ID U3JWF9_FICAL Unreviewed; 1103 AA.
AC U3JWF9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Inositol polyphosphate-5-phosphatase J {ECO:0000313|Ensembl:ENSFALP00000007113.2};
GN Name=INPP5J {ECO:0000313|Ensembl:ENSFALP00000007113.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000007113.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000007113.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000007113.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type II family. {ECO:0000256|ARBA:ARBA00005910}.
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DR AlphaFoldDB; U3JWF9; -.
DR STRING; 59894.ENSFALP00000007113; -.
DR Ensembl; ENSFALT00000007144.2; ENSFALP00000007113.2; ENSFALG00000006809.2.
DR eggNOG; KOG0565; Eukaryota.
DR GeneTree; ENSGT00940000156855; -.
DR HOGENOM; CLU_011711_3_2_1; -.
DR Proteomes; UP000016665; Chromosome 15.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR CDD; cd09094; INPP5c_INPP5J-like; 1.
DR Gene3D; 2.60.40.2840; -; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR046985; IP5.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR041611; SKICH.
DR InterPro; IPR022189; SMTN.
DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR PANTHER; PTHR11200:SF127; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 5-PHOSPHATASE A; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF17751; SKICH; 1.
DR Pfam; PF12510; Smoothelin; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR PROSITE; PS50021; CH; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1103
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032505022"
FT DOMAIN 427..532
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 135..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 122965 MW; 43D751B2D6346510 CRC64;
MLTLCYFCVI PSLACFFPSI SADSGGNGDP GSLEYSPVGA GVLLPLPRWP HGAEQRPAPR
PAGSRLDAMK TFFTIEIKDG RVQPLAPRIT AAPGSQRAEV TLGLRSTPIR ITTIPSSVSS
ICNISSVSSN VTKDPCAHFE GTEEPGGPVA HPPTFSSTRQ QSALHLSRSN SSMEPEVVEQ
HQAPRREPEL PNGMEKVQVR EVEKRSKLNV EELSKIEDED VLDKMLDRTT DFEERRLIRN
AMRELRQRKR DQREKERDQR LQEARSQSVA GRAGHATETT TRQSTQSADG SACSTITKTE
RLVQSSDGTK TSRTTTMESS YVKRSDNGNS TFVQTKSSYS SSSKKTGSVF DREDESASRQ
SSLAALERRQ AEKKKELMKA QSLPKTSASQ ARKAMMEKLQ KESGSSNPAA SQTTVQRSSS
FGVPNANSIK QMLLDWCRAK TRGYEHVDIQ NFSSSWSDGM AFCALVHNFF PDAFDYSKLT
PQNRRQNFEV AFSSAETLVD CVPLVEVEDM MIMGKKPDAK LQEVNSKINK RLKDALFTDQ
WSELFMDVLS PFHFILVSTV RMQGVILLVF AKYYHLPFLH DIQTDCTRTG LGGYWGNKGG
VSVRLSIFGH MVCFLNCHLP AHLEKAEQRK EDFATILHMQ QFEGPVANGI LDHDLVFWFG
DLNFRIESLD ICFVKYAIDS NVLSQLWEKD QLNIAKSTWP VLRGFQEGPL NFPPTFKFDV
GTNKYDSSAK KRKPAWTDRI LWKIKSPSKG LDTGGHRPSQ GILSVSQLCY CSHMEYTVSD
HKPVAAIFAV QFASKVDKPL VEIYVADEWS RPEQAVVRYK MAVGFHRSSW DWIGLYRVGF
RHPKDYVSYV WARSEEGERC LEKQLYAQVM FSEEALPKGN GEYILGYYSN TSSSIAGVTE
PFQISLPRSE EGSSSTDSSG SSSEEDDSTL VLLAPKSRSP SPGKMKRHRS RSPSLAKFQG
LILRPSSRDR GTSRSPSPQS RHSLPRSIPT IHLPQEELGH RGVKSKELGQ AAESPEGSSS
YQTPQEQGGL QRPCADSSLA RADPRNLGLL PALRLEMIDQ ALGRRRENAD QGYYPSRRMS
PTSPPGCGTS PEELDRHSCA MGH
//
