Full text data of PRUNE
PRUNE
[Confidence: low (only semi-automatic identification from reviews)]
Protein prune homolog; hPrune; 3.6.1.1 (Drosophila-related expressed sequence 17; DRES-17; DRES17; HTcD37)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein prune homolog; hPrune; 3.6.1.1 (Drosophila-related expressed sequence 17; DRES-17; DRES17; HTcD37)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q86TP1
ID PRUNE_HUMAN Reviewed; 453 AA.
AC Q86TP1; B2RCH8; B4DFL7; Q5SZF9; Q659E5; Q6P4E0; Q8N654; Q96JU5;
read moreAC Q9C071; Q9C072; Q9UIV0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 22-JAN-2014, entry version 81.
DE RecName: Full=Protein prune homolog;
DE Short=hPrune;
DE EC=3.6.1.1;
DE AltName: Full=Drosophila-related expressed sequence 17;
DE Short=DRES-17;
DE Short=DRES17;
DE AltName: Full=HTcD37;
GN Name=PRUNE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP INTERACTION WITH NME1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10602478; DOI=10.1038/sj.onc.1203140;
RA Reymond A., Volorio S., Merla G., Al-Maghtheh M., Zuffardi O.,
RA Bulfone A., 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 [MRNA] (ISOFORMS 2 AND 4).
RA Zollo M., Volorio S.;
RT "Human Prune homolog.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 7), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 211-453 (ISOFORMS 1/3).
RC TISSUE=Brain cortex, Kidney, and Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 6).
RC TISSUE=Blood, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-453 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10524757;
RA Volorio S., Simon G., Repetto M., Cucciardi M., Banfi S., Borsani G.,
RA Ballabio A., Zollo M.;
RT "Sequencing analysis of forty-eight human image cDNA clones similar to
RT Drosophila mutant protein.";
RL DNA Seq. 9:307-315(1998).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-453 (ISOFORMS
RP 1/2/3/4/5/6/7).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=11687967; DOI=10.1038/sj.onc.1204874;
RA Forus A., D'Angelo A., Henriksen J., Merla G., Maelandsmo G.M.,
RA Floerenes V.A., Olivieri S., Bjerkehagen B., Meza-Zepeda L.A.,
RA del Vecchio Blanco F., Mueller C., Sanvito F., Kononen J.,
RA Nesland J.M., Fodstad O., Reymond A., Kallioniemi O.-P., Arrigoni G.,
RA Ballabio A., Myklebost O., Zollo M.;
RT "Amplification and overexpression of PRUNE in human sarcomas and
RT breast carcinomas-a possible mechanism for altering the nm23-H1
RT activity.";
RL Oncogene 20:6881-6890(2001).
RN [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH NME1, ENZYME
RP REGULATION, AND MUTAGENESIS OF ASP-28; ASP-106; 126-ASP--PRO-129 AND
RP ASP-179.
RX PubMed=14998490; DOI=10.1016/S1535-6108(04)00021-2;
RA D'Angelo A., Garzia L., Andre A., Carotenuto P., Aglio V.,
RA Guardiola O., Arrigoni G., Cossu A., Palmieri G., Aravind L.,
RA Zollo M.;
RT "Prune cAMP phosphodiesterase binds nm23-H1 and promotes cancer
RT metastasis.";
RL Cancer Cell 5:137-149(2004).
RN [11]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15671547;
RA Zollo M., Andre A., Cossu A., Sini M.C., D'Angelo A., Marino N.,
RA Budroni M., Tanda F., Arrigoni G., Palmieri G.;
RT "Overexpression of h-prune in breast cancer is correlated with
RT advanced disease status.";
RL Clin. Cancer Res. 11:199-205(2005).
RN [12]
RP INTERACTION WITH GSK3B, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16428445; DOI=10.1128/MCB.26.3.898-911.2006;
RA Kobayashi T., Hino S., Oue N., Asahara T., Zollo M., Yasui W.,
RA Kikuchi A.;
RT "Glycogen synthase kinase 3 and h-prune regulate cell migration by
RT modulating focal adhesions.";
RL Mol. Cell. Biol. 26:898-911(2006).
