CNRN_DICDI
ID CNRN_DICDI Reviewed; 639 AA.
AC Q54JL7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase cnrN;
DE EC=3.1.3.67;
GN Name=cnrN; ORFNames=DDB_G0287969;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=18676953; DOI=10.1128/ec.00210-08;
RA Tang Y., Gomer R.H.;
RT "A protein with similarity to PTEN regulates aggregation territory size by
RT decreasing cyclic AMP pulse size during Dictyostelium discoideum
RT development.";
RL Eukaryot. Cell 7:1758-1770(2008).
CC -!- FUNCTION: Protein phosphatase that negatively regulates PI3K-dependent
CC pathways. Regulates cAMP signal transduction to control territory size.
CC During development, a lawn of Dictyostelium cells breaks up into
CC territories where cells aggregate in dendritic streams to form groups
CC of 20'000 cells. {ECO:0000269|PubMed:18676953}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:25017,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57836,
CC ChEBI:CHEBI:58456; EC=3.1.3.67;
CC Evidence={ECO:0000269|PubMed:18676953};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- DEVELOPMENTAL STAGE: Level is low in vegetative cells, increases after
CC starvation, peaks between 5 and 10 hours, and then decreases.
CC Aggregation territories and streams form after 5 to 8 hours of
CC starvation. This pattern of accumulation indicates that cnrN mRNA is
CC present when aggregation territories and streams are forming.
CC {ECO:0000269|PubMed:18676953}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking cnrN form abnormally small groups,
CC which can be rescued by the expression of exogenous cnrN. They also
CC overaccumulate cAMP during development and form abnormally small
CC fruiting bodies. Five seconds after cAMP stimulation, a prolonged and
CC higher peak of phosphatidylinositol (3,4,5)-trisphosphate is shown
CC compared to wild type cells. {ECO:0000269|PubMed:18676953}.
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DR EMBL; AAFI02000107; EAL63410.1; -; Genomic_DNA.
DR RefSeq; XP_636914.1; XM_631822.1.
DR AlphaFoldDB; Q54JL7; -.
DR SMR; Q54JL7; -.
DR STRING; 44689.DDB0229881; -.
DR PaxDb; Q54JL7; -.
DR PRIDE; Q54JL7; -.
DR EnsemblProtists; EAL63410; EAL63410; DDB_G0287969.
DR GeneID; 8626389; -.
DR KEGG; ddi:DDB_G0287969; -.
DR dictyBase; DDB_G0287969; cnrN.
DR eggNOG; KOG2283; Eukaryota.
DR HOGENOM; CLU_428608_0_0_1; -.
DR InParanoid; Q54JL7; -.
DR OMA; HAKEPIL; -.
DR Reactome; R-DDI-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-DDI-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-DDI-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-DDI-199418; Negative regulation of the PI3K/AKT network.
DR Reactome; R-DDI-202424; Downstream TCR signaling.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-5689896; Ovarian tumor domain proteases.
DR Reactome; R-DDI-8948747; Regulation of PTEN localization.
DR Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
DR PRO; PR:Q54JL7; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0016791; F:phosphatase activity; IDA:dictyBase.
DR GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IDA:dictyBase.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IMP:dictyBase.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:dictyBase.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IBA:GO_Central.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..639
FT /note="Phosphatidylinositol 3,4,5-trisphosphate 3-
FT phosphatase cnrN"
FT /id="PRO_0000363860"
FT DOMAIN 20..190
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 195..350
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT REGION 243..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
SQ SEQUENCE 639 AA; 71714 MW; CF7DCEF658057929 CRC64;
MNQVFFSKIR SLVSADRHRF KSKEMDLDLD LSYITDNILA MGFPGTGLEA SWRNSIDDVC
ELLKQKHHGK YMIWNLSERV YDYSKLNNQI LEFPFLDHHP PPLSLLFEIV NSLSNWLKAD
AENVAVVHCK GGKGRTGTII CCYLYYSCQF EIMDDAKNHF AEKRSKMKKG VTQPSQQRYI
NYFKEIVSGS HMVEEFVLTF RSIELGPLTK DQANSLSFEI FEHAKEPILN FASSSNSIQI
VPINNDNSES NNNNNNNNNN NNNNNNQQQQ LYKIIILIQK KVQNDVLIRV YRGDTGKGKG
KMKKQIFHLI FNIAFVNLDQ CLFGMNEFDH FKSSKKYDPN LQMECRFQNN CTGAPDHSFK
IWNIMALQYQ RTKSSLNNSI TDIKSINEIN STNNNNILAS SAPTPLTTTT TTTTTTTTTS
LPSSEHSTPQ ILISSSDANL DLKNCNINCD SSSGGGSNSS RNSNSNSRGG SSNSSSNRSS
TSSRSSITTD SIKPSCSSDS ICNNSSICNN SCNNNNNNNN NNNNNNNNNN NNNNNNNNNK
NSNNNNNESS SNSNDDSDSE ASIRKRKNTL WSSGSSIKLK PSPNLSRLSL FNGHRQSFTK
KINPNNNEEN VDQKTLPILK KETNDPSESD IKNVEIIQD
