PP3BA_XENLA
ID PP3BA_XENLA Reviewed; 280 AA.
AC Q5BL87;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 3B-A;
GN Name=ppp1r3b-a;
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=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2005) 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; BC090563; AAH90563.1; -; mRNA.
DR RefSeq; NP_001089995.1; NM_001096526.1.
DR AlphaFoldDB; Q5BL87; -.
DR SMR; Q5BL87; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR DNASU; 735066; -.
DR GeneID; 735066; -.
DR KEGG; xla:735066; -.
DR CTD; 735066; -.
DR Xenbase; XB-GENE-6078118; ppp1r3b.L.
DR OrthoDB; 1232750at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 735066; 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; 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; Reference proteome.
FT CHAIN 1..280
FT /note="Protein phosphatase 1 regulatory subunit 3B-A"
FT /id="PRO_0000324547"
FT DOMAIN 121..229
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT MOTIF 58..61
FT /note="PP1-binding motif"
SQ SEQUENCE 280 AA; 32544 MW; 496C887DCFF9B412 CRC64;
MAVDIAMKFY LRSPPLRRDR VECRIARKSN EPLRPCIQTT DKTLLSELSN QENKVKKRVS
FADSRGLALT MVKVYSDFDD ELEIPFNISE LIDNIVNLTT VEKERFVLDF VQPSADYLDF
RNRLQADSVC LENCMLKDKA LVGTVKVKNL AFQKCVKIRM TFDSWQTYTD YDCQYVKDTY
AGSDKDTFSF DVSLPEGIQS NTRIEFAVYF ECEGRIFWDS NKSLNYKIAR QDHRIPSNFE
SRHYDPVCMS VDQYGSPRCS YGIFPELPTY SGFDKLGPYY