RN [13]
RP INTERACTION WITH NME1, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=17655525; DOI=10.1042/BJ20070408;
RA Middelhaufe S., Garzia L., Ohndorf U.M., Kachholz B., Zollo M.,
RA Steegborn C.;
RT "Domain mapping on the human metastasis regulator protein h-Prune
RT reveals a C-terminal dimerization domain.";
RL Biochem. J. 407:199-205(2007).
RN [14]
RP INTERACTION WITH NME1, AND FUNCTION.
RX PubMed=17906697; DOI=10.1038/sj.onc.1210822;
RA Garzia L., D'Angelo A., Amoresano A., Knauer S.K., Cirulli C.,
RA Campanella C., Stauber R.H., Steegborn C., Iolascon A., Zollo M.;
RT "Phosphorylation of nm23-H1 by CKI induces its complex formation with
RT h-prune and promotes cell motility.";
RL Oncogene 27:1853-1864(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Phosphodiesterase (PDE) that has higher activity toward
CC cAMP than cGMP, as substrate. Plays a role in cell proliferation,
CC is able to induce cell motility and acts as a negative regulator
CC of NME1.
CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate.
CC -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC -!- ENZYME REGULATION: Activated by magnesium ions and inhibited by
CC manganese ions. Inhibited by dipyridamole, moderately sensitive to
CC IBMX and inhibited by vinpocetine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.91 uM for cAMP;
CC KM=2.3 uM for cGMP;
CC Vmax=12.8 pmol/min/ug enzyme with cAMP as substrate;
CC Vmax=0.8 pmol/min/ug enzyme with cGMP as substrate;
CC -!- SUBUNIT: Homooligomer. Able to homodimerize via its C-terminal
CC domain. Interacts with NME1. Interacts with GSK3; at focal
CC adhesion complexes where paxillin and vinculin are colocalized.
CC -!- INTERACTION:
CC P15531:NME1; NbExp=2; IntAct=EBI-2127112, EBI-741141;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell junction, focal
CC adhesion. Note=In some transfected cells a nuclear staining is
CC also observed.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q86TP1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86TP1-2; Sequence=VSP_034016;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q86TP1-3; Sequence=VSP_034014;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q86TP1-4; Sequence=VSP_034015, VSP_034017;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q86TP1-5; Sequence=VSP_034014, VSP_034017;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=Q86TP1-6; Sequence=VSP_034013, VSP_034017;
CC Note=No experimental confirmation available;
CC Name=7;
CC IsoId=Q86TP1-7; Sequence=VSP_034013;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Seems to be
CC overexpressed in aggressive sarcoma subtypes, such as
CC leiomyosarcomas and malignant fibrous histiocytomas (MFH) as well
CC as in the less malignant liposarcomas.
CC -!- SIMILARITY: Belongs to the PPase class C family. Prune subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55423.1; Type=Erroneous initiation;
CC Sequence=BAG60534.1; Type=Erroneous initiation;
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DR EMBL; AF051907; AAC95290.1; -; mRNA.
DR EMBL; AF123538; AAK00592.1; -; mRNA.
DR EMBL; AF123539; AAK00593.1; -; mRNA.
DR EMBL; AK027875; BAB55423.1; ALT_INIT; mRNA.
DR EMBL; AK294154; BAG57478.1; -; mRNA.
DR EMBL; AK298273; BAG60534.1; ALT_INIT; mRNA.
DR EMBL; AK315120; BAG37575.1; -; mRNA.
DR EMBL; AL590133; CAI13338.1; -; Genomic_DNA.
DR EMBL; AL590133; CAI13341.1; -; Genomic_DNA.
DR EMBL; AL590133; CAI13342.1; -; Genomic_DNA.
DR EMBL; AL590133; CAI13343.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53486.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53488.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53489.1; -; Genomic_DNA.
DR EMBL; BC014886; AAH14886.1; -; mRNA.
DR EMBL; BC025304; AAH25304.1; -; mRNA.
DR EMBL; BC063481; AAH63481.1; -; mRNA.
