ID A0A1S3SDX2_SALSA Unreviewed; 886 AA.
AC A0A1S3SDX2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3 {ECO:0000256|ARBA:ARBA00019787, ECO:0000256|PIRNR:PIRNR000587};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073, ECO:0000256|PIRNR:PIRNR000587};
GN Name=LOC106608867 {ECO:0000313|RefSeq:XP_014062528.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014062528.1};
RN [1] {ECO:0000313|RefSeq:XP_014062528.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014062528.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|PIRNR:PIRNR000587};
CC -!- SUBCELLULAR LOCATION: Midbody {ECO:0000256|ARBA:ARBA00004214}.
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_014062528.1; XM_014207053.1.
DR AlphaFoldDB; A0A1S3SDX2; -.
DR GeneID; 106608867; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000087266; Chromosome ssa07.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08397; C2_PI3K_class_III; 1.
DR CDD; cd00870; PI3Ka_III; 1.
DR CDD; cd00896; PI3Kc_III; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
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 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; 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; IPR008290; PI3K_Vps34.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR PIRSF; PIRSF000587; PI3K_Vps34; 1.
DR SMART; SM00142; PI3K_C2; 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 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; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000587};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 34..183
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 292..519
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 604..870
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 147..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 100563 MW; 8FFC0313F37D26C9 CRC64;
MDTDKFNYVY SCDLDINVQL KIGSLEGKRE QKSYKALLQD PMLRFSGLYQ ENCSDLYVTC
QVFAEGKPLA LPVRTSYKAF STRWNWNEWL KLPVKYPDLP QSAQVALTVW DVYGPGRATP
VGGTTVTLFG KYGMFRQGMH DLKVWPGVEG DGGEPTSTPG RTSSSLAEDQ MGRLAKAPDL
EFLSDLTKAH RQGHMVKVDW LDRLTFREIE MINESEKRSS NFMYLMVEFP RVKTGEKPEY
SIVYYEKDGD DASPVLTSAD IVKVPDPQMC MENLVESKHH KLARSLRSGP SDHDLKPNAA
TRDQLNVIVN YPPTKQLSSE EQDLVWKFRY YLTTQEKALT KFLKCVNWAL PGEAKQALEL
LGKWRPMDVE DSLELLSSQF TNPTVRRYAV TRLQQADDED LLMYLLQLVQ ALKYENFNDI
QCGLEPGGKR DSQGLAESST LGDLDSSQIL TAPAVPPPVP NGKEGADSEN PEDLCTFLIS
RACKNSTLAN YLYWYVIVEC EDQDTQQRDL KTHKMYLNVI GRFSQALLKG DKSVRVMRSL
LASQQTFVDR LVQLMKAVQR ESGNRKKKTE RLQALLADNE KVNLCEIDPI PLPLEPSVRI
RGIVPDTATL FKSALMPAKL IFKAEDGAMY PVIFKHGDDL RQDQLILQII SLMDKLLRKE
NLDLKLTPYK VLATSTKHGF MQFVQSVPVA EVLATEGNIQ SFFRKHAPSE KGPYGISPEV
MDTYVKSCAG YCVITYILGV GDRHLDNLLL TKTGKLFHID FGYILGRDPK PLPPPMKLSK
EMVEGMGGMQ SEQYQEFRKQ CYTAFLHLRR YSNLILNLFS LMVDANIPDI ALEPDKTVKK
VQDKFRLDLS DEEAVHYMQS LIDESVGALF AAVVEQIHKF AQYWRR
//
