ID L5M1T8_MYODS Unreviewed; 1848 AA.
AC L5M1T8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=MDA_GLEAN10026080 {ECO:0000313|EMBL:ELK32609.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK32609.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the WD repeat ATG16 family.
CC {ECO:0000256|ARBA:ARBA00009271}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC family. {ECO:0000256|ARBA:ARBA00008734}.
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DR EMBL; KB105166; ELK32609.1; -; Genomic_DNA.
DR eggNOG; KOG0565; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
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; cd22887; Atg16_CCD; 1.
DR CDD; cd09100; INPP5c_SHIP1-INPP5D; 1.
DR CDD; cd10343; SH2_SHIP; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR013923; Autophagy-rel_prot_16_dom.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR46051:SF3; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 5-PHOSPHATASE 1; 1.
DR PANTHER; PTHR46051; SH2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08614; ATG16; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 4.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000010556};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 5..101
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REPEAT 1559..1600
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1603..1644
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1645..1686
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1703..1725
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1781..1812
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1814..1848
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 104..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1323..1471
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 104..118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1848 AA; 207283 MW; CD8957BE057A5608 CRC64;
MVPCWNHGNI TRSKAEELLS RTGKDGSFLV RASESISRAY ALCVLYRNCV YTYRILPNED
DKFTVQASEG VPMRFFTKLD QLIEFYKKEN MGLVTHLQYP VPLEEEDTGD EPEEEIEGVP
SPPELPPRNI PLSAGPCEAK EVPLLSENLR ATEVSRPCLS ETLFQRLQNM DTSGLPEEHL
KAIQDYLSTQ LTLDADFVKT GSSSLPHLRK LTLLLCKELY GEVTRTLPSL ESLQRLFDQQ
LSPGLRPRPQ VPGEANPINM VTKLSQLTSL LSSIEDKLKA LLHEGPESSH RRSLIPPVTF
EVKSESLALP QKLQLKVDVE TGKLIIKKSK DGSEDKFYSH KKILQLIKSQ KFLNKLVILV
ETEKEKTVRK EYVFADSKKR EGFCQLLQQM KNKHSEQPEP DMITIFIGTW NMGNAPPPKK
ITSWFLSKGQ GKTRDDSADY IPHDIYVIGT QEDPLGEKEW LEILKNSLQE ITSITFKMIA
IHTLWNIRIV VLAKPEHENR ISHICTDNVK TGIANTLGNK GAVGVSFMFN GTSLGFVNSH
LTSGSEKKLR RNQNYTNILR FLALGDKKLS PFNITHRFTH LFWLGDLNYR VELPTWEAEP
MIQKIKQQQY ADLLCHDQLL MERKEQKVFL HFEEEEITFA PTYRFERLTR DKYAYIKQKA
TGMKYNLPSW CDRVLWKSYP LVHVVCQSYG STSDIMTSDH SPVFATFEAG VTSQFVSKNG
PGTVDSQGQI EFLRCFATLK TKSQTKFYLE FHSSCLESFV KSQEGENEEG SEGELVVKFG
ETLPKLKPII SDPEYLLDQH ILISIKSSDS DESYGEGCIA LRLEATETQL PIYTPLTHHG
EMTGHFRGEI KLQTSQGKMR EKLYDFVKTE RDESSGPKSL KSLTSHDPMK QWEPASRVPL
CSGSSITEII NPNYMGVGSF GYIKQTLSPD QQPTAWSYDQ PLKDSSLGSG RGETPPTPPS
QPPISPKKFS SSTTTRVPCP RTQESRPSDL GKNAVEPLPQ EDPKLTKPEM FENPLYGSVC
SFSKLVPRKE QESPKMLKKE LPPCPDPGSL SPNILLSKAQ EAEGNKGTGK PVPTPAPTPF
ISPTPRLRSF TCSSPAEGRP AAGDKSQGKP KAPASSPVPV PAKRPIKPSR SELSQQAPPT
PAQRPPLPLK SPAVLHLQHS KGRDYRETAE LPHHGKHRPD DTPLSRTAMQ DSSSFPYHRS
DSWPMLHPAG TGAVTGARAE PARSPNASQR PPLSPQCFRP REGVIDERDC VGADHRHISE
ELRRRDRLQR QAFEEIILQY NKLLEKSDLH SVLAQKLQAE KPDIPNRHEI SPGHDGAWND
GQLQEMAHLK MKHQEELTEL HKKRGELAQL VIDLNNQMQQ KDREMQMNEA KIAECLQTIS
DLETECQELR SKLQDLERAN QTLKDEYDAL QITFTALEEK LRKTSEENQE LVTRWMAEKA
QEANRLNAEN EKDSRRRQAR LQKELAEAAK EPLPVEQDDD IEVIVDETSD HTEETSPMRA
ISRAATKRLS QPAGGLLDSI TNIFGRRSVS SFPVPHDNAD THPGSSKEVR VPTTAVCVFD
AHDGEVNAVQ FSPGSRLLAT GGMDRRVKLW EVSGDKCEFK GSLSGSNAGI TSIEFDSAGS
YLLAASNDFA SRIWTVDDYR LRHTLTGHSG KVLSAKFLLD NARIVSGSHD RTLKLWDLRS
KVCIKTVFAG SSCNDIVCTE QCVMSGHFDK KIRFWDIRSE TIIREMELLG KITALDLNPE
RTELLSCSRD DLLKIIDLRI NAVRQTFSAP GFKCGSDWTR VVFSPDGSYV AAGSAEGSLY
VWSVLSGKVE KVLSKHHGSS INAVAWSPSG SHIVSVDKGS KAVLWSEY
//
