PP16A_MOUSE
ID PP16A_MOUSE Reviewed; 524 AA.
AC Q923M0; Q4V9Z1;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 16A;
DE AltName: Full=Myosin phosphatase targeting subunit 3;
DE Flags: Precursor;
GN Name=Ppp1r16a; Synonyms=Mypt3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ISOPRENYLATION AT CYS-521.
RX PubMed=11336659; DOI=10.1042/0264-6021:3560257;
RA Skinner J.A., Saltiel A.R.;
RT "Cloning and identification of MYPT3: a prenylatable myosin targeting
RT subunit of protein phosphatase 1.";
RL Biochem. J. 356:257-267(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Olfactory epithelium;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Inhibits protein phosphatase 1 activity toward phosphorylase,
CC myosin light chain and myosin substrates.
CC -!- SUBUNIT: Binds PP1.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, followed by liver,
CC heart, brain and lung.
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DR EMBL; AY010723; AAG40949.1; -; mRNA.
DR EMBL; BC057450; AAH57450.1; -; mRNA.
DR EMBL; BC096620; AAH96620.1; -; mRNA.
DR CCDS; CCDS27585.1; -.
DR RefSeq; NP_203535.1; NM_033371.2.
DR RefSeq; XP_006521530.1; XM_006521467.2.
DR AlphaFoldDB; Q923M0; -.
DR SMR; Q923M0; -.
DR STRING; 10090.ENSMUSP00000037356; -.
DR iPTMnet; Q923M0; -.
DR PhosphoSitePlus; Q923M0; -.
DR MaxQB; Q923M0; -.
DR PaxDb; Q923M0; -.
DR PRIDE; Q923M0; -.
DR ProteomicsDB; 289374; -.
DR Antibodypedia; 14950; 93 antibodies from 22 providers.
DR DNASU; 73062; -.
DR Ensembl; ENSMUST00000037551; ENSMUSP00000037356; ENSMUSG00000033819.
DR Ensembl; ENSMUST00000135388; ENSMUSP00000155515; ENSMUSG00000033819.
DR GeneID; 73062; -.
DR KEGG; mmu:73062; -.
DR UCSC; uc007wlo.1; mouse.
DR CTD; 84988; -.
DR MGI; MGI:1920312; Ppp1r16a.
DR VEuPathDB; HostDB:ENSMUSG00000033819; -.
DR eggNOG; KOG0505; Eukaryota.
DR GeneTree; ENSGT00940000154090; -.
DR HOGENOM; CLU_000134_54_2_1; -.
DR InParanoid; Q923M0; -.
DR OMA; DLEEVCQ; -.
DR OrthoDB; 564568at2759; -.
DR PhylomeDB; Q923M0; -.
DR TreeFam; TF316803; -.
DR BioGRID-ORCS; 73062; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ppp1r16a; mouse.
DR PRO; PR:Q923M0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q923M0; protein.
DR Bgee; ENSMUSG00000033819; Expressed in spermatid and 216 other tissues.
DR ExpressionAtlas; Q923M0; baseline and differential.
DR Genevisible; Q923M0; MM.
DR GO; GO:0005829; C:cytosol; TAS:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0017020; F:myosin phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0035304; P:regulation of protein dephosphorylation; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017417; Pase-1_reg_su_16AB.
DR Pfam; PF12796; Ank_2; 2.
DR PIRSF; PIRSF038159; PP1_16AB_vert; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW ANK repeat; Cell membrane; Coiled coil; Lipoprotein; Membrane; Methylation;
KW Palmitate; Phosphoprotein; Prenylation; Reference proteome; Repeat.
FT CHAIN 1..521
FT /note="Protein phosphatase 1 regulatory subunit 16A"
FT /id="PRO_0000067041"
FT PROPEP 522..524
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396708"
FT REPEAT 70..99
FT /note="ANK 1"
FT REPEAT 103..132
FT /note="ANK 2"
FT REPEAT 136..165
FT /note="ANK 3"
FT REPEAT 231..260
FT /note="ANK 4"
FT REPEAT 264..293
FT /note="ANK 5"
FT REGION 368..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 448..469
FT /evidence="ECO:0000255"
FT COMPBIAS 381..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96I34"
FT MOD_RES 521
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 520
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 521
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000305|PubMed:11336659"
SQ SEQUENCE 524 AA; 57530 MW; A0F682A794475429 CRC64;
MAEHLELLAE MPMVGRMSTQ ERLKHAQKRR AQQVKMWAQA EKEAHSKKGH GERPWKEVAG
LRPRKHVLFP PSVALLEAAA RNDLEEVRQF LTSGVSPNLA NEDGLTALHQ CCIDDFQEMA
QQLLDAGADV NARDSECWTP LHAAATCGHL HLVELLISRG ADLLAVNSDG NMPYDLCEDA
QTLDCLETAM ANQGITQEGI EEARAVPELC MLNDLQNRLQ AGANLSDPLD HGATLLHIAA
ANGFSEVATL LLEQGASLSA KDHDGWEPLH AAAYWGQVHL VELLVAHGAD LNGKSLVDET
PLDVCGDEEV RAKLLELKHK QDALLRAQGR QRSLLRRRTS SAGSRGKVVR RVSLTHRTNL
YRKEHAQEAI VWQQPPPTSP EPLEDEDRQT DAELRLQPPE DDGPEVARPH NGQVGAPPGR
HLYSKRLDRS VSYHLSPEEN SAPDALVRDK AHHTLAELKR QRAAAKLQRP APEGPETFEP
GLSVDAGTSQ PDCGFSTIGD PPLLKLTAPS EEASVEKRPC CLLM
