PP16B_MOUSE
ID PP16B_MOUSE Reviewed; 568 AA.
AC Q8VHQ3;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein phosphatase 1 regulatory inhibitor subunit 16B;
DE AltName: Full=CAAX box protein TIMAP;
DE AltName: Full=TGF-beta-inhibited membrane-associated protein;
DE Flags: Precursor;
GN Name=Ppp1r16b;
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].
RC STRAIN=BALB/cJ; TISSUE=Cerebellum;
RX PubMed=12638124; DOI=10.1016/s1567-133x(02)00010-8;
RA Magdaleno S., Northcutt G.M., Curran T., Kurschner C.;
RT "mPPP1R16B is a novel mouse protein phosphatase 1 targeting subunit whose
RT mRNA is located in cell bodies and dendrites of neurons in four distinct
RT regions of the brain.";
RL Gene Expr. Patterns 1:143-149(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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).
RN [4]
RP FUNCTION, AND INDUCTION BY LPS.
RX PubMed=21907835; DOI=10.1016/j.resp.2011.08.012;
RA Poirier C., Gorshkov B.A., Zemskova M.A., Bogatcheva N.V., Verin A.D.;
RT "TIMAP protects endothelial barrier from LPS-induced vascular leakage and
RT is down-regulated by LPS.";
RL Respir. Physiol. Neurobiol. 179:334-337(2011).
CC -!- FUNCTION: Regulator of protein phosphatase 1 (PP1) that acts as a
CC positive regulator of pulmonary endothelial cell (EC) barrier function.
CC Protects the endothelial barrier from lipopolysaccharide (LPS)-induced
CC vascular leakage (PubMed:21907835). Involved in the regulation of the
CC PI3K/AKT signaling pathway (By similarity). Involved in the regulation
CC of angiogenesis and endothelial cell proliferation through the control
CC of ECE1 dephosphorylation, trafficking and activity (By similarity).
CC Involved in the regulation of endothelial cell filopodia extension (By
CC similarity). May be a downstream target for TGF-beta1 signaling cascade
CC in endothelial cells (By similarity). Involved in PKA-mediated moesin
CC dephosphorylation which is important in EC barrier protection against
CC thrombin stimulation. Promotes the interaction of PPP1CA with
CC RPSA/LAMR1 and in turn facilitates the dephosphorylation of RPSA/LAMR1
CC (By similarity). Involved in the dephosphorylation of EEF1A1 (By
CC similarity). {ECO:0000250|UniProtKB:Q95N27,
CC ECO:0000250|UniProtKB:Q96T49, ECO:0000269|PubMed:21907835}.
CC -!- SUBUNIT: Interacts with PPP1CA, PPP1CB and MSN. Interacts (via its
CC fourth ankyrin repeat) with the mature dimeric form of RPSA/LAMR1 (By
CC similarity). Interacts with EEF1A1 (By similarity). Interacts with PTEN
CC (By similarity). Interacts with ECE1 (By similarity).
CC {ECO:0000250|UniProtKB:Q95N27, ECO:0000250|UniProtKB:Q96T49}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96T49}.
CC Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Nucleus
CC {ECO:0000250|UniProtKB:Q96T49}. Cell projection
CC {ECO:0000250|UniProtKB:Q96T49}. Note=Colocalizes with RPSA/LAMR1 in the
CC cell membrane (By similarity). Localizes to the perinuclear region (By
CC similarity). Colocalizes with PTEN at the tip of EC projections (By
CC similarity). {ECO:0000250|UniProtKB:Q95N27,
CC ECO:0000250|UniProtKB:Q96T49}.
CC -!- INDUCTION: Inhibited by TGF-beta1 (Probable). Down-regulated by LPS
CC (PubMed:21907835). {ECO:0000269|PubMed:21907835, ECO:0000305}.
CC -!- PTM: Phosphorylated by PKA and, after PKA priming, by GSK3B.
CC Phosphorylation by GSK3B reduces its association with PP1C and enhances
CC PP1C activity. Dephosphorylation by its associated PP1C results in
CC enhanced association with PP1C, but reduced PP1C activity (By
CC similarity). {ECO:0000250|UniProtKB:Q95N27}.
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DR EMBL; AF423761; AAL62093.1; -; mRNA.
DR EMBL; BC054764; AAH54764.1; -; mRNA.
DR EMBL; BC057542; AAH57542.1; -; mRNA.
DR CCDS; CCDS16991.1; -.
DR RefSeq; NP_001153134.1; NM_001159662.1.
DR RefSeq; NP_694729.1; NM_153089.4.
DR RefSeq; XP_011237794.1; XM_011239492.2.
DR AlphaFoldDB; Q8VHQ3; -.
DR SMR; Q8VHQ3; -.
