PPP6_RAT
ID PPP6_RAT Reviewed; 305 AA.
AC Q64620; Q6AZ47;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Serine/threonine-protein phosphatase 6 catalytic subunit {ECO:0000305};
DE Short=PP6C {ECO:0000250|UniProtKB:O00743};
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:O00743};
DE AltName: Full=Protein phosphatase V {ECO:0000303|PubMed:8077208};
DE Short=PP-V {ECO:0000303|PubMed:8077208};
GN Name=Ppp6c {ECO:0000312|RGD:708460};
GN Synonyms=Ppv {ECO:0000303|PubMed:8077208};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Testis;
RX PubMed=8077208; DOI=10.1016/s0021-9258(17)31686-1;
RA Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.;
RT "Molecular cloning of a protein serine/threonine phosphatase containing a
RT putative regulatory tetratricopeptide repeat domain.";
RL J. Biol. Chem. 269:22586-22592(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalytic subunit of protein phosphatase 6 (PP6). PP6 is a
CC component of a signaling pathway regulating cell cycle progression in
CC response to IL2 receptor stimulation. N-terminal domain restricts G1 to
CC S phase progression in cancer cells, in part through control of cyclin
CC D1. During mitosis, regulates spindle positioning. Down-regulates
CC MAP3K7 kinase activation of the IL1 signaling pathway by
CC dephosphorylation of MAP3K7. Participates also in the innate immune
CC defense against viruses by desphosphorylating RIG-I/DDX58, an essential
CC step that triggers RIG-I/DDX58-mediated signaling activation.
CC {ECO:0000250|UniProtKB:O00743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:O00743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:O00743};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P36873};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P36873};
CC -!- SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a
CC heterotrimeric complex formed by the catalytic subunit, a SAPS domain-
CC containing subunit (PP6R) and an ankyrin repeat-domain containing
CC regulatory subunit (ARS). Interacts with subunits PPP6R1, PPP6R2 and
CC PPP6R3. Interacts with subunit ANKRD28. Interacts with IGBP1. Interacts
CC with MAP3K7. Interacts with NFKBIE. Interacts with TRIM14 and WRNIP1;
CC these interactions positively regulate the RIG-I/DDX58 signaling
CC pathway. {ECO:0000250|UniProtKB:O00743}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O00743}.
CC Cytoplasm {ECO:0000250|UniProtKB:O00743}.
CC -!- TISSUE SPECIFICITY: Highest levels found in spleen, brain and lung.
CC {ECO:0000269|PubMed:8077208}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-6 (PP-V)
CC subfamily. {ECO:0000305}.
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DR EMBL; X77236; CAA54453.1; -; mRNA.
DR EMBL; BC078747; AAH78747.1; -; mRNA.
DR PIR; B55346; B55346.
DR RefSeq; NP_598273.2; NM_133589.2.
DR AlphaFoldDB; Q64620; -.
DR SMR; Q64620; -.
DR BioGRID; 251128; 2.
DR IntAct; Q64620; 3.
DR MINT; Q64620; -.
DR STRING; 10116.ENSRNOP00000021176; -.
DR PhosphoSitePlus; Q64620; -.
DR jPOST; Q64620; -.
DR PaxDb; Q64620; -.
DR PRIDE; Q64620; -.
DR Ensembl; ENSRNOT00000102106; ENSRNOP00000094628; ENSRNOG00000015145.
DR GeneID; 171121; -.
DR KEGG; rno:171121; -.
DR UCSC; RGD:708460; rat.
DR CTD; 5537; -.
DR RGD; 708460; Ppp6c.
DR eggNOG; KOG0373; Eukaryota.
DR GeneTree; ENSGT00550000074961; -.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; Q64620; -.
DR OMA; CQNKYGN; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; Q64620; -.
DR TreeFam; TF105563; -.
DR Reactome; R-RNO-171319; Telomere Extension By Telomerase.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR PRO; PR:Q64620; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000015145; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q64620; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:RGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:RGD.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cytoplasm; Hydrolase; Immunity; Innate immunity;
KW Manganese; Metal-binding; Mitochondrion; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..305
FT /note="Serine/threonine-protein phosphatase 6 catalytic
FT subunit"
FT /id="PRO_0000058879"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 53
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 113
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O00743"
FT CONFLICT 72
FT /note="P -> L (in Ref. 1; CAA54453)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="Y -> H (in Ref. 1; CAA54453)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="E -> V (in Ref. 1; CAA54453)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="F -> N (in Ref. 1; CAA54453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 35159 MW; 662969DE1B2EF490 CRC64;
MAPLDLDKYV EIARQCKYLP ENDLKRLCDY VCDLLLEESN VQPVSTPVTV CGDIHGQFYD
LCELFRTGGQ VPDTNYIFMG DFVDRGYYSL ETFTYLLALK AKWPDRITLL RGNHESRQIT
QVYGFYDECQ TKYGNANAWR YCTKVFDMLT VAALIDEQIL CVHGGLSPDI KTLDQIRTIE
RNQEIPHKGA FCDLVWSDPE DVDTWAISPR GAGWLFGAKV TNEFVHINNL KLICRAHQLV
HEGYKFMFDE KLVTVWSAPN YCYRCGNIAS IMVFKDVNTR EPKLFRAVPD SERVIPPRTT
TPYFL
