PRUN1_RAT
ID PRUN1_RAT Reviewed; 454 AA.
AC Q6AYG3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Exopolyphosphatase PRUNE1;
DE EC=3.6.1.1;
GN Name=Prune1; Synonyms=Prune;
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 [LARGE SCALE MRNA].
RC 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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SIMILARITY: Belongs to the PPase class C family. Prune subfamily.
CC {ECO:0000305}.
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DR EMBL; BC079054; AAH79054.1; -; mRNA.
DR RefSeq; NP_001007698.1; NM_001007697.1.
DR AlphaFoldDB; Q6AYG3; -.
DR SMR; Q6AYG3; -.
DR STRING; 10116.ENSRNOP00000028677; -.
DR iPTMnet; Q6AYG3; -.
DR PhosphoSitePlus; Q6AYG3; -.
DR jPOST; Q6AYG3; -.
DR PaxDb; Q6AYG3; -.
DR PRIDE; Q6AYG3; -.
DR Ensembl; ENSRNOT00000028677; ENSRNOP00000028677; ENSRNOG00000021120.
DR GeneID; 310664; -.
DR KEGG; rno:310664; -.
DR UCSC; RGD:1359521; rat.
DR CTD; 58497; -.
DR RGD; 1359521; Prune1.
DR eggNOG; KOG4129; Eukaryota.
DR GeneTree; ENSGT00450000040262; -.
DR HOGENOM; CLU_019358_2_0_1; -.
DR InParanoid; Q6AYG3; -.
DR OMA; HSRKRVA; -.
DR OrthoDB; 1545660at2759; -.
DR PhylomeDB; Q6AYG3; -.
DR TreeFam; TF323914; -.
DR PRO; PR:Q6AYG3; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000021120; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q6AYG3; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:RGD.
DR GO; GO:0015631; F:tubulin binding; ISO:RGD.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISO:RGD.
DR GO; GO:0050767; P:regulation of neurogenesis; ISO:RGD.
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_0000337989"
FT REGION 394..421
FT /note="Essential for homodimerization"
FT /evidence="ECO:0000250"
FT REGION 398..421
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:22673903"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIW1"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIW1"
SQ SEQUENCE 454 AA; 49998 MW; 3DE36BDFB273C6A0 CRC64;
MEDYLQDCRA ALQESRPLHV VLGNEACDLD SMVSALALAF YLTKTSEAED IFIPVLNIKR
SELPLRGDNV FFLQEVKIAE SALIFRDEID LLALHQAGQL TLILVDHHML PKSDAALEEA
VAEVLDHRPI EQKYCPPCHV SVELVGSCAT LVAERILQGA PETLDRQTAA LLHGTIILDC
VNMDAKIGKA TLKDNEYVEK LEALFPDLPK RKDIFDSLQK AKFDVSGLTT EQMLRKDQKT
IYRQGTKVAV SAVYMDLEAF LQRSGLLSDL SAFCQDHSYD ALVAMAIFFN THNEPVRQLA
IFCPHEALRM TICGVLEQST SPALKLTPIP SISAHLQAYL QGNTQVSRKK LLPVLQEALS
AYLDSMRTPA GQLEAALGMS REQADKELDK ASNSLIAGLS QDDEDPPLPP TPMNSLVDEC
PLDQGLPKLS AEAVFEKCSQ ISLSQSTRAC PSNK