DR EMBL; U67085; AAF04914.1; -; mRNA.
DR EMBL; AL122054; CAH56396.1; -; mRNA.
DR RefSeq; NP_067045.1; NM_021222.1.
DR RefSeq; XP_005245452.1; XM_005245395.1.
DR RefSeq; XP_005245453.1; XM_005245396.1.
DR RefSeq; XP_005245454.1; XM_005245397.1.
DR UniGene; Hs.78524; -.
DR ProteinModelPortal; Q86TP1; -.
DR SMR; Q86TP1; 18-360.
DR IntAct; Q86TP1; 2.
DR ChEMBL; CHEMBL2079850; -.
DR PhosphoSite; Q86TP1; -.
DR DMDM; 229462737; -.
DR PaxDb; Q86TP1; -.
DR PRIDE; Q86TP1; -.
DR DNASU; 58497; -.
DR Ensembl; ENST00000271620; ENSP00000271620; ENSG00000143363.
DR Ensembl; ENST00000368934; ENSP00000357930; ENSG00000143363.
DR Ensembl; ENST00000368935; ENSP00000357931; ENSG00000143363.
DR Ensembl; ENST00000368936; ENSP00000357932; ENSG00000143363.
DR Ensembl; ENST00000368937; ENSP00000357933; ENSG00000143363.
DR GeneID; 58497; -.
DR KEGG; hsa:58497; -.
DR UCSC; uc001ewh.1; human.
DR CTD; 58497; -.
DR GeneCards; GC01P150980; -.
DR H-InvDB; HIX0001042; -.
DR HGNC; HGNC:13420; PRUNE.
DR HPA; HPA028411; -.
DR neXtProt; NX_Q86TP1; -.
DR PharmGKB; PA134939749; -.
DR eggNOG; COG1227; -.
DR HOVERGEN; HBG058142; -.
DR InParanoid; Q86TP1; -.
DR KO; K01514; -.
DR OMA; ISAIYMD; -.
DR PhylomeDB; Q86TP1; -.
DR GenomeRNAi; 58497; -.
DR NextBio; 64992; -.
DR PRO; PR:Q86TP1; -.
DR ArrayExpress; Q86TP1; -.
DR Bgee; Q86TP1; -.
DR CleanEx; HS_PRUNE; -.
DR Genevestigator; Q86TP1; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR InterPro; IPR004097; DHHA2.
DR InterPro; IPR001667; Pesterase_RecJ.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02833; DHHA2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell junction; Complete proteome;
KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Nucleus; Polymorphism;
KW Reference proteome.
FT CHAIN 1 453 Protein prune homolog.
FT /FTId=PRO_0000337987.
FT REGION 393 420 Essential for homodimerization.
FT MOTIF 106 108 DHH motif.
FT METAL 28 28 Manganese 1 (By similarity).
FT METAL 30 30 Manganese 2 (By similarity).
FT METAL 106 106 Manganese 1 (By similarity).
FT METAL 106 106 Manganese 2 (By similarity).
FT METAL 179 179 Manganese 2 (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 1 232 Missing (in isoform 6 and isoform 7).
FT /FTId=VSP_034013.
FT VAR_SEQ 1 182 Missing (in isoform 3 and isoform 5).
FT /FTId=VSP_034014.
FT VAR_SEQ 15 174 Missing (in isoform 4).
FT /FTId=VSP_034015.
FT VAR_SEQ 45 112 TTEAEEVFVPVLNIKRSELPLRGDIVFFLQKVHIPESILIF
FT RDEIDLHALYQAGQLTLILVDHHILSK -> A (in
FT isoform 2).
FT /FTId=VSP_034016.
FT VAR_SEQ 259 311 Missing (in isoform 4, isoform 5 and
FT isoform 6).
FT /FTId=VSP_034017.
FT VARIANT 397 397 G -> R (in dbSNP:rs3738477).
FT /FTId=VAR_059559.
FT VARIANT 397 397 G -> S (in dbSNP:rs3738477).
FT /FTId=VAR_043728.
