ID A0A485PMB5_LYNPA Unreviewed; 1486 AA.
AC A0A485PMB5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JAN-2026, entry version 34.
DE RecName: Full=Phosphatidylinositol 3-kinase C2 domain-containing subunit gamma {ECO:0000256|ARBA:ARBA00074898};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
DE EC=2.7.1.154 {ECO:0000256|ARBA:ARBA00012013};
DE AltName: Full=Phosphoinositide 3-kinase-C2-gamma {ECO:0000256|ARBA:ARBA00077517};
GN ORFNames=LYPA_23C019265 {ECO:0000313|EMBL:VFV44806.1};
OS Lynx pardinus (Iberian lynx) (Felis pardina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX NCBI_TaxID=191816 {ECO:0000313|EMBL:VFV44806.1, ECO:0000313|Proteomes:UP000386466};
RN [1] {ECO:0000313|EMBL:VFV44806.1, ECO:0000313|Proteomes:UP000386466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and
CC phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as
CC second messengers. May play a role in SDF1A-stimulated chemotaxis.
CC {ECO:0000256|ARBA:ARBA00054180}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; CAAGRJ010036391; VFV44806.1; -; Genomic_DNA.
DR Proteomes; UP000386466; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:TreeGrafter.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:TreeGrafter.
DR CDD; cd04012; C2A_PI3K_class_II; 1.
DR CDD; cd05177; PI3Kc_C2_gamma; 1.
DR FunFam; 3.30.1010.10:FF:000001; Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta; 1.
DR FunFam; 1.10.1070.11:FF:000013; Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma; 1.
DR FunFam; 1.25.40.70:FF:000010; Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma; 1.
DR FunFam; 3.10.20.90:FF:000260; Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma; 1.
DR FunFam; 3.30.1520.10:FF:000026; Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma; 1.
DR FunFam; 2.60.40.150:FF:000160; phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma isoform X1; 1.
DR FunFam; 2.60.40.150:FF:000125; Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 gamma; 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; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 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; IPR037707; PI3-kinase_C2_gamma_cat.
DR InterPro; IPR015433; PI3/4_kinase.
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; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF29; PHOSPHATIDYLINOSITOL 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT GAMMA; 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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:VFV44806.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000386466};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 285..371
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 521..669
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 684..860
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 929..1207
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1240..1352
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1365..1486
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 1486 AA; 170718 MW; F43A7CC4BCA82E94 CRC64;
MAYCWKTDLN TSESHEEQHE HQEFHSVNQS FFPSHVSLGF DQLVDEIRIK IPLYQSEIEE
NTVCVPHAPN WDSTRHSLHE THQIPLNELT SQTSELSCHQ VGKTPVIGFR RSVLPNPEDM
NKQSSCGNPI GKYHGGDDYR INISAPSSTS LDKINSQRES ENANHNYHIG FESSIPSTYP
SFSTNFMPKE ENKRSRNMNI VKHSLMLSEG SFPPRTWEST QPENTELTGC SIQLVEVPQG
SNKSLASFCD KVKKIRETYH AADINSNSGK IWSTTAAFPC QLFSNTKFNI NICIDNSTQR
LHFKPYANYL VKDLIAEVLH FSTNDELFPK DHLLSICGYE EFLQNDYSLG SHKIFQKDKS
VIQLTLHKNG KVPGKLSRKH EDDHSQFYLN QLLEFMHIWK ISRQCLSTVI KKYDFHLKCL
LKTQQNVDNI IEEVKNICSV LGCVETKQIT DAVNELNLTL QRNAENFHQN SETSAKGLIE
KVTTELSRAI YQLISVYCRS FYADFQPLNI PDDISYVNPG LHSHLSFTVY AAHNIPETWV
HSYKTFSFSC WLTYAGKKLC QVRSYRNIPV KKLFFFLVNW NEIINFPLEV KSLPRESMLT
IRLFGIICTT NNANLLAWTC LPLFPKDKSI LGSMLFSMTL QSEPPIEMIA PGVWDISQPS
PVILQIAFPA TEWEYMKLDS EENRSKPEEP PKECLKHISR LSQKQSPLLL SEEKRRYLWF
YRFYCNNENC SLPLVLGSAP GWDERTVSEM HTILRRWKFS CPLEALGLLT SSFPDQEIRK
VAVQQLDNLL NDELLDYLPQ LVQAAKFEWN LESPLVQLLL HRSLQSIQIA HRLYWLLKDA
QNETYFKSWY QKLLAALQFC SGKALSDEFS KEKKLIKILG DIGEKVKSAS DPQRQEVLKK
EIGRLEEFFQ CINTCHLPLN PALCIRGIDH DACSYFTSNA LPLKITFINA NPMGKNISVI
FKAGDDLRQD MLVLQIIQVM DNIWLQEGLD MQMIIYRCLS TGKGQGLVQM VPDAITLAKI
HRHSGLIGPL KENTIKKWFS QHNHLKADYE KALRNFFYSC AGWCVVTFIL GVCDRHNDNI
MLTKSGHMFH IDFGKFLGHA QTFGGIKRDR APFIFTSEME YFITEGGKNP QHFQDFVELC
CRAYNIVRRH SRLLLNLLEM MLHAGLPELS GIQDLKYVYN NLRPQDTDLE ATSHFTKKIK
ESLECFPVKL NNLIHTLAQM TATSPAKSAS QTPSQESCML SATRSIQRAT ILRFSKKTSN
LYLIQVIHGN NEMSLTEKSF DQFSKLHSQL QKQFASLTLP EFPHWWHVPF TNSDHKRFRD
LNHYMEQILN GSYKVANSDC VLSFFLSEPV QQTIEEPSFV DLGEKFPDKT PKVQLVISHE
DAKLTILVKH MKNIHLPDGS APSAHVEFYL LPYPSEVRRR KTKSVPKCTD PTYNEIVVYD
EVTELQGHIL MLIVKSKSIF VGAINIQLYT VPLNEEKWYP LGNCII
//
