ID A0A0Q9WR72_DROWI Unreviewed; 1228 AA.
AC A0A0Q9WR72;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN Name=Dwil\GK28263 {ECO:0000313|EMBL:KRF97859.1};
GN ORFNames=Dwil_GK28263 {ECO:0000313|EMBL:KRF97859.1};
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260 {ECO:0000313|EMBL:KRF97859.1, ECO:0000313|Proteomes:UP000007798};
RN [1] {ECO:0000313|EMBL:KRF97859.1, ECO:0000313|Proteomes:UP000007798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000256|ARBA:ARBA00001786};
CC -!- SIMILARITY: Belongs to the synaptojanin family.
CC {ECO:0000256|ARBA:ARBA00008943}.
CC -!- SIMILARITY: In the central section; belongs to the inositol 1,4,5-
CC trisphosphate 5-phosphatase family. {ECO:0000256|ARBA:ARBA00009678}.
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DR EMBL; CH963848; KRF97859.1; -; Genomic_DNA.
DR RefSeq; XP_015034502.1; XM_015179016.1.
DR AlphaFoldDB; A0A0Q9WR72; -.
DR SMR; A0A0Q9WR72; -.
DR STRING; 7260.A0A0Q9WR72; -.
DR EnsemblMetazoa; FBtr0421295; FBpp0379394; FBgn0280129.
DR GeneID; 26530265; -.
DR KEGG; dwi:26530265; -.
DR InParanoid; A0A0Q9WR72; -.
DR OrthoDB; 21647at2759; -.
DR PhylomeDB; A0A0Q9WR72; -.
DR Proteomes; UP000007798; Unassembled WGS sequence.
DR GO; GO:0044754; C:autolysosome; IEA:EnsemblMetazoa.
DR GO; GO:0061174; C:type I terminal bouton; IEA:EnsemblMetazoa.
DR GO; GO:0012506; C:vesicle membrane; IEA:EnsemblMetazoa.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0150008; P:bulk synaptic vesicle endocytosis; IEA:EnsemblMetazoa.
DR GO; GO:0150007; P:clathrin-dependent synaptic vesicle endocytosis; IEA:EnsemblMetazoa.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IEA:EnsemblMetazoa.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IEA:EnsemblMetazoa.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IEA:EnsemblMetazoa.
DR CDD; cd09089; INPP5c_Synj; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR046985; IP5.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR002013; SAC_dom.
DR InterPro; IPR015047; SYNJ1/2_RRM.
DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR PANTHER; PTHR11200:SF257; PHOSPHOINOSITIDE 5-PHOSPHATASE; 1.
DR Pfam; PF08952; DUF1866; 1.
DR Pfam; PF02383; Syja_N; 1.
DR SMART; SM01165; DUF1866; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50275; SAC; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007798}.
FT DOMAIN 120..457
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT REGION 1007..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1034
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1079
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1228
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1228 AA; 135471 MW; A7E6CB8AC7649EDC CRC64;
MAMSKVIRVL EKSIAPSPHS VLLEHRNKSD SILFESHAVA LLTQQETDVI KKLYTKVCDA
YGCLGALQLN AGESTVLFLV LVTGCVSMGK IGDVEIFRIT QTTFVSLQNA APNEDKISEV
RKLLNSGTFY FAHTNVSASA QVGGGASSKF DITLCAQRRQ RSSETDNRFF WNRMMHIHLM
RFGIDCQSWL LQAMCGSVEV RTVYIGAKQA RAAIISRLSC ERAGTRFNVR GTNDEGYVAN
FVETEQVIYV DGDVTSYVQT RGSVPLFWEQ PGVQVGSHKV KLSRGFETSA AAFDRHMSMM
RQRYGYQTIV NLLGSSLIGS KEGEAMLSNE FQRHHGMSAH KDVPHIIFDY HQECRGGNFS
ALSKLKERIV ACGANYGVFY ASNGQVLKEQ FGVVRTNCLD CLDRTNCVQT YLGLDVLNLQ
LESLKLGGKQ QNVSRFEEIF RQMWINNGNE VSKIYAGTGA IQGGSKLMDG ARSAARTIQN
NLLDNSKQEA IDVLLVGSTL SSELADRARI LLPSNMLHAP TTVLRELCKR YTEYVHPRLA
RVAVGTYNVN GGKHFRSIVF KDSLADWLLD CHAQARSKAL VDVNNPSEHA DHPVDIYAIG
FEEIVDLNAS NIMAASTDNA KLWAEELQKT ISRDNDYVLL TYQQLVGVCL YIYIRPEHAP
HIRDVAIDCV KTGLGGATGN KGACAIRFVL HGTSMCFVCA HFAAGQSQVA ERNADYAEIT
RKLAFPMGRS LKSHDWVFWC GDFNYRIDMD KDELKECVKN GDLPTVLEFD QLRKEQEAGN
VFGEFLEGEI SFDPTYKYDL FSDDYDTSEK QRAPAWTDRV LWRRRKALAE GDFGAAWNPG
KLIHYGRSEL KQSDHRPVIA IIDAEIMEID QQRRRLVFEQ VIRDLGPPDS TIVVHVQETS
SANEDEDGPT IYDENVMSAL IAELSKMGEV TLVRYVEDTM WVTFRDGESA LNAASKRSTQ
VCGLELVFEL KSVNWQHLVD NEIDLCTTNT IPLCANPMEQ AQLLSQMTPE VPQRPKQPPT
RPPARPPMPM SPKNSPRHMP HAGVISIVPK AAGPSRPPQP LMQAPLQPVQ VPPPRPPAMV
DAGNGSGSKS QSPTEMINSI SSSTSTSSSG KASPTTGAAL SGPPTPPRQM TSKTATPITT
PTRQLAADTA YETASNIYEE IQEDVPAPCH PPPAGAPPPP PPVVPLDSPR RQVPPMGPPP
PLPNRRGPPP IPNRSGNAPP LPSRPTNN
//