FT MUTAGEN 28 28 D->A: Partial loss of cAMP PDE activity.
FT Partial loss of cAMP PDE activity; when
FT associated with D-106. Partial loss of
FT cAMP PDE activity; when associated with
FT D-106 and D-179.
FT MUTAGEN 106 106 D->A: No change in cAMP PDE activity.
FT Partial loss of cAMP PDE activity; when
FT associated with D-28. Partial loss of
FT cAMP PDE activity; when associated with
FT D-28 and D-179.
FT MUTAGEN 126 129 DHRP->AAAA: Partial loss of cAMP PDE
FT activity.
FT MUTAGEN 179 179 D->A: Partial loss of cAMP PDE activity.
FT Partial loss of cAMP PDE activity; when
FT associated with D-28 and D-106.
FT CONFLICT 14 14 E -> A (in Ref. 2; AAK00592).
FT CONFLICT 19 22 HVVL -> AWHE (in Ref. 7; AAF04914).
FT CONFLICT 221 221 A -> V (in Ref. 1; AAC95290 and 7;
FT AAF04914).
SQ SEQUENCE 453 AA; 50200 MW; 34BE1909AB89DBD5 CRC64;
MEDYLQGCRA ALQESRPLHV VLGNEACDLD STVSALALAF YLAKTTEAEE VFVPVLNIKR
SELPLRGDIV FFLQKVHIPE SILIFRDEID LHALYQAGQL TLILVDHHIL SKSDTALEEA
VAEVLDHRPI EPKHCPPCHV SVELVGSCAT LVTERILQGA PEILDRQTAA LLHGTIILDC
VNMDLKIGKA TPKDSKYVEK LEALFPDLPK RNDIFDSLQK AKFDVSGLTT EQMLRKDQKT
IYRQGVKVAI SAIYMDLEAF LQRSNLLADL HAFCQAHSYD VLVAMTIFFN THNEPVRQLA
IFCPHVALQT TICEVLERSH SPPLKLTPAS STHPNLHAYL QGNTQVSRKK LLPLLQEALS
AYFDSMKIPS GQPETADVSR EQVDKELDRA SNSLISGLSQ DEEDPPLPPT PMNSLVDECP
LDQGLPKLSA EAVFEKCSQI SLSQSTTASL SKK
//
ID PRUNE_HUMAN Reviewed; 453 AA.
AC Q86TP1; B2RCH8; B4DFL7; Q5SZF9; Q659E5; Q6P4E0; Q8N654; Q96JU5;
read moreAC Q9C071; Q9C072; Q9UIV0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 22-JAN-2014, entry version 81.
DE RecName: Full=Protein prune homolog;
DE Short=hPrune;
DE EC=3.6.1.1;
DE AltName: Full=Drosophila-related expressed sequence 17;
DE Short=DRES-17;
DE Short=DRES17;
DE AltName: Full=HTcD37;
GN Name=PRUNE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP INTERACTION WITH NME1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10602478; DOI=10.1038/sj.onc.1203140;
RA Reymond A., Volorio S., Merla G., Al-Maghtheh M., Zuffardi O.,
RA Bulfone A., 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 [MRNA] (ISOFORMS 2 AND 4).
RA Zollo M., Volorio S.;
RT "Human Prune homolog.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 7), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 211-453 (ISOFORMS 1/3).
RC TISSUE=Brain cortex, Kidney, and Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 6).
RC TISSUE=Blood, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-453 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10524757;
RA Volorio S., Simon G., Repetto M., Cucciardi M., Banfi S., Borsani G.,
RA Ballabio A., Zollo M.;
RT "Sequencing analysis of forty-eight human image cDNA clones similar to
RT Drosophila mutant protein.";
RL DNA Seq. 9:307-315(1998).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-453 (ISOFORMS
RP 1/2/3/4/5/6/7).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=11687967; DOI=10.1038/sj.onc.1204874;
RA Forus A., D'Angelo A., Henriksen J., Merla G., Maelandsmo G.M.,
RA Floerenes V.A., Olivieri S., Bjerkehagen B., Meza-Zepeda L.A.,
RA del Vecchio Blanco F., Mueller C., Sanvito F., Kononen J.,
RA Nesland J.M., Fodstad O., Reymond A., Kallioniemi O.-P., Arrigoni G.,
RA Ballabio A., Myklebost O., Zollo M.;
RT "Amplification and overexpression of PRUNE in human sarcomas and
RT breast carcinomas-a possible mechanism for altering the nm23-H1
RT activity.";
RL Oncogene 20:6881-6890(2001).
