PP3BB_XENLA
ID PP3BB_XENLA Reviewed; 271 AA.
AC Q6GQ68;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 3B-B;
GN Name=ppp1r3b-b;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a glycogen-targeting subunit for phosphatase PP1.
CC Facilitates interaction of the PP1 with enzymes of the glycogen
CC metabolism and regulates its activity. Suppresses the rate at which PP1
CC dephosphorylates (inactivates) glycogen phosphorylase and enhances the
CC rate at which it activates glycogen synthase and therefore limits
CC glycogen breakdown (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with glycogen, PPP1CC catalytic subunit of PP1 and
CC PYGL. Associates with glycogen particles. Forms complexes with
CC debranching enzyme, glycogen phosphorylase, glycogen synthase and
CC phosphorylase kinase which is necessary for its regulation of PP1
CC activity (By similarity). {ECO:0000250}.
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 PYGL. {ECO:0000250}.
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DR EMBL; BC072880; AAH72880.1; -; mRNA.
DR RefSeq; NP_001085518.1; NM_001092049.1.
DR AlphaFoldDB; Q6GQ68; -.
DR SMR; Q6GQ68; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR DNASU; 443944; -.
DR GeneID; 443944; -.
DR KEGG; xla:443944; -.
DR CTD; 443944; -.
DR Xenbase; XB-GENE-6251522; ppp1r3b.S.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 443944; Expressed in egg cell and 19 other tissues.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:InterPro.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0005981; P:regulation of glycogen catabolic process; IEA:InterPro.
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; IPR030682; PP1_3B.
DR PANTHER; PTHR12307:SF13; PTHR12307:SF13; 1.
DR Pfam; PF03370; CBM_21; 1.
DR PIRSF; PIRSF038207; PP1_GT_animal; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycogen metabolism; Reference proteome.
FT CHAIN 1..271
FT /note="Protein phosphatase 1 regulatory subunit 3B-B"
FT /id="PRO_0000324548"
FT DOMAIN 119..227
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT MOTIF 56..59
FT /note="PP1-binding motif"
SQ SEQUENCE 271 AA; 31269 MW; 2C29389EF083509D CRC64;
MALDIAMKFY LRSPLRRDRV ECRITQSNEP LRPCIQTTDK TLLSELSNQE NKVKKRVSFA
DSRGLALTMV KVYSDFDDEL EIPFNISELI DNIVNLTTVE KEHFVLDFVQ PSADYLDFRN
RLKADSVCLE NCMLKDKALV GTVKVKNLAF QKCVKIRITF DSWQTYTDYD CQYVKDSYGG
SDKDTFSFDV SLPDSIQSNA RLEFAVCFDC EGRIFWDSNK GLNYRIVRHG HRIPYDPVCV
SVDQYGSPRC SYGIFPELPT YSGFDKLGPY Y