ID A0A1S3PGL3_SALSA Unreviewed; 714 AA.
AC A0A1S3PGL3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A-like isoform X2 {ECO:0000313|RefSeq:XP_014026775.1};
GN Name=LOC106585266 {ECO:0000313|RefSeq:XP_014026775.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014026775.1};
RN [1] {ECO:0000313|RefSeq:XP_014026775.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014026775.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_014026775.1; XM_014171300.1.
DR AlphaFoldDB; A0A1S3PGL3; -.
DR GeneID; 106585266; -.
DR OrthoDB; 21647at2759; -.
DR Proteomes; UP000087266; Chromosome ssa24.
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: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; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR046985; IP5.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR041611; SKICH.
DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR PANTHER; PTHR11200:SF127; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 5-PHOSPHATASE A; 1.
DR Pfam; PF17751; SKICH; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 180..502
FT /note="Inositol polyphosphate-related phosphatase"
FT /evidence="ECO:0000259|SMART:SM00128"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..659
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 78263 MW; 2625A2ACE45E835B CRC64;
MDPDNQNQSQ PHPENPSGLS EVLTPTPAAP PGTETPTSEP CANAPAPQPS VPARPRRPQR
TPRVEGSVDV CEPKPDPTEA NQDRSTPDAP AGASRHKPLR PGAAKPPGGP GEPVGYTETT
PKAGPKVPGH PPGARNPISM RAASVPQPPS SRPIPPHLNP HAQRAFSVSG TADTQAQVVE
DFRVHIITWN VGGAMPPDDI TALLGLHVGD GNTDMYIIGL QEVNSMINKR LKDVLFTDQW
SDACMERLSP FGYILVTSQR MQGVLLLVFA KYYHLPFLRG VQTETTRTGL GGYWGNKGGV
SARMSVFGHT ICFLNCHLPA HMENSEQRME DFESILQQQQ FEGQAATGVL DHDVVFWFGD
LNFRIDDLEI PAVKTAIDNN KLTMLWEKDQ LNMAKDSETV LVGFLEGPLK FPPTYKFDVG
TDTYDTSGKK RKPAWTDRIL WRLRATAPFG QAPNAGKRGS VSGLSSGTKV TQHFYRSHME
YMVSDHKPVS SIFTLQFPYK VDMPLVTIMV EDEWNSIADA TCTFKAAPNF ARSSWDWIGL
YKVGFKHHKD YVGYVWAKQE EADYHRVEHE VTFTEEELPK GSGDFILCYY SNNMSTLVGV
TEPFQIQLPT SSPAGSPSDD SSDFTSEDDS TVVGMKTKSR SPSPRKKKHR TRHSQSRSPS
HSRSRSGSPA LQEMKGLKLQ PGLAHNTTDG SASGNAPEGT DREKASAEAG NTGL
//
