ID A0A096MPN3_PAPAN Unreviewed; 1315 AA.
AC A0A096MPN3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 {ECO:0000256|ARBA:ARBA00034348};
DE EC=3.1.3.86 {ECO:0000256|ARBA:ARBA00012981};
DE AltName: Full=Inositol polyphosphate phosphatase-like protein 1 {ECO:0000256|ARBA:ARBA00034353};
DE AltName: Full=Protein 51C {ECO:0000256|ARBA:ARBA00034368};
DE AltName: Full=SH2 domain-containing inositol 5'-phosphatase 2 {ECO:0000256|ARBA:ARBA00034357};
GN Name=INPPL1 {ECO:0000313|Ensembl:ENSPANP00000001694.3};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000001694.3, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000001694.3, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000001694.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-
CC 3-phospho-(1D-myo-inositol-3,4-bisphosphate) + phosphate;
CC Xref=Rhea:RHEA:43556, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83420, ChEBI:CHEBI:83422;
CC Evidence={ECO:0000256|ARBA:ARBA00034236};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43557;
CC Evidence={ECO:0000256|ARBA:ARBA00034236};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:43548,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416,
CC ChEBI:CHEBI:83417; Evidence={ECO:0000256|ARBA:ARBA00034246};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43549;
CC Evidence={ECO:0000256|ARBA:ARBA00034246};
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: Basal cell membrane
CC {ECO:0000256|ARBA:ARBA00034304}. Cell projection, filopodium
CC {ECO:0000256|ARBA:ARBA00004486}. Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Nucleus speckle
CC {ECO:0000256|ARBA:ARBA00004324}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC family. {ECO:0000256|ARBA:ARBA00008734}.
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DR AlphaFoldDB; A0A096MPN3; -.
DR Ensembl; ENSPANT00000008196.3; ENSPANP00000001694.3; ENSPANG00000002495.4.
DR eggNOG; KOG0565; Eukaryota.
DR eggNOG; KOG4384; Eukaryota.
DR GeneTree; ENSGT00940000156576; -.
DR HOGENOM; CLU_007493_1_1_1; -.
DR OMA; TERMGTR; -.
DR Proteomes; UP000028761; Chromosome 12.
DR Bgee; ENSPANG00000002495; Expressed in iris and 66 other cell types or tissues.
DR ExpressionAtlas; A0A096MPN3; baseline.
DR GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IEA:Ensembl.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
DR CDD; cd09101; INPP5c_SHIP2-INPPL1; 1.
DR CDD; cd09491; SAM_Ship2; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
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; PF00536; SAM_1; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
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:UP000028761};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 21..174
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 1261..1315
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 176..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1011
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1066
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1315 AA; 144886 MW; 89DF0DFA8B2D8575 CRC64;
MASACGAPGP GGALGSQAPS WYHRDLSRAA AEELLARAGR DGSFLVRDSE SVAGAFALCV
LSLEGRGYGV LRPSVTVMDE KFGHSPADPF RHPPGRSEQG RGCAFYVVCS PVWIGTEWYQ
KHVHTYRILP DGEDFLAVQT SQGVPVRRFQ TLGELIGLYA QPNQGLVCAL LLPVEGEREP
DPPDDRDASD GEDEKPPLPP RSGSTSISAT TGPSSPLSVP ETPTTPAAES APNGLSTVSH
EYLKGSYGLD LEAVRGGASH LPHLTRTLAT SCRRLHSEVD KVLSGLEILS KVFDQQSSPM
VTRLLQQQNL PQTGEQELES LVLKLSVLKD FLSGIQKKAL KALQDMSSTA PPAPQPSTRK
AKTIPVQAFE VKLDVTLGDL TKIGKSQKFT LSVDVEGGRL VLLRRQRDSQ EDWTTFTHDR
IRQLIKSQRV QNKLGVVFEK EKDRTQRKDF IFVSARKREA FCQLLQLMKN KHSKQDEPDM
ISIFIGTWNM GSVPPPKNVT SWFTSKGLGK TLDEVTVTIP HDIYVFGTQE NSVGDREWLD
LLRGGLKELT DLDYRPIAMQ SLWNIKVAVL VKPEHENRIS HVSTSSVKTG IANTLGNKGA
VGVSFMFNGT SFGFVNCHLT SGNEKTARRN QNYLDILRLL SLGDRQLSAF DISLRFTHLF
WFGDLNYRLD MDIQEILNYI SRKEFEPLLR VDQLNLEREK HKVFLRFSEE EISFPPTYRY
ERGSRDTYAW HKQKPTGVRT NVPSWCDRIL WKSYPETHII CNSYGCTDDI VTSDHSPVFG
TFEVGVTSQF ISKKGLSKTS DQAYIEFESI EAIVKTASRT KFFIEFYSTC LEEYKKSFEN
DAQSSDNINF LKVQWSSRQL PTLKPILADI EYLQDQHLLL TVKSMDGYES YGECVVALKS
MIGSTAQQFL TFLSHRGEET GNIRGSMKVR VPTERLGTRE RLYEWISIDK DEAGAKSKAP
SVSRGIQEPR SGSRKPAFTE ASCPLSRLFE EPEKPPPTGR PPAPPRAAPR EEPLTPRLKP
EGAPEPEGVA APPPKNSFNN PAYYVLEGVP HQLLPPEPPS PARAPVPPAT KNKVAITVPA
PQLGRHRPPR VGEGSSSDEE SGGTLPPPDF PPPPLPDSAI FLSPSLDPLP GPVVRGRGGG
EARGPPPPKA HPRPPLPPGP SPASTFLGEV AGGDDRSCSV LQMAKTLSEV DYAPAGPARS
ALLPGPLELQ PHRGLSSDYG RPLSFPPPRI RESIQEDLAE EAPCPQGGRA SGLGEAGMGA
WLRAIGLERY EEGLVHNGWD DLEFLSDITE EDLEEAGVQD PAHKRLLLDT LQLSK
//
