ID   PPR3B_BOVIN             Reviewed;         284 AA.
AC   A6QNP3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 3B;
GN   Name=PPP1R3B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) 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. Its activity is inhibited by PYGL, resulting in
CC       inhibition of the glycogen synthase and glycogen phosphorylase
CC       phosphatase activities of PP1. Dramatically increases basal and
CC       insulin-stimulated glycogen synthesis upon overexpression in
CC       hepatocytes (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; BC148936; AAI48937.1; -; mRNA.
DR   RefSeq; NP_001096717.1; NM_001103247.1.
DR   AlphaFoldDB; A6QNP3; -.
DR   SMR; A6QNP3; -.
DR   STRING; 9913.ENSBTAP00000014032; -.
DR   CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR   PaxDb; A6QNP3; -.
DR   Ensembl; ENSBTAT00000070313; ENSBTAP00000058425; ENSBTAG00000010606.
DR   GeneID; 514428; -.
DR   KEGG; bta:514428; -.
DR   CTD; 79660; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010606; -.
DR   VGNC; VGNC:33243; PPP1R3B.
DR   eggNOG; KOG3986; Eukaryota.
DR   GeneTree; ENSGT00940000159475; -.
DR   HOGENOM; CLU_040215_2_1_1; -.
DR   InParanoid; A6QNP3; -.
DR   OrthoDB; 1232750at2759; -.
DR   TreeFam; TF105537; -.
DR   Proteomes; UP000009136; Chromosome 27.
DR   Bgee; ENSBTAG00000010606; Expressed in cardiac ventricle and 106 other tissues.
DR   ExpressionAtlas; A6QNP3; baseline and differential.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR   GO; GO:2001069; F:glycogen binding; IBA:GO_Central.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
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:0005979; P:regulation of glycogen biosynthetic process; IBA:GO_Central.
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; PIRSF500814; PP1_GL; 1.
DR   PIRSF; PIRSF038207; PP1_GT_animal; 1.
DR   PROSITE; PS51159; CBM21; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycogen metabolism; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..284
FT                   /note="Protein phosphatase 1 regulatory subunit 3B"
FT                   /id="PRO_0000324542"
FT   DOMAIN          124..232
FT                   /note="CBM21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT   MOTIF           61..64
FT                   /note="PP1-binding motif"
FT   MOD_RES         260
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C767"
SQ   SEQUENCE   284 AA;  32383 MW;  79C2552FC85DA27A CRC64;
     MAVDIECRYS CMAPSLRRER FAFQIAPKPS KPLRPCIQLS GKNEASGTVA PTVQEKKVKK
     RVSFADNQGL ALTMVKVFSE FDDPLDIPLN ITELLDSIVS LTTAESESFV LDFSQPSADY
     LDFRNRLQTD HVCLENCVLK DRSIAGTVKV QNLAFEKTVK VRMTFDTWKS FTDFPCWYVK
     DTYAGSDKDT FSFDISLPEK IQSYERMEFA VCYECNGQTY WDSNKGKNYR IIRAELQSTQ
     GTAQPPNGPD FEIAFDQFGS PRCSYGLFPE WPSYLGYEKL GPYY