PPR3A_RABIT
ID PPR3A_RABIT Reviewed; 1109 AA.
AC Q00756;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 3A;
DE AltName: Full=Protein phosphatase 1 glycogen-associated regulatory subunit;
DE AltName: Full=Protein phosphatase type-1 glycogen targeting subunit;
DE Short=RG1;
GN Name=PPP1R3A; Synonyms=PP1G;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 13-52; 59-68; 75-118;
RP 163-193; 540-561; 565-580 AND 625-632, TISSUE SPECIFICITY, AND VARIANTS
RP MET-311 AND LYS-413.
RC STRAIN=New Zealand; TISSUE=Skeletal muscle;
RX PubMed=1651919; DOI=10.1016/s0021-9258(18)98477-2;
RA Tang P.M., Bondor J.A., Swiderek K.M., DePaoli-Roach A.A.;
RT "Molecular cloning and expression of the regulatory (RG1) subunit of the
RT glycogen-associated protein phosphatase.";
RL J. Biol. Chem. 266:15782-15789(1991).
RN [2]
RP PROTEIN SEQUENCE OF 33-46, AND PHOSPHORYLATION AT SER-40; SER-44; SER-48
RP AND SER-67.
RX PubMed=2542090; DOI=10.1016/0014-5793(89)80433-8;
RA Dent P., Campbell D.G., Hubbard M.J., Cohen P.;
RT "Multisite phosphorylation of the glycogen-binding subunit of protein
RT phosphatase-1G by cyclic AMP-dependent protein kinase and glycogen synthase
RT kinase-3.";
RL FEBS Lett. 248:67-72(1989).
RN [3]
RP PHOSPHORYLATION AT SER-48.
RX PubMed=2123524; DOI=10.1038/348302a0;
RA Dent P., Lavoinne A., Nakielny S., Caudwell F.B., Watt P., Cohen P.;
RT "The molecular mechanism by which insulin stimulates glycogen synthesis in
RT mammalian skeletal muscle.";
RL Nature 348:302-308(1990).
CC -!- FUNCTION: Seems to act as a glycogen-targeting subunit for PP1. PP1 is
CC essential for cell division, and participates in the regulation of
CC glycogen metabolism, muscle contractility and protein synthesis. Plays
CC an important role in glycogen synthesis but is not essential for
CC insulin activation of glycogen synthase (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPP1CC catalytic subunit of PP1, and associates
CC with glycogen. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Skeletal muscle, diaphragm and cardiac muscle.
CC {ECO:0000269|PubMed:1651919}.
CC -!- DOMAIN: The CBM21 domain is known to be involved in the localization to
CC glycogen and is characteristic of some regulatory subunit of
CC phosphatase complexes.
CC -!- PTM: Phosphorylation at Ser-48 by ISPK stimulates the dephosphorylation
CC of glycogen synthase and phosphorylase kinase.
CC {ECO:0000269|PubMed:2123524, ECO:0000269|PubMed:2542090}.
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DR EMBL; M65109; AAA31462.1; -; mRNA.
DR PIR; A40801; A40801.
DR RefSeq; NP_001075772.1; NM_001082303.1.
DR PDB; 2M83; NMR; -; A=102-237.
DR PDB; 6DNO; X-ray; 1.45 A; B=64-93.
DR PDBsum; 2M83; -.
DR PDBsum; 6DNO; -.
DR AlphaFoldDB; Q00756; -.
DR BMRB; Q00756; -.
DR SMR; Q00756; -.
DR BioGRID; 1172163; 3.
DR IntAct; Q00756; 2.
DR MINT; Q00756; -.
DR STRING; 9986.ENSOCUP00000000266; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR iPTMnet; Q00756; -.
DR PRIDE; Q00756; -.
DR Ensembl; ENSOCUT00000000303; ENSOCUP00000000266; ENSOCUG00000000303.
DR GeneID; 100009140; -.
DR KEGG; ocu:100009140; -.
DR CTD; 5506; -.
DR eggNOG; KOG3986; Eukaryota.
DR GeneTree; ENSGT00940000157682; -.
DR HOGENOM; CLU_009399_0_0_1; -.
DR InParanoid; Q00756; -.
DR OMA; TFKPGFS; -.
DR OrthoDB; 1232750at2759; -.
DR TreeFam; TF105537; -.
DR Proteomes; UP000001811; Chromosome 7.
