ID T2MJV2_HYDVU Unreviewed; 623 AA.
AC T2MJV2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform {ECO:0000313|EMBL:CDG72192.1};
DE Flags: Fragment;
GN Name=PIK3CD {ECO:0000313|EMBL:CDG72192.1};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG72192.1};
RN [1] {ECO:0000313|EMBL:CDG72192.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole animals {ECO:0000313|EMBL:CDG72192.1};
RX PubMed=24065732; DOI=10.1093/gbe/evt142;
RA Wenger Y., Galliot B.;
RT "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT bilaterian, euteleostome, and hominidae ancestors.";
RL Genome Biol. Evol. 5:1949-1968(2013).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
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DR EMBL; HAAD01005960; CDG72192.1; -; mRNA.
DR AlphaFoldDB; T2MJV2; -.
DR EnsemblMetazoa; XM_002157773.3; XP_002157809.3; LOC100210375.
DR EnsemblMetazoa; XM_047274332.1; XP_047130288.1; LOC100210375.
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; cd08380; C2_PI3K_like; 1.
DR Gene3D; 3.10.20.770; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
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; 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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR PANTHER; PTHR10048:SF118; PI-3 KINASE; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 2: Evidence at transcript level;
KW Kinase {ECO:0000313|EMBL:CDG72192.1};
KW Transferase {ECO:0000313|EMBL:CDG72192.1}.
FT DOMAIN 52..155
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 192..351
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 375..554
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CDG72192.1"
FT NON_TER 623
FT /evidence="ECO:0000313|EMBL:CDG72192.1"
SQ SEQUENCE 623 AA; 72436 MW; A69F0E5EB8B35390 CRC64;
EFRSKCIQFC DFISYQRSQS SWDRKAIYTY PPEFEEDYNL SSSLKEKLRI ENNCIHLSVS
IVKNSFITFK VADNIYPKEL IEKVLCKKIQ TSKLAQKENV NDYVLKVYGR LNFFLGHVVT
DSFGNEILEE KPILQYKYVR DCLQWDKPIR LVLIPKADLD IEKECAAPIL DNPPPTPEKR
KKNEICLWDI SPKTLFKVNI FAAKGIHNAQ MWKEIHCGIF HGGEEVCKVQ STNKLQQSTT
PHWNEFLEFD LPVADIPRMA RLCFSIVGYQ QNDRKKRKPV CIGWVNMPIF NYKAYLKTGT
CALYCWQYSI GRKNENQNFL NPLGTVASSG DENGACLIIK LTEFAHPVVY PSEEKIIQYA
ADKIKAEQVN GDQPHPYLRK GGKLHRQQIE EVIQRDTLLP MFEKEKELMW LLRVECSLEY
PQCLPKLLQC VKWNNRDSVA QIHLLLTTWK IDPLEVDVAL DLLDYKFPDN NVRTIAVKVL
DNLTDGELEM YLLQLIQALK YESYLDSPLA KYLLKRALNN RRIGHYLFWH LKAEAGNLEC
SLQFGLLLEL YCRGSVQHID ILTKQVEAIN KMKTMTEYLH QCKDQSKEDK IEMMRNIFNG
SSYKKAFSEI VSPLDPSIKL KCL
//