RN [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH NME1, ENZYME
RP REGULATION, AND MUTAGENESIS OF ASP-28; ASP-106; 126-ASP--PRO-129 AND
RP ASP-179.
RX PubMed=14998490; DOI=10.1016/S1535-6108(04)00021-2;
RA D'Angelo A., Garzia L., Andre A., Carotenuto P., Aglio V.,
RA Guardiola O., Arrigoni G., Cossu A., Palmieri G., Aravind L.,
RA Zollo M.;
RT "Prune cAMP phosphodiesterase binds nm23-H1 and promotes cancer
RT metastasis.";
RL Cancer Cell 5:137-149(2004).
RN [11]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15671547;
RA Zollo M., Andre A., Cossu A., Sini M.C., D'Angelo A., Marino N.,
RA Budroni M., Tanda F., Arrigoni G., Palmieri G.;
RT "Overexpression of h-prune in breast cancer is correlated with
RT advanced disease status.";
RL Clin. Cancer Res. 11:199-205(2005).
RN [12]
RP INTERACTION WITH GSK3B, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16428445; DOI=10.1128/MCB.26.3.898-911.2006;
RA Kobayashi T., Hino S., Oue N., Asahara T., Zollo M., Yasui W.,
RA Kikuchi A.;
RT "Glycogen synthase kinase 3 and h-prune regulate cell migration by
RT modulating focal adhesions.";
RL Mol. Cell. Biol. 26:898-911(2006).
RN [13]
RP INTERACTION WITH NME1, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=17655525; DOI=10.1042/BJ20070408;
RA Middelhaufe S., Garzia L., Ohndorf U.M., Kachholz B., Zollo M.,
RA Steegborn C.;
RT "Domain mapping on the human metastasis regulator protein h-Prune
RT reveals a C-terminal dimerization domain.";
RL Biochem. J. 407:199-205(2007).
RN [14]
RP INTERACTION WITH NME1, AND FUNCTION.
RX PubMed=17906697; DOI=10.1038/sj.onc.1210822;
RA Garzia L., D'Angelo A., Amoresano A., Knauer S.K., Cirulli C.,
RA Campanella C., Stauber R.H., Steegborn C., Iolascon A., Zollo M.;
RT "Phosphorylation of nm23-H1 by CKI induces its complex formation with
RT h-prune and promotes cell motility.";
RL Oncogene 27:1853-1864(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Phosphodiesterase (PDE) that has higher activity toward
CC cAMP than cGMP, as substrate. Plays a role in cell proliferation,
CC is able to induce cell motility and acts as a negative regulator
CC of NME1.
CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate.
CC -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC -!- ENZYME REGULATION: Activated by magnesium ions and inhibited by
CC manganese ions. Inhibited by dipyridamole, moderately sensitive to
CC IBMX and inhibited by vinpocetine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.91 uM for cAMP;
CC KM=2.3 uM for cGMP;
CC Vmax=12.8 pmol/min/ug enzyme with cAMP as substrate;
CC Vmax=0.8 pmol/min/ug enzyme with cGMP as substrate;
CC -!- SUBUNIT: Homooligomer. Able to homodimerize via its C-terminal
CC domain. Interacts with NME1. Interacts with GSK3; at focal
CC adhesion complexes where paxillin and vinculin are colocalized.
