ID A0A1V4J356_PATFA Unreviewed; 2849 AA.
AC A0A1V4J356;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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|EMBL:OPJ66474.1};
GN ORFNames=AV530_016530 {ECO:0000313|EMBL:OPJ66474.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ66474.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ66474.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ66474.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ66474.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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 GCF family. {ECO:0000256|ARBA:ARBA00010801}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ66474.1}.
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DR EMBL; LSYS01009367; OPJ66474.1; -; Genomic_DNA.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR GO; GO:0003352; P:regulation of cilium movement; IEA:InterPro.
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; IPR021298; CFAP298.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR012890; GCFC2-like.
DR InterPro; IPR022783; GCFC_dom.
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; PTHR12214; GC-RICH SEQUENCE DNA-BINDING FACTOR; 1.
DR PANTHER; PTHR12214:SF2; PAX3- AND PAX7-BINDING PROTEIN 1; 1.
DR Pfam; PF11069; CFAP298; 1.
DR Pfam; PF08952; DUF1866; 1.
DR Pfam; PF07842; GCFC; 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:UP000190648};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 1086..1409
FT /note="SAC"
FT /evidence="ECO:0000259|PROSITE:PS50275"
FT DOMAIN 1856..1933
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1992..2261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2502..2557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1992..2022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2036..2059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2060..2091
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2111..2134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2193..2214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2244..2261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2849 AA; 319305 MW; BEF27BEA78697BFE CRC64;
MFRKARRVNV RKRNDSEEED EERDEEPPQE PGPAAGTGGE GPGEASMALA AGSGLLPLPP
GCVPLALPGS PAAFACAAGY GAALGLGLGL MGADRAGLGA LPAPALLSSP PPPQQQGNGL
PGAGRPKEKK RPRENKEVPR ASLLSFQDEE EETEEVFKVK KSSYSKKIVK QLKKEYKEDL
EKSKVRTEVN SPTDVEPPLD KTGQIKDIGQ EDGTANSEHG EEEMEVESEK EEEKTKAGGA
FSSALSSLNV LRPGEIPDAA FIHAARKKRQ MARELGDFTP VDSEPGKSRL VREDENDASD
DEDDDEKRRI VFTVKEKSQR QKIAEEIGIE GSDDEALGAG EQDEELSRWE QEQIRKGINI
PQVQPSQPAE VNNMYYQTTY QTLSYGSSYG VPYTYTAYGS SETKSQKTDN TVPFKTPSNE
