Hmdb loader
Identification
HMDB Protein ID HMDBP08160
Secondary Accession Numbers
  • 13871
Name Protein prune homolog
Synonyms
  1. DRES-17
  2. DRES17
  3. Drosophila-related expressed sequence 17
  4. HTcD37
  5. hPrune
Gene Name PRUNE
Protein Type Unknown
Biological Properties
General Function Involved in pyrophosphatase activity
Specific Function 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.
Pathways
  • Purine metabolism
Reactions
Pyrophosphate + Water → Phosphate details
Guanosine 3'-diphosphate 5'-triphosphate + Water → Guanosine 3',5'-bis(diphosphate) + Phosphate details
GO Classification
Cellular Component
focal adhesion
cytoplasm
nucleus
Component
cell part
intracellular part
cytoplasm
Function
manganese ion binding
ion binding
cation binding
metal ion binding
binding
catalytic activity
hydrolase activity
transition metal ion binding
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
Molecular Function
manganese ion binding
inorganic diphosphatase activity
Cellular Location
  1. Nucleus
  2. Cytoplasm
  3. Cell junction
  4. focal adhesion
Gene Properties
Chromosome Location 1
Locus 1q21
SNPs PRUNE
Gene Sequence
>1362 bp
ATGGAGGACTACCTGCAGGGTTGTCGAGCTGCTCTGCAGGAGTCCCGACCTCTACATGTT
GTGCTGGGAAATGAAGCCTGTGATTTGGACTCCACAGTGTCTGCTCTTGCCCTGGCTTTT
TACCTAGCAAAGACAACTGAGGCTGAGGAAGTCTTTGTGCCAGTTTTAAATATAAAACGT
TCTGAACTACCTCTGCGAGGTGACATTGTCTTCTTTCTTCAGAAGGTTCATATTCCAGAG
AGTATCTTGATTTTTCGGGATGAGATTGACCTCCATGCATTATACCAGGCTGGCCAACTC
ACCCTCATCCTTGTCGACCATCATATCTTATCCAAAAGTGACACAGCCCTAGAGGAGGCA
GTAGCAGAGGTGCTAGACCATCGACCCATCGAGCCGAAACACTGCCCTCCCTGCCATGTT
TCAGTTGAGCTGGTGGGGTCCTGTGCTACCCTGGTGACCGAGAGAATCCTGCAGGGGGCA
CCAGAGATCTTGGACAGGCAAACTGCAGCCCTTCTGCATGGAACCATCATCCTGGACTGT
GTCAACATGGACCTTAAAATTGGAAAGGCAACCCCAAAGGACAGCAAATATGTGGAGAAA
CTAGAGGCCCTTTTCCCAGACCTACCCAAGAGAAATGATATATTTGATTCCCTACAAAAG
GTAAAGTTTGATGTATCAGGACTGACCACTGAGCAGATGCTGAGAAAAGACCAGAAGACT
ATCTATAGACAAGGCGTCAAGGTGGCCATTAGTGCAATATATATGGATTTGGAGGCCTTT
CTGCAGAGGTCTAACCTCCTTGCAGATCTCCATGCTTTCTGCCAGGCTCACAGCTATGAT
GTCCTGGTTGCCATGACTATCTTTTTCAACACTCACAATGAGCCAGTGCGGCAGTTGGCT
ATTTTCTGTCCCCATGTGGCACTCCAAACAACGATCTGTGAAGTCCTGGAACGCTCCCAC
TCTCCACCCCTGAAGCTGACCCCTGCCTCAAGTACCCACCCTAACCTCCATGCCTATCTT
CAAGGCAACACCCAGGTCTCTCGAAAGAAACTTCTGCCCCTGCTCCAGGAAGCCCTGTCA
GCATATTTTGACTCCATGAAGATCCCTTCAGGACAGCCTGAGACAGCAGATGTGTCCAGG
GAGCAAGTGGACAAGGAATTGGACAGGGCAAGTAACTCCCTGATTTCTGGACTGAGTCAA
GATGAGGAGGACCCTCCGCTGCCCCCGACGCCCATGAACAGCTTGGTGGATGAGTGCCCT
CTAGATCAGGGGCTGCCTAAACTCTCTGCTGAGGCCGTCTTCGAGAAGTGCAGTCAGATC
TCACTGTCACAGTCTACCACAGCCTCCCTGTCCAAGAAGTGA
Protein Properties
Number of Residues 453
Molecular Weight 50199.04
Theoretical pI 5.502
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Protein prune homolog
MEDYLQGCRAALQESRPLHVVLGNEACDLDSTVSALALAFYLAKTTEAEEVFVPVLNIKR
SELPLRGDIVFFLQKVHIPESILIFRDEIDLHALYQAGQLTLILVDHHILSKSDTALEEA
