Q5RAY1

PR
Gene name
PIK3C2A
Protein name
Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
Names
PI3K-C2-alpha, PtdIns-3-kinase C2 subunit alpha, Phosphoinositide 3-kinase-C2-alpha
Species
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
KEGG Pathway
pon:100457125
EC number
2.7.1.137: Phosphotransferases with an alcohol group as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-52 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

1266-1290 (Activation loop from InterPro)

Target domain

1041-1393 (Catalytic domain of Class II Phosphoinositide 3-kinase alpha)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for Q5RAY1

Entry ID Method Resolution Chain Position Source
AF-Q5RAY1-F1 Predicted AlphaFoldDB

No variants for Q5RAY1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5RAY1

No associated diseases with Q5RAY1

11 regional properties for Q5RAY1

Type Name Position InterPro Accession
domain C2 domain 683 - 805 IPR000008-1
domain C2 domain 1554 - 1679 IPR000008-2
domain Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain 407 - 510 IPR000341
domain Phosphatidylinositol 3-/4-kinase, catalytic domain 1103 - 1394 IPR000403
domain Phosphoinositide 3-kinase, accessory (PIK) domain 859 - 1045 IPR001263
domain Phox homology 1420 - 1536 IPR001683
domain C2 phosphatidylinositol 3-kinase-type domain 672 - 839 IPR002420
conserved_site Phosphatidylinositol 3/4-kinase, conserved site 1135 - 1149 IPR018936-1
conserved_site Phosphatidylinositol 3/4-kinase, conserved site 1233 - 1253 IPR018936-2
domain PI3K-C2-alpha, catalytic domain 1041 - 1393 IPR037705
domain Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha, PX domain 1424 - 1532 IPR042133

Functions

Description
EC Number 2.7.1.137 Phosphotransferases with an alcohol group as acceptor
Subcellular Localization
  • Cell membrane
  • Cytoplasmic vesicle, clathrin-coated vesicle
  • Nucleus
  • Cytoplasm
  • Golgi apparatus, trans-Golgi network
  • Inserts preferentially into membranes containing PtdIns(4,5)P2
  • Associated with RNA-containing structures
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
clathrin-coated vesicle A vesicle with a coat formed of clathrin connected to the membrane via one of the clathrin adaptor complexes.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
trans-Golgi network The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
vesicle Any small, fluid-filled, spherical organelle enclosed by membrane.

7 GO annotations of molecular function

Name Definition
1-phosphatidylinositol-3-kinase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol + ATP = a 1-phosphatidyl-1D-myo-inositol 3-phosphate + ADP + 2 H(+).
1-phosphatidylinositol-4-phosphate 3-kinase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4-phosphate + ATP = 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + ADP + 2 H(+).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
clathrin binding Binding to a clathrin heavy or light chain, the main components of the coat of coated vesicles and coated pits, and which also occurs in synaptic vesicles.
phosphatidylinositol binding Binding to an inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives.
phosphatidylinositol-3,4-bisphosphate 5-kinase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + ATP = a 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + ADP + 2 H(+).
phosphatidylinositol-4,5-bisphosphate 3-kinase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + ATP = a 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + ADP + 2 H(+).

