PRUN1_MOUSE
ID PRUN1_MOUSE Reviewed; 454 AA.
AC Q8BIW1; Q80VU0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Exopolyphosphatase PRUNE1;
DE EC=3.6.1.1;
DE AltName: Full=PRUNEM1;
GN Name=Prune1; Synonyms=Prune;
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 DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10602478; DOI=10.1038/sj.onc.1203140;
RA Reymond A., Volorio S., Merla G., Al-Maghtheh M., Zuffardi O., Bulfone A.,
RA Ballabio A., Zollo M.;
RT "Evidence for interaction between human PRUNE and nm23-H1 NDPKinase.";
RL Oncogene 18:7244-7252(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Heart;
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 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; THR-411 AND SER-415, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Spleen, and Testis;
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: Phosphodiesterase (PDE) that has higher activity toward cAMP
CC than cGMP, as substrate. Plays a role in cell proliferation, migration
CC and differentiation, and acts as a negative regulator of NME1. Plays a
CC role in the regulation of neurogenesis. Involved in the regulation of
CC microtubule polymerization. {ECO:0000250|UniProtKB:Q86TP1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; EC=3.6.1.1;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by magnesium ions and inhibited by
CC manganese ions. Inhibited by dipyridamole, moderately sensitive to IBMX
CC and inhibited by vinpocetine (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Able to homodimerize via its C-terminal domain.
CC Interacts with NME1. Interacts with GSK3; at focal adhesion complexes
CC where paxillin and vinculin are colocalized. Interacts with alpha and
CC beta tubulin. {ECO:0000250|UniProtKB:Q86TP1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cell junction, focal adhesion {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: In the developing embryo, a high level of
CC expression is confined to the nervous system particularly in the dorsal
CC root ganglia, cranial nerves, and neural retina. From 10.5 dpc,
CC expressed at low levels in the basal plate along the entire neural
CC tube, while at 12.5 dpc the expression in the nervous system is
CC definitively stronger, especially in the cranial and dorsal root
CC ganglia and in the spinal nerves. In the hypothalamus, the expression
CC is confined to the retro-chiasmatic area (RCH) and is also detectable
CC in the remnant of the Rathke's pouch. In the developing eye,
CC exclusively expressed in the prospective neural retina, equally
CC distributed in both the deep and superficial layers. At 16.5 dpc,
CC expression is still detectable in the outer neuroblast layer of the
CC neural retina. {ECO:0000269|PubMed:10602478}.
CC -!- SIMILARITY: Belongs to the PPase class C family. Prune subfamily.
CC {ECO:0000305}.
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DR EMBL; AF051908; AAC95291.2; -; mRNA.
DR EMBL; AK081637; BAC38278.1; -; mRNA.
DR EMBL; AK142160; BAE24953.1; -; mRNA.
DR EMBL; BC057546; AAH57546.1; -; mRNA.
DR EMBL; BC058635; AAH58635.1; -; mRNA.
DR CCDS; CCDS17610.1; -.
DR RefSeq; NP_775482.1; NM_173347.2.
DR AlphaFoldDB; Q8BIW1; -.
DR SMR; Q8BIW1; -.
DR BioGRID; 230866; 13.
DR IntAct; Q8BIW1; 2.
DR STRING; 10090.ENSMUSP00000015855; -.
DR iPTMnet; Q8BIW1; -.
DR PhosphoSitePlus; Q8BIW1; -.
DR EPD; Q8BIW1; -.
DR MaxQB; Q8BIW1; -.
DR PaxDb; Q8BIW1; -.
DR PeptideAtlas; Q8BIW1; -.
DR PRIDE; Q8BIW1; -.
DR ProteomicsDB; 291536; -.
DR Antibodypedia; 34044; 216 antibodies from 27 providers.
DR Ensembl; ENSMUST00000015855; ENSMUSP00000015855; ENSMUSG00000015711.
DR GeneID; 229589; -.
DR KEGG; mmu:229589; -.
DR UCSC; uc008qiz.1; mouse.
DR CTD; 58497; -.
DR MGI; MGI:1925152; Prune1.
DR VEuPathDB; HostDB:ENSMUSG00000015711; -.
DR eggNOG; KOG4129; Eukaryota.
DR GeneTree; ENSGT00450000040262; -.
DR HOGENOM; CLU_019358_2_0_1; -.
DR InParanoid; Q8BIW1; -.
DR OMA; HSRKRVA; -.
DR OrthoDB; 1545660at2759; -.
DR PhylomeDB; Q8BIW1; -.
DR TreeFam; TF323914; -.
DR BioGRID-ORCS; 229589; 15 hits in 73 CRISPR screens.
DR ChiTaRS; Prune1; mouse.
DR PRO; PR:Q8BIW1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BIW1; protein.
DR Bgee; ENSMUSG00000015711; Expressed in extensor digitorum longus and 275 other tissues.
DR Genevisible; Q8BIW1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004309; F:exopolyphosphatase activity; IBA:GO_Central.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:0050767; P:regulation of neurogenesis; ISO:MGI.
DR Gene3D; 3.10.310.20; -; 1.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR004097; DHHA2.
DR InterPro; IPR038222; DHHA2_dom_sf.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02833; DHHA2; 1.
DR SMART; SM01131; DHHA2; 1.
DR SUPFAM; SSF64182; SSF64182; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell junction; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..454
FT /note="Exopolyphosphatase PRUNE1"
FT /id="PRO_0000337988"
FT REGION 394..421
FT /note="Essential for homodimerization"
FT /evidence="ECO:0000250"
FT REGION 397..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 106..108
FT /note="DHH motif"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q86TP1"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 75
FT /note="E -> A (in Ref. 1; AAC95291)"
FT /evidence="ECO:0000305"
FT CONFLICT 397..398
FT /note="SG -> LW (in Ref. 1; AAC95291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 50239 MW; 646FBF6B345028E6 CRC64;
MEDYLQDCRA ALQDSRPLHV VLGNEACDLD SMVSALALAF YLTKTSEAED IFIPVLNIKR
SELPLRGDNV FFLQEVKIPE PALIFRDEID LLALHQAGQL TLILVDHHIL PKSDAALEEA
VAEVLDHRPI EQKYCPPCHV SVELVGSCAT LVTERILQGA PETLDRQTAA LLHGTIILDC
VNMDTNIGKA TPKDSKYVEE LEALFPDLPK RKDIFDSLQK AKFDVSGLTT EQMLRKDQKT
VYRQGTKVAI SAIYMDLKAF LQRTDLFTDL SSFCHDHSYD ALVAMTIFFN TQNEPVRQLA
IFCPHEALRM TICGILERST SPPLKLTPIP STSPNLQAYH QGNTQVSRKK LLPVLQEALS
AYLDSAKMAS GQSEVAVGMS REQVDKDLDK ASNSLISGLS QDEEDPPLPP TPMNSLVDEC
PLDQGLPKFS AEAVFEKCSQ ISLSQSARAC TSNK