VAEVLDHRPIEPKHCPPCHVSVELVGSCATLVTERILQGAPEILDRQTAALLHGTIILDC
VNMDLKIGKATPKDSKYVEKLEALFPDLPKRNDIFDSLQKAKFDVSGLTTEQMLRKDQKT
IYRQGVKVAISAIYMDLEAFLQRSNLLADLHAFCQAHSYDVLVAMTIFFNTHNEPVRQLA
IFCPHVALQTTICEVLERSHSPPLKLTPASSTHPNLHAYLQGNTQVSRKKLLPLLQEALS
AYFDSMKIPSGQPETADVSREQVDKELDRASNSLISGLSQDEEDPPLPPTPMNSLVDECP
LDQGLPKLSAEAVFEKCSQISLSQSTTASLSKK
GenBank ID Protein 4007408
UniProtKB/Swiss-Prot ID Q86TP1
UniProtKB/Swiss-Prot Entry Name PRUNE_HUMAN
PDB IDs Not Available
GenBank Gene ID AF051907
GeneCard ID PRUNE
GenAtlas ID PRUNE
HGNC ID HGNC:13420
References
General References
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  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  5. Garzia L, D'Angelo A, Amoresano A, Knauer SK, Cirulli C, Campanella C, Stauber RH, Steegborn C, Iolascon A, Zollo M: Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility. Oncogene. 2008 Mar 20;27(13):1853-64. Epub 2007 Oct 1. [PubMed:17906697 ]
  6. Kobayashi T, Hino S, Oue N, Asahara T, Zollo M, Yasui W, Kikuchi A: Glycogen synthase kinase 3 and h-prune regulate cell migration by modulating focal adhesions. Mol Cell Biol. 2006 Feb;26(3):898-911. [PubMed:16428445 ]
  7. Reymond A, Volorio S, Merla G, Al-Maghtheh M, Zuffardi O, Bulfone A, Ballabio A, Zollo M: Evidence for interaction between human PRUNE and nm23-H1 NDPKinase. Oncogene. 1999 Dec 2;18(51):7244-52. [PubMed:10602478 ]
  8. Volorio S, Simon G, Repetto M, Cucciardi M, Banfi S, Borsani G, Ballabio A, Zollo M: Sequencing analysis of forty-eight human image cDNA clones similar to Drosophila mutant protein. DNA Seq. 1998;9(5-6):307-15. [PubMed:10524757 ]
  9. Forus A, D'Angelo A, Henriksen J, Merla G, Maelandsmo GM, Florenes VA, Olivieri S, Bjerkehagen B, Meza-Zepeda LA, del Vecchio Blanco F, Muller C, Sanvito F, Kononen J, Nesland JM, Fodstad O, Reymond A, Kallioniemi OP, Arrigoni G, Ballabio A, Myklebost O, Zollo M: Amplification and overexpression of PRUNE in human sarcomas and breast carcinomas-a possible mechanism for altering the nm23-H1 activity. Oncogene. 2001 Oct 18;20(47):6881-90. [PubMed:11687967 ]
  10. D'Angelo A, Garzia L, Andre A, Carotenuto P, Aglio V, Guardiola O, Arrigoni G, Cossu A, Palmieri G, Aravind L, Zollo M: Prune cAMP phosphodiesterase binds nm23-H1 and promotes cancer metastasis. Cancer Cell. 2004 Feb;5(2):137-49. [PubMed:14998490 ]
  11. Zollo M, Andre A, Cossu A, Sini MC, D'Angelo A, Marino N, Budroni M, Tanda F, Arrigoni G, Palmieri G: Overexpression of h-prune in breast cancer is correlated with advanced disease status. Clin Cancer Res. 2005 Jan 1;11(1):199-205. [PubMed:15671547 ]
  12. Middelhaufe S, Garzia L, Ohndorf UM, Kachholz B, Zollo M, Steegborn C: Domain mapping on the human metastasis regulator protein h-Prune reveals a C-terminal dimerization domain. Biochem J. 2007 Oct 15;407(2):199-205. [PubMed:17655525 ]