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Database: UniProt
Entry: A0A2I2V0B7_FELCA
LinkDB: A0A2I2V0B7_FELCA
Original site: A0A2I2V0B7_FELCA 
ID   A0A2I2V0B7_FELCA        Unreviewed;      1439 AA.
AC   A0A2I2V0B7;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 2.
DT   24-JAN-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|Ensembl:ENSFCAP00000038098.2,
GN   ECO:0000313|VGNC:VGNC:65887};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000038098.2, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000038098.2, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000038098.2,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000038098.2, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000038098.2,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000038098.2}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000038098.2};
RG   Ensembl;
RL   Submitted (SEP-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; AANG04000169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSFCAT00000041813.3; ENSFCAP00000038098.2; ENSFCAG00000010854.6.
DR   VGNC; VGNC:65887; SYNJ2.
DR   GeneTree; ENSGT00940000160715; -.
DR   Proteomes; UP000011712; Chromosome B2.
DR   Bgee; ENSFCAG00000010854; Expressed in prefrontal cortex and 9 other cell types or tissues.
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; 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:UP000011712};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT   DOMAIN          120..444
FT                   /note="SAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50275"
FT   DOMAIN          889..968
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          1156..1288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1304..1346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1167..1181
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1198..1213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1220..1234
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1256..1279
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1439 AA;  158809 MW;  0228C8984BB00863 CRC64;
     MALSKGLRLL GRLDPAGESS VLLEARGRGD CLLFEAGTVA TLAPEEKEVI KGQYGKITDA
     YGCLGELRLK SGGASLSFLV LVTGCTSVGR IPEAEIYKIT ATDFYPLQEE AKEEDRLTAL
     RKILNSGFFY FSWPNDGSSF DLTVRAQKQD HDSYEWGSSF FWNQLLHVPL RQHQVSCCDW
     LLKVICGVVS IRTVYASHKQ AKACLISRIS CERAGARFHT RGVNDDGHVS NFVETEQTIY
     MDDGVSSFVQ IRGSVPLFWE QPGLQVGSHH LRLNRGLEAN APAFDRHMVL LKEQYGKQVV
     VNLLGSRGGE EVLNRAFKKL LWASCHAGDT PMINFDFHQL AKGGKLEKLE NLLRPQLKLH
     WDDFGVFTKG ENVSPRFQKG TLRMNCLDCL DRTNTVQSFI ALEVLHLQLE SLGLNSKPIA
     DRFVESFKAM WSLNGHSLSK MFTGSRALEG KAKVGKLKDG ARSVSRTIQS NFFDGVKQEA
     IKLLLVGDVY TEESADRGRV LLDNTALLVT PRILRAMAER QSEFTHFRRI RIAMGTWNVN
     GGKQFRSNLL GTAELADWLL DSPKLSGLAG SPDDDSPADI FAVGFEEMVE LSAGNIVNAS
     TTNRKMWGEQ LQKAISRSHR YILLTSAQLV GVCLYIFVRP YHVPFIRDVA IDTVKTGMGG
     KAGNKGAVGI RFQFHSTSLC FVCSHLTAGQ AQVKERNDDY REITQKLSFP MGRNIFSHDY
     VFWCGDFNYR IDLTYEEVFY FVKRQDWKKL LEFDQLQLQK SSGKIFKDFH EGTINFGPTY
     KYDVGSAAYD TSDKCRTPAW TDRVLWWRKR HPFDRTAGDL NLLDNDIDAD STVRHSWSPG
     ALKYYGRAEL QASDHRPVLA IVEVEVQEVD VGARERVFQE VSSFQGPLDA TVIVNLQSPT
     VEEKNEFPED VRTELMQTLG NYGTIVLVRV NQGQMLVTFA DSHSALSVLD VDGMKVKGRA
     VKIRPKTKDW LKGWQEEIIR KRDSMASMSP TANSCLLEEN FDFTSLDYES EGDILEDDED
     YLVDELSQPV VSDGETAGDY LSEAPSCTAA VPADTSPALT KKTRHPTYKA GLMVKKSASD
     VSISSGTHGQ YSILQTAKLL PGAPQHAPKA RTGISKPYNV KQIKTTNAQE AEAAIRCLLE
     ARGGIPGEAV NATALRNQGT SKPEPPVAVA PLLPRRPAPR VPAIKKPTLR RTGKPESPEE
     QCGQQSVHFT IGPPETSLET PPLAAVPPVP KPRTLQPRKG TDRKASGGKP VPNDAPPAAG
     ATPPPPLEVL PPAPQAPPRR KKSAPAAFHL QVLQSNSQLL QSLTCSSSDC PPAPRPDQGV
     LFPQPAHPGP LSAAGAQADG TKETQPEAAS LLGDYQDPFW NLLHDTHLLK NAWLSKNSDP
     LDPGTGSLER AHTASLQISA SVADNLPPEH GPNDLGHWMT ISDKDKRTVL QVFDPLAET
//
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