ID A0A3Q0GNB3_ALLSI Unreviewed; 1333 AA.
AC A0A3Q0GNB3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta isoform X3 {ECO:0000313|RefSeq:XP_025061269.1};
GN Name=PIK3C2B {ECO:0000313|RefSeq:XP_025061269.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025061269.1};
RN [1] {ECO:0000313|RefSeq:XP_025061269.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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_025061269.1; XM_025205484.1.
DR Proteomes; UP000189705; Unplaced.
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:0046854; P:phosphatidylinositol phosphate biosynthetic process; 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; cd00869; PI3Ka_II; 1.
DR CDD; cd00895; PI3Kc_C2_beta; 1.
DR CDD; cd07290; PX_PI3K_C2_beta; 1.
DR Gene3D; 3.10.20.770; -; 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; 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; IPR042134; PX_PI3K_C2_beta.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF30; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT BETA; 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; 1.
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:UP000189705};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 74..162
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 326..485
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 504..680
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 749..1027
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1064..1180
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1203..1323
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 1333 AA; 152353 MW; 0DBA82647483AEA2 CRC64;
MQPGASSKGY VASRPHSLAN GYELFEVSEE RDEEVAAFCH MLDVLRSGYS IKDYSLTGYV
WSAVNLSPEH LGHGISLKVT VVYDSLQEPL TFTCDCSSTV DLLIYQTLCY THDELHDIDV
DNFVLKLCGL EEFLQNKHAL GSHEYIQHCR KFDADIRLQL MKRKAVRSDL ARTVNDDQSP
STLNHYIHLQ ERPIKQTISR QALSLLFDTF HNEVDTFLAA EGDVQPKAER VIQSVMAICN
ALAAIESQEI TRALNQMPPC PSRMQPKIQK DPNVLAVREN REKIVETLTA SILDLVELYC
NTFNADFQTA VHGSRKHYLV QEACLLPCPL SFTVYATHRI PITWAASYED FYLSCSLSHG
GKELCSPLQT RKAHVYKYLF HLIIWDQQIC FPIQVNRLPR ETLLSVTLYA VPVPPPGSSS
ETNKQRRVPE ALGWVTTPLF NFRQVLTCGR KLLGLWPATQ DNSRARSSAP NFNQPDSVIL
QIDFPTSAFD VRFMSPPAAE FSPKYEFGSL GDEEQRRLRE VMQKKSLYWL TDADRKRLWE
KRYYCHTEPG SLPLLLASAP SWEWACLPDI YALLKQWTYM NHQDALGLLH ATFPDQEVRR
TAVQWIDSIS DAELLDYLPQ LVQALKYECY LDSPLVRFLM KRAICDLKIT HYFFWLLKDG
LKDSQFSIRY QYLLAALLCC CGKGLREEFD RQCALVNTLA KLAQQIREAA PSSRQAILRE
GLEDVKQFFN IPGSCRLPLS PSLLVKGIVP RDCSYFNSNA VPLKLSFQNV DPLGENIRVI
FKCGDDLRQD MLTLQMIRIM NKIWVQEGLD MRMVIFRCFS TGRGRGMVEM IPNAETLRKI
QVEHGVTGSF KDRPLADWLQ KHNPKEDEYE KAVENFIYSC AGCCVATYVL GICDRHNDNI
MLKTTGHMFH IDFGRFLGHA QMFGNIKRDR APFVFTSDMA YVINGGDKPS SRFHDFVDLC
CQAYNLIRKH THLFLNLLGL MLSCGIPELS DLEDLKYVYD ALRPQDSEAD ATTYFTRLIE
SSLGSVATKL NFFIHNLAQM KFTGSDARPT LSFAPRTHTL KASGRIRDVF LCRHEKIFNP
SKGYMYIVQV QRESPHEITY VQRTFEEFQE LHNKLRLLFP SSQLPSFPSR FVIGRSRGEA
AAERRKEELN GYIWHLIHSA PEVTECDLVY TFFHPLPRDE KAAGTSPAPK PADATWARPI
GKVGGEVKLS ISYKNNKLFI MVMHIRGLQP IQDGNDPDPY VKIYLLPDPQ KTTKRKTKVA
RKTCNPTYNE MLVYDGIPKG DLQQRELRLS VLSEEGFWEN ILLGEVSIKL RDLDLTQEKM
GWFALGSRSH GTM
//