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Protein

Protein prune homolog

Gene

Prune

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Phosphodiesterase (PDE) that has higher activity toward cAMP than cGMP, as substrate. Plays a role in cell proliferation, is able to induce cell motility and acts as a negative regulator of NME1 (By similarity).By similarity

Catalytic activityi

Diphosphate + H2O = 2 phosphate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Enzyme regulationi

Activated by magnesium ions and inhibited by manganese ions. Inhibited by dipyridamole, moderately sensitive to IBMX and inhibited by vinpocetine (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi28 – 281Manganese 1By similarity
Metal bindingi30 – 301Manganese 2By similarity
Metal bindingi106 – 1061Manganese 1By similarity
Metal bindingi106 – 1061Manganese 2By similarity
Metal bindingi179 – 1791Manganese 2By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein prune homolog (EC:3.6.1.1)
Gene namesi
Name:Prune
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi1359521. Prune.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Protein prune homologPRO_0000337989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei400 – 4001PhosphoserineCombined sources
Modified residuei411 – 4111PhosphothreonineBy similarity
Modified residuei415 – 4151PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ6AYG3.
PRIDEiQ6AYG3.

PTM databases

iPTMnetiQ6AYG3.
PhosphoSiteiQ6AYG3.

Expressioni

Gene expression databases

GenevisibleiQ6AYG3. RN.

Interactioni

Subunit structurei

Homooligomer. Able to homodimerize via its C-terminal domain. Interacts with NME1. Interacts with GSK3; at focal adhesion complexes where paxillin and vinculin are colocalized.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028677.

Structurei

3D structure databases

ProteinModelPortaliQ6AYG3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni394 – 42128Essential for homodimerizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi106 – 1083DHH motifBy similarity

Sequence similaritiesi

Belongs to the PPase class C family. Prune subfamily.Curated

Phylogenomic databases

eggNOGiKOG4129. Eukaryota.
COG1227. LUCA.
GeneTreeiENSGT00450000040262.
HOGENOMiHOG000115724.
HOVERGENiHBG058142.
InParanoidiQ6AYG3.
KOiK01514.
OMAiALRTTIC.
OrthoDBiEOG7327PG.
PhylomeDBiQ6AYG3.
TreeFamiTF323914.

Family and domain databases

InterProiIPR001667. DDH_dom.
IPR004097. DHHA2.
[Graphical view]
PfamiPF01368. DHH. 1 hit.
PF02833. DHHA2. 1 hit.
[Graphical view]
SMARTiSM01131. DHHA2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6AYG3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDYLQDCRA ALQESRPLHV VLGNEACDLD SMVSALALAF YLTKTSEAED
60 70 80 90 100
IFIPVLNIKR SELPLRGDNV FFLQEVKIAE SALIFRDEID LLALHQAGQL
110 120 130 140 150
TLILVDHHML PKSDAALEEA VAEVLDHRPI EQKYCPPCHV SVELVGSCAT
160 170 180 190 200
LVAERILQGA PETLDRQTAA LLHGTIILDC VNMDAKIGKA TLKDNEYVEK
210 220 230 240 250
LEALFPDLPK RKDIFDSLQK AKFDVSGLTT EQMLRKDQKT IYRQGTKVAV
260 270 280 290 300
SAVYMDLEAF LQRSGLLSDL SAFCQDHSYD ALVAMAIFFN THNEPVRQLA
310 320 330 340 350
IFCPHEALRM TICGVLEQST SPALKLTPIP SISAHLQAYL QGNTQVSRKK
360 370 380 390 400
LLPVLQEALS AYLDSMRTPA GQLEAALGMS REQADKELDK ASNSLIAGLS
410 420 430 440 450
QDDEDPPLPP TPMNSLVDEC PLDQGLPKLS AEAVFEKCSQ ISLSQSTRAC

PSNK
Length:454
Mass (Da):49,998
Last modified:September 13, 2004 - v1
Checksum:i3DE36BDFB273C6A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079054 mRNA. Translation: AAH79054.1.
RefSeqiNP_001007698.1. NM_001007697.1.
UniGeneiRn.214534.

Genome annotation databases

EnsembliENSRNOT00000028677; ENSRNOP00000028677; ENSRNOG00000021120.
GeneIDi310664.
KEGGirno:310664.
UCSCiRGD:1359521. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079054 mRNA. Translation: AAH79054.1.
RefSeqiNP_001007698.1. NM_001007697.1.
UniGeneiRn.214534.

3D structure databases

ProteinModelPortaliQ6AYG3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028677.

PTM databases

iPTMnetiQ6AYG3.
PhosphoSiteiQ6AYG3.

Proteomic databases

PaxDbiQ6AYG3.
PRIDEiQ6AYG3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028677; ENSRNOP00000028677; ENSRNOG00000021120.
GeneIDi310664.
KEGGirno:310664.
UCSCiRGD:1359521. rat.

Organism-specific databases

CTDi58497.
RGDi1359521. Prune.

Phylogenomic databases

eggNOGiKOG4129. Eukaryota.
COG1227. LUCA.
GeneTreeiENSGT00450000040262.
HOGENOMiHOG000115724.
HOVERGENiHBG058142.
InParanoidiQ6AYG3.
KOiK01514.
OMAiALRTTIC.
OrthoDBiEOG7327PG.
PhylomeDBiQ6AYG3.
TreeFamiTF323914.

Miscellaneous databases

PROiQ6AYG3.

Gene expression databases

GenevisibleiQ6AYG3. RN.

Family and domain databases

InterProiIPR001667. DDH_dom.
IPR004097. DHHA2.
[Graphical view]
PfamiPF01368. DHH. 1 hit.
PF02833. DHHA2. 1 hit.
[Graphical view]
SMARTiSM01131. DHHA2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPRUNE_RAT
AccessioniPrimary (citable) accession number: Q6AYG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: September 13, 2004
Last modified: June 8, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.