DR Bgee; ENSOCUG00000000303; Expressed in skeletal muscle tissue and 8 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IDA:CAFA.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.2440; -; 1.
DR InterPro; IPR005036; CBM21_dom.
DR InterPro; IPR038175; CBM21_dom_sf.
DR Pfam; PF03370; CBM_21; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Glycogen metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1109
FT /note="Protein phosphatase 1 regulatory subunit 3A"
FT /id="PRO_0000071502"
FT TRANSMEM 1066..1086
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 124..232
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT REGION 236..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 64..67
FT /note="PP1-binding motif"
FT COMPBIAS 237..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine; by GSK3"
FT /evidence="ECO:0000269|PubMed:2542090"
FT MOD_RES 44
FT /note="Phosphoserine; by GSK3"
FT /evidence="ECO:0000269|PubMed:2542090"
FT MOD_RES 48
FT /note="Phosphoserine; by PKA and ISPK"
FT /evidence="ECO:0000269|PubMed:2123524,
FT ECO:0000269|PubMed:2542090"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MR9"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99MR9"
FT MOD_RES 67
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:2542090"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MR9"
FT VARIANT 311
FT /note="T -> M"
FT /evidence="ECO:0000269|PubMed:1651919"
FT VARIANT 413
FT /note="N -> K"
FT /evidence="ECO:0000269|PubMed:1651919"
FT CONFLICT 26
FT /note="C -> Y (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="C -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:6DNO"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:6DNO"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2M83"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2M83"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:2M83"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:2M83"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:2M83"
FT STRAND 155..169
FT /evidence="ECO:0007829|PDB:2M83"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:2M83"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:2M83"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:2M83"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:2M83"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:2M83"
SQ SEQUENCE 1109 AA; 124170 MW; 1CD9FB8F47890226 CRC64;
MEPSEVPGQN SKDNFLEVPN LSDSLCEDEE VKAIFKPGFS PQPSRRGSES SEEVYVHTAS
SGGRRVSFAD NFGFNLVSVK EFDTWELPSV STTFELGKDA FQTEEYVLSP LFDLPASKED
LMQQLQVQKA MLESTEYVPG STSMKGIIRV LNISFEKLVY VRMSLDDWQT HYDILAEYVP
NSCDGETDQF SFKISLVPPY QKDGSKVEFC IRYETSVGTF WSNNNGTNYT LVCQKKEPEP
EPGKPLEEAP SKQKKGCLKV KSSKEESSET SEENNFENSK IADTYIPTIV CSHEEKEDLK
SSYQNVKDVN TEHDEHNEKE LELMINQRLI RTRCAASEYG KNTLSSDPSN IPNKPEELQK
NQSHSEACTD LSQRLLSPGS SAESSLKGDF YHTEKYSSGN ESSHQPSDMG EINPSLGGTT
SDGSVQLHIS SKEILDDNAN PAHGSGRGEI SCSFPGQLKA SNLNKKYEGG AENSEMKDCE
CLPRDVHLKA SDYFKKSTEN RPSEEDYGTS KDNKEKRIQL DVDEKTSKNF RSIFYDQERN
VGHLEITVEG IEASDRDLTS LPTKDTTIPT WAIMEDTFHS SRTPLGREEA VLTTPEHDLS
SSEGTILGGL TGGVCSPRNG NVLKNDYLFQ VEKRKSGWIN PEDQNKDTQH QQSWNVLESQ
EKARGSKTNI AEQIKEQVDC EDMWEKRDNT GSLKATPAEA LFTCQEAEHC ELSPLADHGI
PGKAEAGTAY IIKTTSETTP ESMSAGEKAI IAKLPQETAR SDRPMEVKET AFDPHEGRND
DSHYTLCQRD TVGVIDDNGV EKESHLDICN ARLDEMRKEE AMSMHSPGKM RDREKLGIGN
ITSVEESSQV IANNEKATSR LDLHLEMPSA DKKIFPENRD LGQVQELSKK TDIDNTVHSA
FNSDTNRASR DDSLLSSHHT ETSVLSCEQA NAVKNTVTTT ALQTSATESE YNCSPTRETQ
GQPASKPEEV SRGSRRVTSE TRKEKCVGQM FQSGECNVEM SQGPMILVSE SRENVERERH
ENEGLINSGD KEFESSASSS LPVQETQDQS NESLLSKYTN SKIPYFLLFL MFLVTVYHYD
LMIGLAFYLF SLYWLYWEEG RQKESVKKK
