ID H0WTB4_OTOGA Unreviewed; 1615 AA.
AC H0WTB4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN Name=SYNJ1 {ECO:0000313|Ensembl:ENSOGAP00000005375.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000005375.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000005375.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AAQR03132269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03132270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03132271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03132272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03132273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03132274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03132275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03132276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03132277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03132278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 30611.ENSOGAP00000005375; -.
DR Ensembl; ENSOGAT00000006013.2; ENSOGAP00000005375.2; ENSOGAG00000006010.2.
DR eggNOG; KOG0566; Eukaryota.
DR GeneTree; ENSGT00940000157964; -.
DR HOGENOM; CLU_003016_5_1_1; -.
DR InParanoid; H0WTB4; -.
DR OMA; NIMKAST; -.
DR TreeFam; TF354311; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:Ensembl.
DR GO; GO:1904980; P:positive regulation of endosome organization; IEA:Ensembl.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
DR CDD; cd09098; INPP5c_Synj1; 1.
DR CDD; cd12719; RRM_SYNJ1; 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; IPR000504; RRM_dom.
DR InterPro; IPR002013; SAC_dom.
DR InterPro; IPR015047; SYNJ1/2_RRM.
DR InterPro; IPR034971; SYNJ1_RRM.
DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR PANTHER; PTHR11200:SF158; SYNAPTOJANIN-1; 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; PS50102; RRM; 1.
DR PROSITE; PS50275; SAC; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 159..482
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT DOMAIN 942..1011
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1534..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1331
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1542..1560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1596
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1615 AA; 178361 MW; 190A0613FCE81E4B CRC64;
MRKSWSCWSG SDASGGCGGC SCERRRRRSR RKRAVSEERR MAFSKGFRIY HKLDPPPFSL
IVETRNKEEC LMFESGAVAI LSSAEKEAIK GTYSKVLDAY GLLGVLRLNL GDTMLHYLVL
VTGCMSVGKI QESEVFRVTS TEFISLRIDS SDEDRISEVR KVLNSGNFYF AWSASGISLD
LSLNAHRSMQ EQTTDNRFFW NQSLHLHLKH YGVNCDEWLL RLMCGGVEIR TIYAAHKQAK
ACLISRLSCE RAGTRFNVRG TNDDGHVANF VETEQVVYLD DSVSSFIQIR GSVPLFWEQP
GLQVGSHRVR MSRGFEANAP AFDRHFRTLK NLYGKQIIVN LLGSKEGEHM LSKAFQVIYG
CSQYNSFIFF CIIENFNNKL KRESGQYILI TSILVCFSLF LFKTSSFNLL NLRCQSGTVR
TNCLDCLDRT NSVQAFLGLE MLTKQLEALS LAEKPQLVTR FQEVFRSMWS VNGDSISKIY
AGTGALEGKA KLKDGARSVT RTIQNNFFDS SKQEAIDVLL LGNTLNSDLA DKARALLTTG
SLRGILMQLK FSSSKVLKSM CENFYKYSKP RKIRVCVGTW NVNGGKQFRS IAFKNQTLTD
WLLDAPKLAG IQEFQDKRSK PTDIFAIGFE EMVELNAGNI VNASTTNQKL WAVELQKTIS
RDNKYVLLAS EQLVGVCLFV FIRPQHAPFI RDVAVDTVKT GMGGATGNKG AVAIRMLFHT
TSLCFVCSHF AAGQSQVKER NEDFVEIARK LSFPMGRMLF SHDYVFWCGD FNYRIDLPNE
EVKELIRQQN WDSLIAGDQL INQKNAGQIF RGFLEGKVTF APTYKYDLFS DDYDTSEKCR
TPAWTDRVLW RRRKWPFDRS AEDLDLLNAS FQDESKILYT WTPGTLLHYG RAELKTSDHR
PVVALIDIDI FEVEAEERQN IYKEVIAVQG PPDGTVLVSI KSSLPENNFF DDALIDDLLQ
QFANFGEVIL IRFVEDKMWV TFLEGSSALN VLSLNGKELL NRTITITLKS PDWIKNLEEE
MSLEKISIAL PSSTSSTLLG EDAEVTADFD MEGDVDDYSA EVEEILPQHL QPSSSSGLGT
SPGSSPRTSP CQSPTVPEVP VPSLPVRPSR APSRTPGPPS AQSSPVDVQP APPLQQKDPA
QPLEPKRPPP PRPVAPPTRP APPQRPPPPS GARSPAPARK EFGGTGAPPS PGVARREMEA
PKSPGTTRKD NIGRNQPSPQ AVLAGPGPAG YSAARPTIPP RAGVISAPQS HARAAAGRLT
PESQSKPAEA AKSSAFLPEP LKPQAAFPPQ SSLPPPAQRL QEPLVPVTAP MPQSAPQPNL
ETPPQPPPRS RSSHSLPSEA SPSQLQVKTN GVSDVKGESP LKSDPFEDLS LNLLAVSKAQ
LSVQMSPVLT PDPKRLVQLP SATQSNVNTL SSTSCMLAIP PIPARSKSQE NMRSSSNPFI
TSLTSTDPSS DRTVVGNPFR TESQELEATS WFSREESVTN SPFPSLKPPG YNKSKPSSSL
DGFKDSFDLQ CQSTVKISNP KGWVTFEEED DFNVKGKSKS TCPDLLGNQP SSFSGSSVTL
DDDWNKDKNV SFCVLPSRRP PPPPVSVLPP GTSPPVDPFT TLASKASPTL DFTER
//
