PP1G_RAT
ID PP1G_RAT Reviewed; 323 AA.
AC P63088; O09186; O09189; P37139; Q64679;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING.
RX PubMed=2177460; DOI=10.1111/j.1349-7006.1990.tb02690.x;
RA Sasaki K., Shima H., Kitagawa Y., Irino S., Sugimura T., Nagao M.;
RT "Identification of members of the protein phosphatase 1 gene family in the
RT rat and enhanced expression of protein phosphatase 1 alpha gene in rat
RT hepatocellular carcinomas.";
RL Jpn. J. Cancer Res. 81:1272-1280(1990).
RN [2]
RP ERRATUM OF PUBMED:2177460.
RX PubMed=1653777;
RA Sasaki K., Shima H., Kitagawa Y., Irino S., Sugimura T., Nagao M.;
RL Jpn. J. Cancer Res. 82:873-873(1991).
RN [3]
RP PROTEIN SEQUENCE OF 42-58 AND 212-234, AND INTERACTION WITH PPP1R9A.
RC STRAIN=Sprague-Dawley;
RX PubMed=10504266; DOI=10.1021/bi991227d;
RA McAvoy T., Allen P.B., Obaishi H., Nakanishi H., Takai Y., Greengard P.,
RA Nairn A.C., Hemmings H.C. Jr.;
RT "Regulation of neurabin I interaction with protein phosphatase 1 by
RT phosphorylation.";
RL Biochemistry 38:12943-12949(1999).
RN [4]
RP TISSUE SPECIFICITY (ISOFORM 2).
RX PubMed=8393674; DOI=10.1006/bbrc.1993.1910;
RA Shima H., Haneji T., Hatano Y., Kasugai I., Sugimura T., Nagao M.;
RT "Protein phosphatase 1 gamma 2 is associated with nuclei of meiotic cells
RT in rat testis.";
RL Biochem. Biophys. Res. Commun. 194:930-937(1993).
RN [5]
RP INTERACTION WITH PPP1R3B.
RX PubMed=7720853; DOI=10.1016/0014-5793(95)00197-h;
RA Moorhead G., MacKintosh C., Morrice N., Cohen P.;
RT "Purification of the hepatic glycogen-associated form of protein
RT phosphatase-1 by microcystin-Sepharose affinity chromatography.";
RL FEBS Lett. 362:101-105(1995).
RN [6]
RP INTERACTION WITH PPP1R3B.
RX PubMed=9841883; DOI=10.1042/bj3360699;
RA Armstrong C.G., Doherty M.J., Cohen P.T.W.;
RT "Identification of the separate domains in the hepatic glycogen-targeting
RT subunit of protein phosphatase 1 that interact with phosphorylase a,
RT glycogen and protein phosphatase 1.";
RL Biochem. J. 336:699-704(1998).
RN [7]
RP SUBUNIT.
RX PubMed=10585469; DOI=10.1074/jbc.274.50.35845;
RA MacMillan L.B., Bass M.A., Cheng N., Howard E.F., Tamura M., Strack S.,
RA Wadzinski B.E., Colbran R.J.;
RT "Brain actin-associated protein phosphatase 1 holoenzymes containing
RT spinophilin, neurabin, and selected catalytic subunit isoforms.";
RL J. Biol. Chem. 274:35845-35854(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-323 IN COMPLEX WITH MANGANESE
RP AND M.MUSCULUS INHIBITOR PPP1R2.
RX PubMed=17636256; DOI=10.1074/jbc.m703472200;
RA Hurley T.D., Yang J., Zhang L., Goodwin K.D., Zou Q., Cortese M.,
RA Dunker A.K., DePaoli-Roach A.A.;
RT "Structural basis for regulation of protein phosphatase 1 by inhibitor-2.";
RL J. Biol. Chem. 282:28874-28883(2007).
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. {ECO:0000250|UniProtKB:P36873}.
CC -!- FUNCTION: [Isoform 2]: Required for normal male fertility.
