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Database: UniProt
Entry: A0A151NNN8_ALLMI
LinkDB: A0A151NNN8_ALLMI
Original site: A0A151NNN8_ALLMI 
ID   A0A151NNN8_ALLMI        Unreviewed;      1113 AA.
AC   A0A151NNN8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=Y1Q_0015641 {ECO:0000313|EMBL:KYO38393.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO38393.1};
RN   [1] {ECO:0000313|EMBL:KYO38393.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO38393.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYO38393.1}.
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DR   EMBL; AKHW03002524; KYO38393.1; -; Genomic_DNA.
DR   RefSeq; XP_019343430.1; XM_019487885.1.
DR   RefSeq; XP_019343431.1; XM_019487886.1.
DR   AlphaFoldDB; A0A151NNN8; -.
DR   STRING; 8496.A0A151NNN8; -.
DR   GeneID; 102576763; -.
DR   KEGG; amj:102576763; -.
DR   eggNOG; KOG0565; Eukaryota.
DR   OrthoDB; 21647at2759; -.
DR   Proteomes; UP000050525; 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:UP000050525};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191}.
FT   DOMAIN          6..102
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REGION          107..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          878..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          962..1000
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1028..1113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        962..990
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1078..1092
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1099..1113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1113 AA;  124722 MW;  F753BBF58ACCFE97 CRC64;
     MTAASWYHRD ISRVVAEDLL AKAGKDGCFL VRDSESVSGA YALCLLFQRH VHTYRILPDE
     EGLLSVQTIQ GIQAKCFRTL TDLISTYQQP NNGLVTPLLY PVNRVREPAD EDSDGEDGRA
     FYPPSLASHS GAGTGSGWAT TQSNKMQISQ QLHLRLQEQV HSSPASDFMG FMAEYLNHHL
     QLDLEALRNG NLQLRHLSMA LVTACRGLHS EIDFTLAGLE TLAKVFDSPA SPRSPVREQG
     LLASDPDLEL LLSKISTVNH LLSSLEKKVL KSLQETVSRH NLALPSMAVA QTQSPAAKPM
     AVQSFEVKVG KLQKATLTVD VEAGTVAIMK RGSSSPEETI TQDKILQLIK YQSMQTKVRL
     VYDREQHRNL IRDFLFQNAR KREAFCQLLQ LMKIQHSSLD EPDLISVYVG TWNMGSAPPP
     RSLASWLTSR GLGRTHDETT ACIPHDIYVI GTQENSLGDR EWVEFLRASL KTLMAIDFRV
     VALQCLWSIK IVVLVKPEHE RRISHVNTSS VKTGIANTLG NKGAVGVSFL FNGTSFGFVN
     CHLASGSEKI HRRNQNYSDI LRSLVLGDKR LSGFDLTLRF THLFWFGDLN YRLSMDVQDI
     LARVNKKEFE TLLVVDQLNL EREKSKVFLR FNEADISFPP TYRYERGSRD TYVWQKFKHT
     GMRINVPSWC DRILWKSQPE THVICNAYGC TNDIMTSDHS PVFATFEVGV MSQFVPKKAP
     GSSPESLACI EWDSIEVIVK TASRSRCYIE FYSSCLEESQ RSGENSSQNS DIPGFLKLSW
     SAKQLPVLNP ILSDLEYLLD QHLLLSVKGV DGCESYGECC IAMRSMISSL AQQFETFLYH
     RGEETGSMRG WMKVRVPKDR RSTRERLYEW ISFETDATES PEDTSPCTKP SQHSVRSRPF
     SFPETASSYT NPAYFIFEGV PNTWTLGTNL PEPPYSSASD VQEEACLGHV PGHRLRSLAG
     EQTCSSGEPL QRSPHYSVPV STSYGHQLSP LQSGRHKRPK SALLLRDMPA SSDCSLTALH
     LAKHLSDLDT EPHKRGSCLG TSQLKSRKNP LRHTRSALEP PPQDFQEGTV FLQSSHQLSH
     DLERHRRTGP VGSRSAEPHS PRAPQSQASQ EQL
//
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