CC -!- INTERACTION:
CC P15531:NME1; NbExp=2; IntAct=EBI-2127112, EBI-741141;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell junction, focal
CC adhesion. Note=In some transfected cells a nuclear staining is
CC also observed.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q86TP1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86TP1-2; Sequence=VSP_034016;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q86TP1-3; Sequence=VSP_034014;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q86TP1-4; Sequence=VSP_034015, VSP_034017;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q86TP1-5; Sequence=VSP_034014, VSP_034017;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=Q86TP1-6; Sequence=VSP_034013, VSP_034017;
CC Note=No experimental confirmation available;
CC Name=7;
CC IsoId=Q86TP1-7; Sequence=VSP_034013;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Seems to be
CC overexpressed in aggressive sarcoma subtypes, such as
CC leiomyosarcomas and malignant fibrous histiocytomas (MFH) as well
CC as in the less malignant liposarcomas.
CC -!- SIMILARITY: Belongs to the PPase class C family. Prune subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55423.1; Type=Erroneous initiation;
CC Sequence=BAG60534.1; Type=Erroneous initiation;
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DR EMBL; AF051907; AAC95290.1; -; mRNA.
DR EMBL; AF123538; AAK00592.1; -; mRNA.
DR EMBL; AF123539; AAK00593.1; -; mRNA.
DR EMBL; AK027875; BAB55423.1; ALT_INIT; mRNA.
DR EMBL; AK294154; BAG57478.1; -; mRNA.
DR EMBL; AK298273; BAG60534.1; ALT_INIT; mRNA.
DR EMBL; AK315120; BAG37575.1; -; mRNA.
DR EMBL; AL590133; CAI13338.1; -; Genomic_DNA.
DR EMBL; AL590133; CAI13341.1; -; Genomic_DNA.
DR EMBL; AL590133; CAI13342.1; -; Genomic_DNA.
DR EMBL; AL590133; CAI13343.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53486.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53488.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53489.1; -; Genomic_DNA.
DR EMBL; BC014886; AAH14886.1; -; mRNA.
DR EMBL; BC025304; AAH25304.1; -; mRNA.
DR EMBL; BC063481; AAH63481.1; -; mRNA.
DR EMBL; U67085; AAF04914.1; -; mRNA.
DR EMBL; AL122054; CAH56396.1; -; mRNA.
DR RefSeq; NP_067045.1; NM_021222.1.
DR RefSeq; XP_005245452.1; XM_005245395.1.
DR RefSeq; XP_005245453.1; XM_005245396.1.
DR RefSeq; XP_005245454.1; XM_005245397.1.
DR UniGene; Hs.78524; -.
DR ProteinModelPortal; Q86TP1; -.
DR SMR; Q86TP1; 18-360.
DR IntAct; Q86TP1; 2.
DR ChEMBL; CHEMBL2079850; -.
DR PhosphoSite; Q86TP1; -.
DR DMDM; 229462737; -.
DR PaxDb; Q86TP1; -.
DR PRIDE; Q86TP1; -.
DR DNASU; 58497; -.
DR Ensembl; ENST00000271620; ENSP00000271620; ENSG00000143363.
DR Ensembl; ENST00000368934; ENSP00000357930; ENSG00000143363.
DR Ensembl; ENST00000368935; ENSP00000357931; ENSG00000143363.
DR Ensembl; ENST00000368936; ENSP00000357932; ENSG00000143363.
DR Ensembl; ENST00000368937; ENSP00000357933; ENSG00000143363.
DR GeneID; 58497; -.
DR KEGG; hsa:58497; -.
DR UCSC; uc001ewh.1; human.
DR CTD; 58497; -.
DR GeneCards; GC01P150980; -.
DR H-InvDB; HIX0001042; -.
DR HGNC; HGNC:13420; PRUNE.
DR HPA; HPA028411; -.
DR neXtProt; NX_Q86TP1; -.
DR PharmGKB; PA134939749; -.
DR eggNOG; COG1227; -.
DR HOVERGEN; HBG058142; -.
DR InParanoid; Q86TP1; -.
DR KO; K01514; -.
DR OMA; ISAIYMD; -.
DR PhylomeDB; Q86TP1; -.
DR GenomeRNAi; 58497; -.
DR NextBio; 64992; -.
DR PRO; PR:Q86TP1; -.
DR ArrayExpress; Q86TP1; -.
DR Bgee; Q86TP1; -.
