ID A0A1U8D0I3_ALLSI Unreviewed; 1414 AA.
AC A0A1U8D0I3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN Name=SYNJ2 {ECO:0000313|RefSeq:XP_014374828.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014374828.1};
RN [1] {ECO:0000313|RefSeq:XP_014374828.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_014374828.1; XM_014519342.2.
DR GeneID; 102369635; -.
DR CTD; 8871; -.
DR OrthoDB; 21647at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR CDD; cd09099; INPP5c_Synj2; 1.
DR CDD; cd12720; RRM_SYNJ2; 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; IPR034973; SYNJ2_RRM.
DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR PANTHER; PTHR11200:SF148; SYNAPTOJANIN-2; 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:UP000189705};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 63..387
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT DOMAIN 833..912
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1090..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1414 AA; 157644 MW; F541F481E8544568 CRC64;
MDAYGCLGEL QLKCGSARLR FLVLVTGCTS VGKILDAEVY KITGTDFCPL QEETKEEDRV
TALKKILNSG MFYFSLPNSD SDFDLTVRAQ KQGDNSYESG NSFFWNQLLH VPFKHYQVNC
SDWLLKVICG VVDIRTVYAS HKKAKACLIS RISCERAGAR FHIRGVNDDG HVSNFVETEQ
TIYLDNDISS FVQIRGSVPL FWEQPGLQVG SHHLRLNRGL EANAPAFDRH MMLLKEQYGK
QVIVNLLGSR GGEEVLNRAF KKLLWASSHA ADTPMINFDY HQFAKGGKIE KLENLLGPQL
KLHWDEFGIF TKSKNVSPRL QTGTFRSNCL DCLDRTNSVQ SFIALEVLHM QLESLGLNSK
PIVERFVESY KAMWTVNGHN LSRVFTGSRA LEGKHKVGKL KDGARSVSRT IQSNFFDGVK
QEAIKLLLMG DFFSEEYADK GKMLMDNTAL LVTPSILKAM SERQFEFTNF KRIRVAMGTW
NVNGGKQFRS NILGTSELTD WLLDSPKLSG VSEFQDDESC PPDIFAVGFE EMVELSAGNI
VNASTTNKKM WGEQLQKAIS RTHRYIQLTS AQLVGVCLFI FVRPYHVPFI RDVAIDTVKT
GMGGKAGNKG AVGIRFQFYS TSFCFICSHL TAGQSQVKER NEDYKEITQK LSFPMGRNVF
SHDYVFWCGD FNYRIDLTYE EVFYFLKRQD WKTLLEFDQL QQQKSSGKIF KDFHEGTINF
GPTYKYDVGS EAYDTSDKCR TPAWTDRVLW WRKKLPFDKT AGEINLLDSD LSVETKIKHT
WTPGALMYYG RAELQASDHR PVLAIVEVEV QEVNVAARES VFQEVSSFQG PLDATVVVNL
QTPTPEEKNE FPEDLRTELM QIFENYGIIV LVRINGGQML ITFADSKSAL NVLDIDGIKV
KGRAVKIRPK TKDWLKGLQE EITRKRDSFV PMSPTANSCL LEENFDFSSL DYESEGDILD
EEEEYLDDVL PQHLVTEISE DFPEGPEHFA SVVLSNKSLM LTGRNSHLCK AGTSVKKSPS
DTPTSSGGHS LCSILATAKL LPGAPQQPPK VRTGISKPYN VKQIKTTTAQ EAEEAIRCLM
EAKGGVQEEA LKPVPLRTQT VTKPEPLPSI AKSASFQGSQ PGPALVPHRP PPKVPTAKKP
VPLQRTGVKS ENTMSPEEQS DQQTNHPPFG LPDPCLEASA ITSPTRVTPV PKPRTTQPGK
ILQRRKSSER PPPSPDSLEA DMLHSPNSSF APKIPPRRKK SAPAALHLHV LQSSNSPLLR
GLSLNFNNNN SPSAIQDSDI LSPRQSDFSA LMVMASPQND GTKCVTPTPS DLIADLQGPP
ATSSQQPPLL DTSSLTEDTN LLDLDTDFPC PHPTPSVPST PPVHTPKDLK LPGSDFSHWV
TFSDDEDKGT LTETLNTLLV LEQNGNTLKN RNTN
//
