X-ray; 1.90 A; A=1-323.
DR PDB; 1U32; X-ray; 2.00 A; A=6-298.
DR PDB; 2BCD; X-ray; 2.10 A; A=1-323.
DR PDB; 2BDX; X-ray; 2.30 A; A=1-323.
DR PDB; 4UT2; X-ray; 1.96 A; A/B=1-323.
DR PDB; 4UT3; X-ray; 2.19 A; A/B=1-323.
DR PDB; 5INB; X-ray; 1.30 A; A=7-308.
DR PDB; 5J28; X-ray; 2.00 A; A/B=7-308.
DR PDBsum; 1IT6; -.
DR PDBsum; 1JK7; -.
DR PDBsum; 1U32; -.
DR PDBsum; 2BCD; -.
DR PDBsum; 2BDX; -.
DR PDBsum; 4UT2; -.
DR PDBsum; 4UT3; -.
DR PDBsum; 5INB; -.
DR PDBsum; 5J28; -.
DR AlphaFoldDB; P36873; -.
DR SASBDB; P36873; -.
DR SMR; P36873; -.
DR BioGRID; 111495; 689.
DR DIP; DIP-749N; -.
DR IntAct; P36873; 288.
DR MINT; P36873; -.
DR STRING; 9606.ENSP00000341779; -.
DR BindingDB; P36873; -.
DR ChEMBL; CHEMBL4438; -.
DR DrugBank; DB02169; 9,10-Deepithio-9,10-Didehydroacanthifolicin.
DR DrugBank; DB02860; Calyculin A.
DR DrugBank; DB04738; Motuporin.
DR MoonDB; P36873; Predicted.
DR CarbonylDB; P36873; -.
DR DEPOD; PPP1CC; -.
DR iPTMnet; P36873; -.
DR MetOSite; P36873; -.
DR PhosphoSitePlus; P36873; -.
DR SwissPalm; P36873; -.
DR BioMuta; PPP1CC; -.
DR DMDM; 548573; -.
DR EPD; P36873; -.
DR jPOST; P36873; -.
DR MassIVE; P36873; -.
DR MaxQB; P36873; -.
DR PaxDb; P36873; -.
DR PeptideAtlas; P36873; -.
DR PRIDE; P36873; -.
DR ProteomicsDB; 55224; -. [P36873-1]
DR ProteomicsDB; 55225; -. [P36873-2]
DR TopDownProteomics; P36873-1; -. [P36873-1]
DR TopDownProteomics; P36873-2; -. [P36873-2]
DR Antibodypedia; 2879; 448 antibodies from 34 providers.
DR DNASU; 5501; -.
DR Ensembl; ENST00000335007.10; ENSP00000335084.5; ENSG00000186298.12. [P36873-1]
DR Ensembl; ENST00000340766.9; ENSP00000341779.5; ENSG00000186298.12. [P36873-2]
DR GeneID; 5501; -.
DR KEGG; hsa:5501; -.
DR MANE-Select; ENST00000335007.10; ENSP00000335084.5; NM_002710.4; NP_002701.1.
DR UCSC; uc001tru.4; human. [P36873-1]
DR CTD; 5501; -.
DR DisGeNET; 5501; -.
DR GeneCards; PPP1CC; -.
DR HGNC; HGNC:9283; PPP1CC.
DR HPA; ENSG00000186298; Low tissue specificity.
DR MIM; 176914; gene.
DR neXtProt; NX_P36873; -.
DR OpenTargets; ENSG00000186298; -.
DR PharmGKB; PA33611; -.
DR VEuPathDB; HostDB:ENSG00000186298; -.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00940000153472; -.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; P36873; -.
DR OMA; EEHEIRY; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; P36873; -.
DR TreeFam; TF354243; -.
DR BRENDA; 3.1.3.16; 2681.
DR PathwayCommons; P36873; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-5673000; RAF activation.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-9726840; SHOC2 M1731 mutant abolishes MRAS complex function.
DR Reactome; R-HSA-9726842; Gain-of-function MRAS complexes activate RAF signaling.
DR SignaLink; P36873; -.
DR SIGNOR; P36873; -.
DR BioGRID-ORCS; 5501; 35 hits in 1087 CRISPR screens.
DR ChiTaRS; PPP1CC; human.
DR EvolutionaryTrace; P36873; -.
DR GeneWiki; PPP1CC; -.
DR GenomeRNAi; 5501; -.
DR Pharos; P36873; Tchem.
DR PRO; PR:P36873; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P36873; protein.
DR Bgee; ENSG00000186298; Expressed in jejunal mucosa and 219 other tissues.
DR ExpressionAtlas; P36873; baseline and differential.
DR Genevisible; P36873; HS.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:InterPro.
DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
DR GO; GO:0005521; F:lamin binding; IEA:Ensembl.
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:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:Reactome.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IDA:MGI.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IEA:Ensembl.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IEA:Ensembl.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR037981; PPP1CC.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668:SF204; PTHR11668:SF204; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 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 3D-structure; Acetylation; Alternative splicing; Biological rhythms;
KW Carbohydrate metabolism; Cell cycle; Cell division; Centromere; Chromosome;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disulfide bond;
KW Glycogen metabolism; Hydrolase; Kinetochore; Manganese; Metal-binding;
KW Mitochondrion; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..323
FT /note="Serine/threonine-protein phosphatase PP1-gamma
FT catalytic subunit"
FT /id="PRO_0000058787"
FT REGION 302..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:7500362"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11535607,
FT ECO:0000269|PubMed:15280359"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11535607,
FT ECO:0000269|PubMed:15280359"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11535607,
FT ECO:0000269|PubMed:15280359"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11535607,
FT ECO:0000269|PubMed:15280359"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11535607,
FT ECO:0000269|PubMed:15280359"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11535607,
FT ECO:0000269|PubMed:15280359"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11535607,
FT ECO:0000269|PubMed:15280359"
FT SITE 273
FT /note="Inhibition by microcystin toxin binding"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 307
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 311
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 315..323
FT /note="GMITKQAKK -> VASGLNPSIQKASNYRNNTVLYE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8394140"
FT /id="VSP_005094"
FT VARIANT 152
FT /note="F -> S (in dbSNP:rs11558237)"
FT /id="VAR_051734"
FT MUTAGEN 125
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11739654"
FT MUTAGEN 273
FT /note="C->A,S,L: Abolishes interaction with microcystin
FT toxin."
FT /evidence="ECO:0000269|PubMed:7556599"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:5INB"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:5INB"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:5INB"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5INB"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:5INB"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5INB"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:5INB"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:4UT3"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:5INB"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:5INB"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:5INB"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:5INB"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:5INB"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:5INB"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:5INB"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:5INB"
FT STRAND 290..298
FT /evidence="ECO:0007829|PDB:5INB"
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
