ID I3JAI7_ORENI Unreviewed; 1357 AA.
AC I3JAI7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 65.
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:ENSONIP00000005877.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005877.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000005877.2}
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 STRING; 8128.ENSONIP00000071251; -.
DR Ensembl; ENSONIT00000005881.2; ENSONIP00000005877.2; ENSONIG00000004667.2.
DR eggNOG; KOG0566; Eukaryota.
DR GeneTree; ENSGT00940000157964; -.
DR HOGENOM; CLU_003016_5_1_1; -.
DR TreeFam; TF354311; -.
DR Proteomes; UP000005207; Linkage group LG10.
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:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
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:UP000005207}.
FT DOMAIN 119..470
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT REGION 1057..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1087
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1152
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1230
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1304
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1334
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1357 AA; 148279 MW; A81DC997387C6235 CRC64;
MAFSKGYRIY HKLDPPPYSV IVETRAREEC LMFESAAVAV LSAAEKDAIK NTYTKIVDAY
GILGVLRLNL GDSMLHSLVV VTGCSSVGKV QDSEVFRVTQ TDFISLKNDP GDEERIAEVR
KVLNSGHFYF AWSSTGVSMD LSLNAHRRII EDTTDNRFFW NQSLHLHLKH YGVNCDDWLL
RLMCGGVEIR TIYAGHKQAK ACIFSRLSSE RAGTRFNVRG TNDDGQVANF VETEQVIFLD
DKVSSFIQIR GSIPLFWEQP GIQKKSIKGV LLQLNENRHP NRLAENLHLV GSHRVKLSRG
FEANAPAFER HFTALRQLYG KQVIINLLGS KEGEHMLSKA FQSHLKASEH SSAVKMVNFD
YHQNVKGGKA DKLHSVLKPQ LSKFVEECGF FYYSGETGIL RTQGGTMRTN CLDCLDRTNS
VQAFFALEML PKQLEQMGLT EKPQLVARFQ EVFRTMWSAN GDSVSKIYAG TGALDGKAKL
KDGARSVTRT IQNNFFDSSK QEAIDILRLG STLNSDLADK ARALLTTSSL YVTEPVLQSA
SPRVLLGMCQ NYHKYTMPKQ IRVCIGTWNV NGGKQFRSIA FRNQTLNDWL LDAPKKAGHP
EFQDSRTNPI DIFAIGFEEM VELNAGNIVS ASTTNQKLWA AELQKNISRD HKYVLLASEQ
LVGVCLFVFI RPQHAPFIRD VAVDTVKTGM GGATGNKGGV AIRLLFHTTS ICFVCSHFAA
GQSQVKERND DYNEITRRLS FPMGRLLYSH DYVFWCGDFN YRISLPNEEV KDLIKQQNWD
ALTAGDQLLD QKNAGLVFRG FIEGKLDFAP TYKYDLFSED YDTSEKCRTP AWTDRILWKR
RKWNFDKTAE EMNIVGAASS SRDSDDDVEQ TWSPGALKYY GRAELKTSDH RPVVAVIDVD
ILEVDPEARH QVYKDVIARQ GPPDGTILVS LCSSGPDDYF DDALIDELLE KFANFGEVIL
IRFVEEKMWV TFLEGYSALA ALSLSASTVL GKMIDIRLKS PGWIKSLEEE MSVERICGSI
PTSASSTLLA EDTDMGDDDY DMEGDVDEEV EEILPQHLQP GAGTGPGSSP LPSPRSSPCP
SPTHGEPAAP SRPSRGAQPS RPSQGPPVDF QPGAPTAQGL EPKRPPPPRP NAPPARPAPP
QRPPPPSGQK SPALPRPDAA GRGQTAAGAP GPGGASRPNI PPRAGVISVP PQSRPPPPSH
PGAPRPIPEV HPGAPRPIPD THPGAPRPVP SAQTKPADLP LGPQPSGAPP AAPPAVKPQV
SSPMQPPMQP QPAAPPAQSQ LPPPMQPTLP APLQPQPAPA PKAAGPSAAP AAAAPAGPPP
SLASPKPPPR SRSSHALPPD AAKSETAPAA QLEKPSG
//