4 GO annotations of biological process

Name Definition
endocytosis A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
exocytosis A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell.
phosphatidylinositol-mediated signaling The series of molecular signals in which a cell uses a phosphatidylinositol-mediated signaling to convert a signal into a response. Phosphatidylinositols include phosphatidylinositol (PtdIns) and its phosphorylated derivatives.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAQISSNSGF KECPSSHPEP TRAKDVDKEE ALQMEAEALA KLQKDRQVTD NQRGFELSSS
70 80 90 100 110 120
TRKKAQVYNK QDYDLMVFPE SDSQKRALDI DVEKLTQAEL EKLLLDDSLE TRKTPVLPVT
130 140 150 160 170 180
PILSPSFSAQ LYFRPTIQRG QWPPGLSGPS TYALPSIYPS TYSKQAAFQN GFNPRMPTFP
190 200 210 220 230 240
STEPIYLSLP GQSPYFSYPL TPATPFHPQG SLPIYRPVVS PDMAKLFDKI ASTSEFLKNG
250 260 270 280 290 300
KARADLEITD SKVSNLQVSP KSEDISKFDW LDLDPLSKPK VDNVEVLDHE EEKNVSSLLA
310 320 330 340 350 360
KDPWDAVLLE ERSTANCHLE RKMNGKSLSV ATVTRSQSLN IRTTQLAKAH ISQKDPNGTS
370 380 390 400 410 420
SLPTGSSLLQ EVEVQNEEMA AFSRSITKLK TKFPYTNHHT NPGYLLSPVT AQRNICGENA
430 440 450 460 470 480
SVKVSIDIEG FQLPVTFTCD VSSTVEIIIM QALCWVHDDL NQVDVGSYVL KVCGQEEVLQ
490 500 510 520 530 540
NNHCLGSHEH IQNCRKWDTE IRLQLLTFSA MCQNLARTAE DDETPVDLNK HLYQIEKPYK
550 560 570 580 590 600
EAMTRHPVEE LLDSYHNQVE LALQIENQHR AVDQVIKAVR KICSALDGVE TLAITESVKK
610 620 630 640 650 660
LKRAVNLPRS KTADVASLFG GEDTSKSSTR GSLNPENPVQ VSINQLTAAI YDLLRLHANS
670 680 690 700 710 720
GRSPTDCAQS SKSVKEAWTT TEQLQFTIFA AHGISSNWVS NYEKYYLICS LSHNGKDLFK
730 740 750 760 770 780
PIQSKKVGTY KNFFYLIKWD ELIIFPIQIS QLPLESLLHL TLFGILNQSS GSSPDSNKQR
790 800 810 820 830 840
KGPEALGKVS LPLFDFKRFL TCGTKLLYLW TSSHTNSVPG AVTKKGYVME RIVLQVDFPS
850 860 870 880 890 900
PAFDIIYTTP QVDRSIIQQH NLETLENDVK GKLLDILHKD SSLGLSKEDK AFLWEKRYYC
910 920 930 940 950 960
FKHPNCLPKI LASAPNWKWV NLAKTYSLLH QWPALYPLIA LELLDSKFAD QEVRSLAVTW
970 980 990 1000 1010 1020
IEAISDDELT DLLPQFVQAL KYEIYLNSSL VQFLLSRALG NIQIAHNLYW LLKDALHDVQ
1030 1040 1050 1060 1070 1080
FSTRYEHVLG ALLSVGGKRL REELRKQTKL VQLLGGVAEK VRQASGSARQ VVLQRSMERV
1090 1100 1110 1120 1130 1140
QSFFQKNKCR LPLKPSLVAK ELSIKSCSFF SSNAVPLKVT MVNADPMGEE INVMFKVGED
1150 1160 1170 1180 1190 1200
LRQDMLALQM IKIMDKIWLK EGLDLRMVIF KCLSTGRDRG MVELVPASDT LRKIQVEYGV
1210 1220 1230 1240 1250 1260
TGSFKDKPLA EWLRKYNPSE EEYEKASENF IYSCAGCCVA TYVLGICDRH NDNIMLRSTG
1270 1280 1290 1300 1310 1320
HMFHIDFGKF LGHAQMFGTF KRDRAPFVLT SDMAYVINGG EKPTIRFQLF VDLCCQAYNL
1330 1340 1350 1360 1370 1380
IRKQTNLFLN LLSLMIPSGL PELTSIQDLK YVRDALQPQT TDAEATIFFT RLIESSLGSI
1390 1400 1410 1420 1430 1440
ATKFNFLIHN LAQLRFSGLP SNDEPILSFS PKTYSFKQDG RIKEVSVFTY HKKYNPDKHY
1450 1460 1470 1480 1490 1500
IYVVRILREG QIEPSFVFRT FDEFQELHNK LSIIFPLWKL PGFPNRMVLG RTHIKDVAAK
1510 1520 1530 1540 1550 1560
RKIELNSYLQ SLMNASTDVA ECDLVCTFFH PLLRDEKAEG IARSADAGSF SPPTPGQIGG
1570 1580 1590 1600 1610 1620
AVKLSISYRN GTLFIMVMHT KDLVTEDGAD PNPYVKTYLL PDNHKTSKRK TKISRKTRNP
1630 1640 1650 1660 1670 1680
TFNEMLVYSG YSKETLRQRE LQLSVLSAES LRENFFLGGV TLPLKDFNLS KETVKWYQLT
AATYL