MTPVTIDLVK KQLKDRLDSM KELHKANRQQ YEKHQQSRED SIKAIERLEG SSGGIGEQYK
FLQEMRGYVQ DLLECFSEKV PLINELESAM HQLYKQRASR LVQRRQDDIK DESSEFSSHS
NKALMAPNLE SFGRDRVIYQ EQVKRRTAER EARRTRRRQA REQTGKMADH LEGLSSDDEE
TSTDITNFNM ERDRILKESS KVFEDVLESF YSIDCIKSQF EAWRSKYFAS YKDAYIGLCL
PKLFNPLIRL QLLIWTPLEG KCRDFETMLW FESLLFYGCE EQEQVKDDAD ISLLPTIVER
VVLPKLTVIS ENIWDPFSTT QTSRMVEMVQ KLVDGYPSVV NAENKNTQML LKALLLRMRR
TLDDDVFMPL YPKNVLENKN SGPYLFFQRQ FWSSVKLLGN FLQWYGILSN KTLQELSIDG
LLNRYILMAF QNSEYGEDSI KKAQSVIACF PKQWFINLKG DKTISQLENF CRYLVHLADT
IYRNSIGCSD VEKRNAREHI KQIIKLLASI RALDHAVTVA NDHNCTPLNS YIANGRWRGR
TATDKGKMAF SKGYRVYHKL DPLPFSVIVE TRNREECLMF ESGAVAVLSA AEKDTIKNTY
SKVMDAYGLL GVLRLNLGDT LLHYLVLVTG CMSVGKIQDS EVFRVTSTEF VSLRIEPTDE
DRISEVRKVL NSGNFYFAWS ATGVSLDLSL NAHRSMQEHT TDNRFFWNQS LHLHLKHYGV
NCDDWLLRLM CGGVEIRTIY AAHKQAKACL ISRLSCERAG TRFNVRGTND DGHVANFVET
EQVIYLDDSV SSFIQIRGSV PLFWEQPGLQ VGSHRVRMSR GFEANAPAFD RHFQTLKNLY
GKQIIVNLLG AKEGEHMLSK AFQSHLKASE HSADIKMVNF DYHQMVKGGK AEKLHSVLKP
QVQKFLECGF FYFDGKEVKR SQSGTVRTNC LDCLDRTNSV QAFFGLEMLT KQLEVLGLAE
KPQLVTRFQE VFRSMWSVNG DSVSKIYAGT GALEGKAKAG KLKDGARSVT RTIQNNFFDS
SKQEAIDVLL LGNTLNSDLA DKARALLTTS SLRASVKVLK SMCENFYKYA KPKKIRVCVG
TWNVNGGKQF RSIAFRNQTL TDWLLDAPKL AGVHEFQDRK SKPVDIFAIG FEEMVELNAG
NIVNASTTNQ KLWAAELQKT ISRDYKYVLL ASEQLVGVCL FVFIRPQHAP FIRDVAVDTV
KTGMGGATGN KGAVAIRMLF HTSSLCFVCS HFAAGQSQVK ERNEDFVEIA RKLSFPMGRM
LFSHDYIFWC GDFNYRIDIP NEEVKDLIRQ QNWDPLIAGD QLINQKNSGQ IFRGFLEGKI
NFAPTYKYDL FSDDYDTSEK CRTPAWTDRI LWRRRKWPFD RSAEDLDLLN ASFHDDTNVP
YTWNPGTLLH YGRAELKTSD HRPVVALIDI DIFEIEAEER QKVYKEVIAM QGPPDGTIMV
SIRSSSAEEN YFDDYLIDEL LQKFASYGEV ILIRFVEDKM WVTFLEGSSA LNVMNLNGTE
LLGRIINISL KNPDWIRTLE EEMNLEKINI GLPSSTSSTL LCEDAEVTAD YDMEGDIDDY
SAEVEEILPQ HLQPTSGSGL GTSPSSSPRS SPCQSPTLSD GPTLPVRPSR APTKTPGPPV
STHTEPQHST QQKESSQSLE PKRPPPPRPV APPARPAPPQ RPPPPSGLGA PPSPGVARRE
VEAPKSPGTQ RKDNLVRNQP PPSTGISGAG TAGYGTTRPT VPPRAGVISA PQSHVRPSGG
RPAPETQTKP AEPPRVKTAA NILTGSPVLP EPLKPQAAGP TQPTTQPPPV LKMQEPLIPV
ASHPSQTSAP QSLEPPQPPP RSRSSHSLPS ESAPLQQQTK TNGTYCTKLE TQLNSDPFED
LSFQLLVSKM QTSVRTSHLP TLNQKELIQL PSATQRNADA LNTINCMPAM PPIPAFNTSQ
EHKRSSPNPF ITGLNCTNPF TERTPSAGNP FRTETQESEI TSRLLEGRAA CNPFPSLTPP
SCNTSKPVFS VDAPENTFCL RSKSLMVKNV QRKAWVTFDD DEENFNAKLK PSKSVTDFKQ
ISSRKSAGCP DLLCTEQNTF LGSDFNFDND WNKSSTDCFY TMPARRPPAP PVPSRTTSNR
SPADPFTSLA PKRQREGRKR KGGGPAPGGV KVARRSDSDM VRLHVKRADE SQFLLEAAGS
TRLAELAPLV ARIYNGRLKV QRLCSEMEDL AEHGVYLPYN MQGLTDEQIE ELKLKDEWAD
KCVPSGGSVF KKDEIGRRNG HAPNEKMQQV IKKTIEEAKA LISKKQVQAN VCVTMEMVKD
ALDQLRGAVM IVYPMGLPPH DPVRMELEDK EDLSGTHAGL EVIKESEAQL WWAGKELKET
KLLSDYVGKN EKTTIIVKIQ KKGQGAPGRE PLISHEEQKQ MMMYYYKKQE ELKKLEEDDD
DSFLNAEWAD NHALKRQFHG VKDIKWGPR
//
