PPR3C_XENLA
ID PPR3C_XENLA Reviewed; 299 AA.
AC Q6DDQ5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 3C;
GN Name=ppp1r3c {ECO:0000312|EMBL:AAH77483.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH77483.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000312|EMBL:AAH77483.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a glycogen-targeting subunit for PP1 and regulates
CC its activity. Activates glycogen synthase, reduces glycogen
CC phosphorylase activity and limits glycogen breakdown (By similarity).
CC {ECO:0000250|UniProtKB:Q7TMB3}.
CC -!- SUBUNIT: Interacts with PPP1CC catalytic subunit of PP1 and associates
CC with glycogen. Forms complexes with glycogen phosphorylase, glycogen
CC synthase and phosphorylase kinase which is necessary for its regulation
CC of PP1 activity (By similarity). {ECO:0000250|UniProtKB:Q7TMB3}.
CC -!- DOMAIN: The N-terminal region is required for binding to PP1, the
CC central region is required for binding to glycogen and the C-terminal
CC region is required for binding to glycogen phosphorylase, glycogen
CC synthase and phosphorylase kinase. {ECO:0000250|UniProtKB:Q7TMB3}.
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DR EMBL; BC077483; AAH77483.1; -; mRNA.
DR RefSeq; NP_001086808.1; NM_001093339.1.
DR AlphaFoldDB; Q6DDQ5; -.
DR SMR; Q6DDQ5; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR DNASU; 446643; -.
DR GeneID; 446643; -.
DR KEGG; xla:446643; -.
DR CTD; 446643; -.
DR Xenbase; XB-GENE-17331304; ppp1r3c.S.
DR OrthoDB; 1232750at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 446643; Expressed in muscle tissue and 17 other tissues.
DR GO; GO:0019903; F:protein phosphatase binding; ISS:UniProtKB.
DR GO; GO:0005978; P:glycogen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0005977; P:glycogen metabolic process; ISS:UniProtKB.
DR Gene3D; 2.60.40.2440; -; 1.
DR InterPro; IPR005036; CBM21_dom.
DR InterPro; IPR038175; CBM21_dom_sf.
DR InterPro; IPR017434; Pase-1_reg-su_3B/C/D_met.
DR InterPro; IPR030683; PP1_3C.
DR PANTHER; PTHR12307:SF15; PTHR12307:SF15; 1.
DR Pfam; PF03370; CBM_21; 1.
DR PIRSF; PIRSF038207; PP1_GT_animal; 1.
DR PIRSF; PIRSF500813; PP1_PTG; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycogen metabolism; Reference proteome.
FT CHAIN 1..299
FT /note="Protein phosphatase 1 regulatory subunit 3C"
FT /id="PRO_0000285931"
FT DOMAIN 130..238
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT MOTIF 65..68
FT /note="PP1-binding motif"
SQ SEQUENCE 299 AA; 34351 MW; 9B7B5792196D9106 CRC64;
MPVDMAVRIC LAHSPPLKKF LSPSDCRGRN FVNRFKPLRP CLSLKKESES RSNEWNRSKS
RNKKRVVFAD SKGLSLTSVH VFSEFKDESS LDLQFDLIDL EDITASLKLH EEKNLILGFT
QPSADYLQFR NRLQKSFVCL ENCSLQERSV AGTIKVKNVN YTKSVKIRIT FNTWKSFVDV
DCVYMNNVYG STDSDTFSFV IDIPPNIPSH EKIEFCISYE SEGQVFWDNN DGQNYSVIRA
EWKSDGVHTP SPNKTDIASY EYKKKPQNND FDQFGSPRTS AGLYPEWQSW GKIGGSPYW