ID A0A3Q0RB46_AMPCI Unreviewed; 890 AA.
AC A0A3Q0RB46;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Si:rp71-17i16.5 {ECO:0000313|Ensembl:ENSACIP00000009379.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000009379.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000009379.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR Ensembl; ENSACIT00000009661.1; ENSACIP00000009379.1; ENSACIG00000007280.1.
DR GeneTree; ENSGT00940000165924; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; cd00864; PI3Ka; 1.
DR Gene3D; 3.10.20.770; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 2.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR InterPro; IPR016024; ARM-type_fold.
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; 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; IPR045580; PIK3CG_ABD.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF99; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT GAMMA ISOFORM; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 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; PF19710; PIK3CG_ABD; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 781..799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 819..838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 179..267
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 315..486
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 517..695
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 626..873
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 494..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 101584 MW; D0177EA2073E8811 CRC64;
MHFFKKKVKT FSNSRNVLTG IFYFTFISLG SPIEIAIFFT RETGQNSNPF AILDPEKYTL
LYARGGDWYE AYDDCQVIRT LDIPWSHDDP RCLTARILVK PPVAVDPEEK EKQRQCLTYL
IGHDLEKEAS DRLGELTFTR RKLAAPRKQE LKNRDNKLYA TEPWITYASL PDDLQEWLNR
DLPVTFHYMS RISFSIKAEL STTPELLLQV FERVAKAQGV KCESFDDLVL KVTGREEFLS
GDYTLCDFLW VRQCLRXNQE LHLSVVPMSQ LASEAVKFVD WPLVDGFSGX FSSHDDLRLX
GKDLDDIFMI SLWDCRRNFR VKLLGIDIPQ LPSKCPQSVY VEASILYGNK VLSSVCSFPK
AFADEVLWNE WLDFDFLLRD LPRGAKLGLT INESPSDMSP ITKDSRPSVN KDTKKGKGKV
LYFVNLLLID HRSVLSQGPH TLHMWSHPGL DDEAITYQAD KLSSATNPDI ADSMAISFLL
DRYSFPVVVP NTISHSECSD SPTPTKSEPQ ESCRTVPPPL PIKKSYLQAK LPETVTLRSP
SPTSDTRTAG LRRFREESIR YSSSLPHYLR SVDWMSRRVV EDVHWLLGNW NPEELDLTVA
LELLSMDYAD EIARRLAVQR LESLSNDDVL KYLLQLVQTL KVEPYHDSFL ARFLIQRALR
VSHEAFTVDV VYCHIHKGEK SLDLNLIPYG CISTGQNIGM IEIVRNATTI AAVQRSQGGT
TGAFKNNALF EWLKSKCPLQ EIFVKSCAGY CAATYVLGIG DRHNDNIMIT EDGIHWLIGH
FKFPIVFPFF FSVCLYLLPT PTQDTCTEAY LSLRAHSRLL VTLFSLMLLT GIPELSAAED
MRYLRVALQE EQSEADAREH FLQQISECEK LGWTVQANFW IHMVGVFNFQ
//