DR IntAct; Q8VHQ3; 1.
DR MINT; Q8VHQ3; -.
DR STRING; 10090.ENSMUSP00000062615; -.
DR iPTMnet; Q8VHQ3; -.
DR PhosphoSitePlus; Q8VHQ3; -.
DR MaxQB; Q8VHQ3; -.
DR PaxDb; Q8VHQ3; -.
DR PRIDE; Q8VHQ3; -.
DR ProteomicsDB; 289869; -.
DR Antibodypedia; 26914; 157 antibodies from 23 providers.
DR DNASU; 228852; -.
DR Ensembl; ENSMUST00000045503; ENSMUSP00000039540; ENSMUSG00000037754.
DR Ensembl; ENSMUST00000052927; ENSMUSP00000062615; ENSMUSG00000037754.
DR Ensembl; ENSMUST00000103116; ENSMUSP00000099405; ENSMUSG00000037754.
DR GeneID; 228852; -.
DR KEGG; mmu:228852; -.
DR UCSC; uc008nqo.2; mouse.
DR CTD; 26051; -.
DR MGI; MGI:2151841; Ppp1r16b.
DR VEuPathDB; HostDB:ENSMUSG00000037754; -.
DR eggNOG; KOG0505; Eukaryota.
DR GeneTree; ENSGT00940000154090; -.
DR HOGENOM; CLU_000134_54_2_1; -.
DR InParanoid; Q8VHQ3; -.
DR OMA; ISPDLCN; -.
DR OrthoDB; 564568at2759; -.
DR PhylomeDB; Q8VHQ3; -.
DR TreeFam; TF316803; -.
DR BioGRID-ORCS; 228852; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8VHQ3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8VHQ3; protein.
DR Bgee; ENSMUSG00000037754; Expressed in dorsal striatum and 198 other tissues.
DR ExpressionAtlas; Q8VHQ3; baseline and differential.
DR Genevisible; Q8VHQ3; MM.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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; ISO:MGI.
DR GO; GO:0061028; P:establishment of endothelial barrier; IMP:MGI.
DR GO; GO:1902309; P:negative regulation of peptidyl-serine dephosphorylation; ISO:MGI.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0035304; P:regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:1903670; P:regulation of sprouting angiogenesis; 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 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; Cell projection; Coiled coil; Lipoprotein;
KW Membrane; Methylation; Nucleus; Palmitate; Phosphoprotein; Prenylation;
KW Reference proteome; Repeat.
FT CHAIN 1..565
FT /note="Protein phosphatase 1 regulatory inhibitor subunit
FT 16B"
FT /id="PRO_0000067044"
FT PROPEP 566..568
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000396711"
FT REPEAT 100..129
FT /note="ANK 1"
FT REPEAT 133..162
FT /note="ANK 2"
FT REPEAT 228..257
FT /note="ANK 3"
FT REPEAT 261..290
FT /note="ANK 4"
FT REPEAT 531..560
FT /note="ANK 5"
FT REGION 373..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..55
FT /evidence="ECO:0000255"
FT COMPBIAS 382..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q95N27"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q95N27"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T49"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T49"
FT MOD_RES 565
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q923M0"
FT LIPID 564
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q923M0"
FT LIPID 565
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q923M0"
SQ SEQUENCE 568 AA; 63571 MW; 5D8446C81DEBA3D1 CRC64;
MASHVDLLTE LQLLEKVPTL ERLRAAQKRR AQQLKKWAQY EQDLLHRKRK HERKRSTGGR
RKKVSFEASV ALLEASLRND AEEVRYFLKN KVSPDLCNED GLTALHQCCI DNFEEIVKLL
LSHGANVNAK DNELWTPLHA AATCGHINLV KILVQYGADL LAVNSDGNMP YDLCEDEPTL
DVIETCMAYQ GITQEKINEM RAAPEQKMIS DIHCMIAAGQ DLDWIDGQGA TLLHIAGANG
YLRAAELLLD HGVRVDVKDW DGWEPLHAAA FWGQMPMAEL LVSHGASLSA RTSMDEMPID
LCEEEEFKVL LLELKHKHDV IMKSQLRHKS SLSRRTSSAG SRGKVVRRAS LSDRTNLYRK
EYEGEAILWQ QRSAAEDQRT STYNGDIRET RTDQENKDPN PRLEKPVLLS EFSTKISRGE
LDGPVENGLR APVSTYQYAL ANGDIWKMHE MPDYSMAYGN PGVADVPPPW SGFKEQSPQT
LLELKRQRAA AKLLSHPFLS THLGSSVARS GESSSEGKAP LIGGRTSPYS SNGTSVYYTV
TSGDPPLLKF KAPMEEMEEK VHGCCRIS