CC {ECO:0000250|UniProtKB:P36873}.
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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 2 manganese ions per subunit.;
CC -!- ACTIVITY REGULATION: Inactivated by binding to URI1. {ECO:0000250}.
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 sliver), PPP1R3C,
CC PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. PPP1R15A
CC and PPP1R15B mediate binding to EIF2S1. Part of a complex containing
CC PPP1R15B, PP1 and NCK1/2. Interacts with PPP1R3B, PPP1R7 and CDCA2.
CC Isoform 2 interacts with SPZ1. Interacts with IKFZ1; the interaction
CC targets PPP1CC to pericentromeric heterochromatin, dephosphorylates
CC IKAROS, stabilizes it and prevents it from degradation. Interacts with
CC NOM1 and PPP1R8. Component of the PTW/PP1 phosphatase complex, composed
CC of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC.
CC Interacts with PPP1R8 (By similarity). Interacts with NEK2. Interacts
CC with URI1; the interaction is phosphorylation-dependent and occurs in a
CC growth factor-dependent manner (By similarity). Interacts with FOXP3
CC (By similarity). Interacts with TMEM225 (via RVxF motif) (By
CC similarity). Interacts with MKI67 (By similarity). Interacts with
CC RRP1B; this targets PPP1CC to the nucleolus (By similarity). Found in a
CC complex with PPP1CA, PPP1CC, SHC1 and PEAK1 (By similarity)
CC (PubMed:10504266, PubMed:10585469, PubMed:7720853, PubMed:9841883).
CC Interacts with DYNLT4 (By similarity). {ECO:0000250|UniProtKB:P36873,
CC ECO:0000250|UniProtKB:P63087, ECO:0000269|PubMed:10504266,
CC ECO:0000269|PubMed:10585469, ECO:0000269|PubMed:7720853,
CC ECO:0000269|PubMed:9841883}.
CC -!- INTERACTION:
CC P63088; P23385: Grm1; NbExp=15; IntAct=EBI-80049, EBI-4410410;
CC P63088; P31424: Grm5; NbExp=19; IntAct=EBI-80049, EBI-2902734;
CC P63088; P35400: Grm7; NbExp=4; IntAct=EBI-80049, EBI-6936416;
CC P63088; Q63337: mGluR7; NbExp=11; IntAct=EBI-80049, EBI-6935714;
CC P63088; O35867: Ppp1r9a; NbExp=2; IntAct=EBI-80049, EBI-7092421;
CC P63088; O35274: Ppp1r9b; NbExp=3; IntAct=EBI-80049, EBI-80022;
CC P63088; Q5PQX1: Tor1aip1; NbExp=2; IntAct=EBI-80049, EBI-15644430;
CC P63088; O15294: OGT; Xeno; NbExp=3; IntAct=EBI-80049, EBI-539828;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36873}. Nucleus
CC {ECO:0000250|UniProtKB:P36873}. Cleavage furrow
CC {ECO:0000250|UniProtKB:P36873}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P36873}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P36873}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:P36873}. Nucleus speckle
CC {ECO:0000250|UniProtKB:P36873}. Midbody {ECO:0000250|UniProtKB:P36873}.
CC Mitochondrion {ECO:0000250|UniProtKB:P36873}. Cytoplasm, cytoskeleton,
CC microtubule organizing center {ECO:0000250|UniProtKB:P36873}.
CC Note=Colocalizes with SPZ1 in the nucleus. Colocalizes with URI1 at
CC mitochondrion. Rapidly exchanges between the nucleolar, nucleoplasmic
CC and cytoplasmic compartments. Highly mobile in cells and can be
CC relocalized through interaction with targeting subunits. In the
CC presence of PPP1R8 relocalizes from the nucleolus to nuclear speckles.
CC Shows a dynamic targeting to specific sites throughout the cell cycle.