DR CleanEx; HS_PRUNE; -.
DR Genevestigator; Q86TP1; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR InterPro; IPR004097; DHHA2.
DR InterPro; IPR001667; Pesterase_RecJ.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02833; DHHA2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell junction; Complete proteome;
KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Nucleus; Polymorphism;
KW Reference proteome.
FT CHAIN 1 453 Protein prune homolog.
FT /FTId=PRO_0000337987.
FT REGION 393 420 Essential for homodimerization.
FT MOTIF 106 108 DHH motif.
FT METAL 28 28 Manganese 1 (By similarity).
FT METAL 30 30 Manganese 2 (By similarity).
FT METAL 106 106 Manganese 1 (By similarity).
FT METAL 106 106 Manganese 2 (By similarity).
FT METAL 179 179 Manganese 2 (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 1 232 Missing (in isoform 6 and isoform 7).
FT /FTId=VSP_034013.
FT VAR_SEQ 1 182 Missing (in isoform 3 and isoform 5).
FT /FTId=VSP_034014.
FT VAR_SEQ 15 174 Missing (in isoform 4).
FT /FTId=VSP_034015.
FT VAR_SEQ 45 112 TTEAEEVFVPVLNIKRSELPLRGDIVFFLQKVHIPESILIF
FT RDEIDLHALYQAGQLTLILVDHHILSK -> A (in
FT isoform 2).
FT /FTId=VSP_034016.
FT VAR_SEQ 259 311 Missing (in isoform 4, isoform 5 and
FT isoform 6).
FT /FTId=VSP_034017.
FT VARIANT 397 397 G -> R (in dbSNP:rs3738477).
FT /FTId=VAR_059559.
FT VARIANT 397 397 G -> S (in dbSNP:rs3738477).
FT /FTId=VAR_043728.
FT MUTAGEN 28 28 D->A: Partial loss of cAMP PDE activity.
FT Partial loss of cAMP PDE activity; when
FT associated with D-106. Partial loss of
FT cAMP PDE activity; when associated with
FT D-106 and D-179.
FT MUTAGEN 106 106 D->A: No change in cAMP PDE activity.
FT Partial loss of cAMP PDE activity; when
FT associated with D-28. Partial loss of
FT cAMP PDE activity; when associated with
FT D-28 and D-179.
FT MUTAGEN 126 129 DHRP->AAAA: Partial loss of cAMP PDE
FT activity.
FT MUTAGEN 179 179 D->A: Partial loss of cAMP PDE activity.
FT Partial loss of cAMP PDE activity; when
FT associated with D-28 and D-106.
FT CONFLICT 14 14 E -> A (in Ref. 2; AAK00592).
FT CONFLICT 19 22 HVVL -> AWHE (in Ref. 7; AAF04914).
FT CONFLICT 221 221 A -> V (in Ref. 1; AAC95290 and 7;
FT AAF04914).
SQ SEQUENCE 453 AA; 50200 MW; 34BE1909AB89DBD5 CRC64;
MEDYLQGCRA ALQESRPLHV VLGNEACDLD STVSALALAF YLAKTTEAEE VFVPVLNIKR
SELPLRGDIV FFLQKVHIPE SILIFRDEID LHALYQAGQL TLILVDHHIL SKSDTALEEA
VAEVLDHRPI EPKHCPPCHV SVELVGSCAT LVTERILQGA PEILDRQTAA LLHGTIILDC
VNMDLKIGKA TPKDSKYVEK LEALFPDLPK RNDIFDSLQK AKFDVSGLTT EQMLRKDQKT
IYRQGVKVAI SAIYMDLEAF LQRSNLLADL HAFCQAHSYD VLVAMTIFFN THNEPVRQLA
IFCPHVALQT TICEVLERSH SPPLKLTPAS STHPNLHAYL QGNTQVSRKK LLPLLQEALS
AYFDSMKIPS GQPETADVSR EQVDKELDRA SNSLISGLSQ DEEDPPLPPT PMNSLVDECP
LDQGLPKLSA EAVFEKCSQI SLSQSTTASL SKK
//