ID M7BS68_CHEMY Unreviewed; 1142 AA.
AC M7BS68;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase {ECO:0000256|ARBA:ARBA00012981};
DE EC=3.1.3.86 {ECO:0000256|ARBA:ARBA00012981};
GN ORFNames=UY3_02733 {ECO:0000313|EMBL:EMP40044.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP40044.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:57836; EC=3.1.3.86;
CC Evidence={ECO:0000256|ARBA:ARBA00023377};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25529;
CC Evidence={ECO:0000256|ARBA:ARBA00023377};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC family. {ECO:0000256|ARBA:ARBA00008734}.
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DR EMBL; KB514808; EMP40044.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BS68; -.
DR STRING; 8469.M7BS68; -.
DR eggNOG; KOG0565; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR CDD; cd10343; SH2_SHIP; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR PANTHER; PTHR46051:SF2; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 5-PHOSPHATASE 2; 1.
DR PANTHER; PTHR46051; SH2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191}.
FT DOMAIN 6..102
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 107..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1142 AA; 127803 MW; 8825890444355C8C CRC64;
MTAASWYHRD ISRVVAEDLL AKAGKDGCFL VRDSESVSGA YALCLLFQRH VHTYRILPDE
EGLLSVQTIQ GIQAKCFRTL TDLIGAYQQP NNGLVIPLLY PVNRAREPVE EDSDGEDGRA
SHPPSLVPHS GIIAGSTSGW VTAQPNKAQI SQQLQLRLQE QVHSSPASDF MGFMADYLSH
HLQLDLEALR NGNLQLRHLS TALVTACRGL HSEIDFTLAG LETLAKVFDP PASPRSPVRE
QGLLASDPDL ELLLSKIATV NHLLSSLEKK MSITSSVTLP LLRDSHEGQI CVIASFLEQG
IVICSQAITL DASMAKLTES LYGSPKHELF TLSPPLVLKT LQETVIKHKL ALPSMAAVHP
PAAKPMAVQS FEVKVGKTQR ASLTVDVESG TMAITKRGCS SPEETISQDK ILQLIKYQSM
QSKVRLVYDR DQHRSLTRDF IFQNARKREA FCQLLQLMKI QHSNLDEPDL ISVYVGTWNM
GSAPPPRSMA SWLTSRGLGQ TQDETTAGIP HDIYVIGTQE NSLGDREWVE FLRASLKTLM
SIDFRVVALQ CLWSIKIVVL VKPEHERRIS HVNTSSVKTG IANTLGNKGA VGVSFLFNGT
SFGFVNCHLA SGSEKTHRRN QNYSDILRSL VLGDRRLSSF DLTLRFTHLF WFGDLNYRLD
MEVQDILAHV NKKEFEALLA VDQLTLEREK NKVFLRFSEG DISFPPTYRY ERGSRDSYVW
QKFKTTGVRI NVPSWCDRIL WKSHPETHML CNSYGCTDDI VTSDHSPVFA TFEVGVTSQF
VPRKVPGSSP ESLACIEWDS VEVIVKTASR SKCYIEFHSY CLEGECCIAM RSMVGSLAQQ
FETFLFHRGE ETGSMRGWMK VRVPKDRRST RERLYEWISF ETDETESDFP TLSKPALRAV
RSRPLSLPDA AGSYTNPAYF IFEGVPNTWA QCPRLPEPPY SQASDRQADR YLDHSPCRRL
QSLTGAQACS SSKEQLQRSP HYSVPETISC GHQLSPSQIG RHKRPKSAIL TRHPQTSGDC
SLTALHMAWC LSDVDTEPHK RGSCLDPSQP EGRKNLLRHT RSALEPPPQS CWEGAGSQRD
TRRLNRAREF LSFSPLSRNI TDQDLLDTGV LSTTHRKLIQ AKLHESSPRS LQQGPSLKPN
LS
//