CC Highly concentrated in nucleoli of interphase cells and localizes at
CC kinetochores early in mitosis. Relocalization to chromosome-containing
CC regions occurs at the transition from early to late anaphase. Also
CC accumulates at the cleavage furrow and midbody by telophase.
CC {ECO:0000250|UniProtKB:P36873, ECO:0000250|UniProtKB:P63087}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Gamma-1;
CC IsoId=P63088-1; Sequence=Displayed;
CC Name=2; Synonyms=Gamma-2;
CC IsoId=P63088-2; Sequence=VSP_011566;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed only in testis, in the late
CC spermatocytes and early spematids (at protein level).
CC {ECO:0000269|PubMed:8393674}.
CC -!- PTM: Phosphorylated by NEK2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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; D90165; BAA14196.1; -; mRNA.
DR EMBL; D90166; BAA14197.1; -; mRNA.
DR PIR; I76572; I76572.
DR PIR; I76573; I76573.
DR RefSeq; NP_071943.1; NM_022498.2. [P63088-1]
DR PDB; 2O8A; X-ray; 2.61 A; A/B=2-323.
DR PDB; 2O8G; X-ray; 2.50 A; A/B=2-323.
DR PDBsum; 2O8A; -.
DR PDBsum; 2O8G; -.
DR AlphaFoldDB; P63088; -.
DR SMR; P63088; -.
DR BioGRID; 246801; 2.
DR ELM; P63088; -.
DR IntAct; P63088; 10.
DR MINT; P63088; -.
DR STRING; 10116.ENSRNOP00000047912; -.
DR iPTMnet; P63088; -.
DR PhosphoSitePlus; P63088; -.
DR SwissPalm; P63088; -.
DR jPOST; P63088; -.
DR PaxDb; P63088; -.
DR PRIDE; P63088; -.
DR Ensembl; ENSRNOT00000048851; ENSRNOP00000047912; ENSRNOG00000001269. [P63088-2]
DR Ensembl; ENSRNOT00000078761; ENSRNOP00000071829; ENSRNOG00000001269. [P63088-1]
DR GeneID; 24669; -.
DR KEGG; rno:24669; -.
DR UCSC; RGD:3377; rat. [P63088-1]
DR CTD; 5501; -.
DR RGD; 3377; Ppp1cc.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00940000153472; -.
DR InParanoid; P63088; -.
DR OMA; EEHEIRY; -.
DR TreeFam; TF354243; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-5673000; RAF activation.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR EvolutionaryTrace; P63088; -.
DR PRO; PR:P63088; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001269; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; P63088; baseline and differential.
DR Genevisible; P63088; RN.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
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; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:InterPro.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0005521; F:lamin binding; IPI:RGD.
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:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IMP:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IPI:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; IDA:RGD.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
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:0030182; P:neuron differentiation; IDA:MGI.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; ISO:RGD.
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; Glycogen metabolism;
KW Hydrolase; Kinetochore; Manganese; Metal-binding; Mitochondrion; Nucleus;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT CHAIN 2..323
FT /note="Serine/threonine-protein phosphatase PP1-gamma
FT catalytic subunit"
FT /id="PRO_0000058789"
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:0000250"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17636256"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17636256"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17636256"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17636256"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT MOD_RES 307
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT MOD_RES 311
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT VAR_SEQ 315..323
FT /note="GMITKQAKK -> VGSGLNPSIQKASNYRNNTVLYE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2177460"
FT /id="VSP_011566"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:2O8G"
FT TURN 18..21
FT /evidence="ECO:0007829|PDB:2O8G"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:2O8G"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:2O8G"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:2O8G"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2O8G"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:2O8G"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:2O8G"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:2O8G"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:2O8G"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:2O8G"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:2O8G"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:2O8G"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:2O8G"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:2O8G"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:2O8G"
FT CONFLICT P63088-2:214
FT /note="L -> F (in Ref. 1; BAA14197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 36984 MW; 4E28412C16898615 CRC64;
MADIDKLNID 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
