ID A0A1L8GEH2_XENLA Unreviewed; 1689 AA.
AC A0A1L8GEH2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha {ECO:0000313|RefSeq:XP_018115854.1, ECO:0000313|RefSeq:XP_018115855.1};
GN Name=pik3c2a.S {ECO:0000313|RefSeq:XP_018115854.1,
GN ECO:0000313|RefSeq:XP_018115855.1, ECO:0000313|RefSeq:XP_018115856.1,
GN ECO:0000313|Xenbase:XB-GENE-17332306};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018115854.1};
RN [1] {ECO:0000313|RefSeq:XP_018115854.1, ECO:0000313|RefSeq:XP_018115855.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018115854.1,
RC ECO:0000313|RefSeq:XP_018115855.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018115854.1,
RC ECO:0000313|RefSeq:XP_018115855.1};
RG RefSeq;
RL Submitted (APR-2022) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR RefSeq; XP_018115854.1; XM_018260365.2.
DR RefSeq; XP_018115855.1; XM_018260366.2.
DR RefSeq; XP_018115856.1; XM_018260367.2.
DR STRING; 8355.A0A1L8GEH2; -.
DR PaxDb; 8355-A0A1L8GEH2; -.
DR GeneID; 108715313; -.
DR KEGG; xla:108715313; -.
DR AGR; Xenbase:XB-GENE-17332306; -.
DR CTD; 108715313; -.
DR Xenbase; XB-GENE-17332306; pik3c2a.S.
DR OMA; CTRISWA; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 108715313; Expressed in testis and 19 other cell types or tissues.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04012; C2A_PI3K_class_II; 1.
DR CDD; cd08381; C2B_PI3K_class_II; 1.
DR CDD; cd05176; PI3Kc_C2_alpha; 1.
DR CDD; cd07289; PX_PI3K_C2_alpha; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR037705; PI3K-C2-alpha_dom.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042133; PX_PI3K_C2_alpha.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF28; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 424..512
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 683..852
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 861..1038
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1106..1384
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1422..1538
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1562..1681
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1689 AA; 191008 MW; 1DCEC6C8C06F9C8E CRC64;
MAYISSSNGF RQNISSSAGT TRPKEIDKEE ALQMEAEALA KLRKDRRQVR GQGRAFMPTR
QKPPASGRQE PDLMVFPESD AKKNTETLLG IDVEKLTDAE MERLLLDDFF ELKRPPKPLA
LSQVPVVNPR ASSQFYGQPS FQSSQWAPGI QGNMNLLPTF SASYPKCADP FQNGYNANVP
AVQRHNPVYL RLPTCTQYMS YQMSASAPFQ PRGNLPGYSN TVPPDMAKLF DKIATTSEFV
KNGRLSAEAD TPKSESTSPT LHGADNADSI NKFDWLDLDP LSKLKADSTD FSIHAQVSGA
APTDSKAKDP WDAVLLEEKP IKHNSPEKKL NGKPSGATVT RSLSLNIRPT HLQQKWDQTV
RDRGTKVLAE KSPLKEFEAD DEEVAAFCEE VARLRKKYPS NSLQTNPGFV LSPVMLQRNL
NAENANVKVS IEIGSLQQPV TFTCDVSSPV ELIIMQALCW VHDDLSQVDI ESYILKVCGQ
EEVLQNKHCL GSHEYIQLCR KWDTDIRLQL LSHSTVNRDL ARTAEDDVSP VDLNKHLAVV
DRPFKKPITR QSIEELLDTY HEQVSMCLKH ESNPYRLVEQ LIKVVRNICK TVGSVETQAI
TESVKKLRRA VNLPRSRSIE ASPTNLSDQC APDSAGQCDN PLQETLALLT TDLHNLLQLH
FSSENSAVTS PPGGRPLKEA RYSTDHLQFT IFAAHGIPTG WVSCFEKYYL VCSLIHNGKD
KFKPVQSKKV GTYKSFFYLV KWDELIIFPI QISQLPLESI LQLTLYGILN PNSGGSPDAN
KQRKGPEMLG RVSLPLFTFR RMLIGGTKLL HLWTSFHTGP APAATTRKTN LMQRIVLQVD
FPLPAFDIVY IPPHPTKSCA WQSIESLDKE NKSRLLSLLA KESAFGLSKE EKAFIWEKRY
YCLEYRNSLP KILASAPNWD VAYLSDIYSL IHAWPPMTAV SALELLDSRF SDQEVRTVAV
KWVEEGLSDD ELVDFLPQFV QAIKYELYLD NSLVRFLLTR SLGNIRITHY FYWLLKDSLN
DPYFGIRYER ILGALLSVCG KGLREELEKQ TRLTQLLGVV AEKVRQANGS ARQVVLQEGM
ERAQLLFSKT KCRLPLSPSL VAKELNIKAC SFFSSNAVPL KVTMINVDPL GEELNSMFKV
GEDLRQDMLA LQMIKIMDKL WLQEGLDLRM VLFKCLSTGR DRGMVELVLS SDTLRKIQVE
NGVTGSFKDK PLAEWLRKYN PSEEDYAKAS ENFIYSCAGC CVATYVLGIC DRHNDNIMLR
TTGHMFHIDF GKFLGHAQMF GSFKRDRAPF VLTSDMAYVI NGGEKPTRRF QLFVDLCCQA
YNLLRKHTSL FLNLLSLMLP SGLPELTGIQ DLKYVHDALQ PQATDTEATI FFTRLIESSL
GSVATKFNFF IHNLAQRFAG LPSNDEAILS FSPKTYTLKQ DGRIKEATIF TYHKRYNPDK
YYIYVVRVVR EGQDNSAFIF RTFDEFQELH NKLSILFPLW KLPGFPSKVV LGRTHIKEVA
AKRKVELNSY IQSLMGSSPE VAECDLVYTF FHPLLRDDKS EGCDAIVMPL DEPPLSPTSG
RIEGEIKLSI SYRNGTLFIM VMHIKNLVTE DNADPNPYVK TYLLPDPHKT SKRKTKVSRK
TCNPTFNEML VYSGYNKETL RQRELQLSVL SAESLRENFF LGGVTLPLKD FNLNQETIKW
YKLTEVPYL
//
