PP14D_MOUSE
ID PP14D_MOUSE Reviewed; 146 AA.
AC Q7TT52; A2AV57; Q9D878;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 14D;
DE AltName: Full=Gastrointestinal and brain-specific PP1-inhibitory protein 1;
DE Short=GBPI-1;
GN Name=Ppp1r14d; Synonyms=Gbpi;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12974676; DOI=10.1042/bj20030128;
RA Liu Q.-R., Zhang P.-W., Lin Z., Li Q.-F., Woods A.S., Troncoso J.,
RA Uhl G.R.;
RT "GBPI, a novel gastrointestinal- and brain-specific PP1-inhibitory protein,
RT is activated by PKC and inactivated by PKA.";
RL Biochem. J. 377:171-181(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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: Inhibitor of PPP1CA. Has inhibitory activity only when
CC phosphorylated, creating a molecular switch for regulating the
CC phosphorylation status of PPP1CA substrates and smooth muscle
CC contraction (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=GBPI-1;
CC IsoId=Q7TT52-1; Sequence=Displayed;
CC Name=2; Synonyms=GBPI-2;
CC IsoId=Q7TT52-2; Sequence=VSP_011842;
CC -!- TISSUE SPECIFICITY: Isoform 1 is detected in intestine, kidney, lung,
CC spleen, stomach and brain. Isoform 2 is detected in testis.
CC {ECO:0000269|PubMed:12974676}.
CC -!- PTM: Phosphorylated on several residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PP1 inhibitor family. {ECO:0000305}.
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DR EMBL; AY179331; AAO47399.1; -; mRNA.
DR EMBL; AF408400; AAK97532.1; -; mRNA.
DR EMBL; AK008348; BAB25620.1; -; mRNA.
DR EMBL; AL929318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024547; AAH24547.1; -; mRNA.
DR CCDS; CCDS16596.1; -. [Q7TT52-1]
DR CCDS; CCDS71118.1; -. [Q7TT52-2]
DR RefSeq; NP_001277725.1; NM_001290796.1. [Q7TT52-2]
DR RefSeq; NP_082380.1; NM_028104.4. [Q7TT52-1]
DR AlphaFoldDB; Q7TT52; -.
DR STRING; 10090.ENSMUSP00000075453; -.
DR iPTMnet; Q7TT52; -.
DR PhosphoSitePlus; Q7TT52; -.
DR PaxDb; Q7TT52; -.
DR PRIDE; Q7TT52; -.
DR ProteomicsDB; 289372; -. [Q7TT52-1]
DR ProteomicsDB; 289373; -. [Q7TT52-2]
DR Antibodypedia; 49878; 65 antibodies from 23 providers.
DR DNASU; 72112; -.
DR Ensembl; ENSMUST00000076084; ENSMUSP00000075453; ENSMUSG00000027317. [Q7TT52-1]
DR Ensembl; ENSMUST00000110820; ENSMUSP00000106444; ENSMUSG00000027317. [Q7TT52-2]
DR GeneID; 72112; -.
DR KEGG; mmu:72112; -.
DR UCSC; uc008ltj.3; mouse. [Q7TT52-1]
DR UCSC; uc012cbr.2; mouse. [Q7TT52-2]
DR CTD; 54866; -.
DR MGI; MGI:1919362; Ppp1r14d.
DR VEuPathDB; HostDB:ENSMUSG00000027317; -.
DR eggNOG; ENOG502RZZY; Eukaryota.
DR GeneTree; ENSGT00950000182985; -.
DR HOGENOM; CLU_114155_0_0_1; -.
DR InParanoid; Q7TT52; -.
DR OMA; PDEGQRT; -.
DR OrthoDB; 1286840at2759; -.
DR PhylomeDB; Q7TT52; -.
DR TreeFam; TF105546; -.
DR BioGRID-ORCS; 72112; 4 hits in 75 CRISPR screens.
DR PRO; PR:Q7TT52; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q7TT52; protein.
DR Bgee; ENSMUSG00000027317; Expressed in small intestine Peyer's patch and 37 other tissues.
DR Genevisible; Q7TT52; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; ISS:UniProtKB.
DR GO; GO:1905183; P:negative regulation of protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:1905184; P:positive regulation of protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042325; P:regulation of phosphorylation; IEA:InterPro.
DR Gene3D; 1.10.150.220; -; 1.
DR InterPro; IPR008025; CPI-17.
DR InterPro; IPR036658; CPI-17_sf.
DR PANTHER; PTHR16188; PTHR16188; 1.
DR Pfam; PF05361; PP1_inhibitor; 1.
DR SUPFAM; SSF81790; SSF81790; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..146
FT /note="Protein phosphatase 1 regulatory subunit 14D"
FT /id="PRO_0000071498"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..25
FT /note="Interaction with protein phosphatase 1"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 87..146
FT /note="GQEESSEPEIDLEALMDLSTEDQRTQLEAILQDCPGNREPFISELLSQLKRL
FT RRLSRPSK -> TSQGKSSQATEEGSSQRTHFTRVKKNLLSQRLIWKLSWTCQQKIKGH
FT SWRPFSKTAQATESLLSLSYSVNSRDFGDSAGLRNNPGGTIS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12974676"
FT /id="VSP_011842"
SQ SEQUENCE 146 AA; 16817 MW; E2C217525CC46271 CRC64;
MLSSSPASCT SPSPGTDNPD KKVHWASEKR RRASSTDSES KTHLDISKLP RSRRPSRLTV
KYDRGHLQRW LEMEQWVDAQ VQELFQGQEE SSEPEIDLEA LMDLSTEDQR TQLEAILQDC
PGNREPFISE LLSQLKRLRR LSRPSK
