PRUN1_BOVIN
ID PRUN1_BOVIN Reviewed; 453 AA.
AC Q5E9Y6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Exopolyphosphatase PRUNE1;
DE EC=3.6.1.1;
GN Name=PRUNE1; Synonyms=PRUNE;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphodiesterase (PDE) that has higher activity toward cAMP
CC than cGMP, as substrate. Plays a role in cell proliferation, is able to
CC induce cell motility and acts as a negative regulator of NME1 (By
CC similarity). {ECO:0000250}.
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. {ECO:0000250}.
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; BT020783; AAX08800.1; -; mRNA.
DR EMBL; BC142289; AAI42290.1; -; mRNA.
DR RefSeq; NP_001030429.1; NM_001035352.1.
DR AlphaFoldDB; Q5E9Y6; -.
DR SMR; Q5E9Y6; -.
DR STRING; 9913.ENSBTAP00000020388; -.
DR PaxDb; Q5E9Y6; -.
DR PRIDE; Q5E9Y6; -.
DR Ensembl; ENSBTAT00000020388; ENSBTAP00000020388; ENSBTAG00000015336.
DR GeneID; 524973; -.
DR KEGG; bta:524973; -.
DR CTD; 58497; -.
DR VEuPathDB; HostDB:ENSBTAG00000015336; -.
DR VGNC; VGNC:33428; PRUNE1.
DR eggNOG; KOG4129; Eukaryota.
DR GeneTree; ENSGT00450000040262; -.
DR HOGENOM; CLU_019358_2_0_1; -.
DR InParanoid; Q5E9Y6; -.
DR OMA; HSRKRVA; -.
DR OrthoDB; 1545660at2759; -.
DR TreeFam; TF323914; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000015336; Expressed in biceps femoris and 106 other tissues.
DR ExpressionAtlas; Q5E9Y6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 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 2: Evidence at transcript level;
KW Acetylation; Cell junction; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..453
FT /note="Exopolyphosphatase PRUNE1"
FT /id="PRO_0000337986"
FT REGION 393..420
FT /note="Essential for homodimerization"
FT /evidence="ECO:0000250"
FT REGION 396..419
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 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIW1"
FT MOD_RES 410
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIW1"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIW1"
SQ SEQUENCE 453 AA; 50080 MW; EB2425D394BBBA30 CRC64;
MENYLQGCRA ALQESRPIHV VLGNEACDLD SMVSALALAF YLAKTTEAEE VFVPVLNIKR
SELPLRGDNV FFLQKIHIPE SVLIFRDEID LHALHQAGQL TLILVDHHVL PKSDAALEEA
VAEVLDHRPI DQRHCPPCHV SVELVGSCAT LVAERILQGA PEILDRQTAA LLHGTILLDC
VNMDLKIGKA TLKDSHYVEK LEALFPDLPS RNDIFDSLQK AKFDVSGLTT EQMLRKDQKT
ISRQGTKVAI SAIYMDMEAF LQRSGLLADL RAFCQAHSYD ALVAMTIFFN TYNEPVRQLA
VFCPHAALRM TICGILEHSH SPPLKLTPVP SSHPDLQAYL QGNTQISRKK VLPLLQEALS
AYFDSTNIPL GQPETEGVSR EQVDKELDRA GNSLLSGLSQ DEEEPPLPPT PMNSLVDECP
LDQGLPKFSA EVIFEKCSQI SLSEPTTASL SKK
