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Q5RAY1 (P3C2A_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha

Short name=PI3K-C2-alpha
Short name=PtdIns-3-kinase C2 subunit alpha
EC=2.7.1.154
Alternative name(s):
Phosphoinositide 3-kinase-C2-alpha
Gene names
Name:PIK3C2A
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length1685 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane and glucose uptake in response to insulin-mediated RHOQ activation. Regulates insulin secretion through two different mechanisms: involved in glucose-induced insulin secretion downstream of insulin receptor in a pathway that involves AKT1 activation and TBC1D4/AS160 phosphorylation, and participates in the late step of insulin granule exocytosis probably in insulin granule fusion. Synthesizes PtdIns3P in response to insulin signaling. Functions in clathrin-coated endocytic vesicle formation and distribution. Regulates dynamin-independent endocytosis, probably by recruiting EEA1 to internalizing vesicles. In neurosecretory cells synthesizes PtdIns3P on large dense core vesicles. Participates in calcium induced contraction of vascular smooth muscle by regulating myosin light chain (MLC) phosphorylation through a mechanism involving Rho kinase-dependent phosphorylation of the MLCP-regulatory subunit MYPT1. May play a role in the EGF signaling cascade. May be involved in mitosis and UV-induced damage response. Required for maintenance of normal renal structure and function by supporting normal podocyte function By similarity.

Catalytic activity

ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate.

Cofactor

Calcium or magnesium. Manganese cannot be used By similarity.

Enzyme regulation

Only slightly inhibited by wortmannin and LY294002. Activated by clathrin and insulin By similarity.

Subunit structure

Part of a complex with ERBB2 and EGFR. Interacts with clathrin trimers By similarity.

Subcellular location

Cell membrane. Golgi apparatus. Cytoplasmic vesicleclathrin-coated vesicle. Nucleus. Cytoplasm By similarity.

Post-translational modification

Phosphorylated on Ser-259 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation. Phosphorylated upon insulin stimulation; which may lead to enzyme activation By similarity.

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 C2 domain.

Contains 1 C2 PI3K-type domain.

Contains 1 PI3K-RBD domain.

Contains 1 PI3K/PI4K domain.

Contains 1 PIK helical domain.

Contains 1 PX (phox homology) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 16851684Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
PRO_0000088797

Regions

Domain419 – 50789PI3K-RBD
Domain680 – 839160C2 PI3K-type
Domain859 – 1035177PIK helical
Domain1131 – 1395265PI3K/PI4K
Domain1420 – 1536117PX
Domain1558 – 1661104C2
Region2 – 142141Interaction with clathrin; sufficient to induce clathrin assemby By similarity
Region1486 – 14916Interaction with PtdIns(4,5)P2-containing membranes By similarity
Motif1607 – 161812Nuclear localization signal By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue601Phosphoserine By similarity
Modified residue1081Phosphoserine By similarity
Modified residue2591Phosphoserine By similarity
Modified residue3271Phosphoserine By similarity
Modified residue3381Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RAY1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 2C48ED378DE0C2BD

FASTA1,685190,466
        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 

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858880 mRNA. Translation: CAH91079.1.
RefSeqNP_001125626.1. NM_001132154.1.
UniGenePab.799.

3D structure databases

ProteinModelPortalQ5RAY1.
SMRQ5RAY1. Positions 1419-1530, 1560-1681.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100457125.
KEGGpon:100457125.

Organism-specific databases

CTD5286.

Phylogenomic databases

HOVERGENHBG082099.
InParanoidQ5RAY1.
KOK00923.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 2 hits.
3.30.1520.10. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR001683. Phox.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR002420. PI3K_C2_dom.
IPR000341. PI3K_Ras-bd_dom.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERPTHR10048. PTHR10048. 1 hit.
PfamPF00168. C2. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
PF00787. PX. 1 hit.
[Graphical view]
SMARTSM00239. C2. 2 hits.
SM00142. PI3K_C2. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
SM00312. PX. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
PS50195. PX. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameP3C2A_PONAB
AccessionPrimary (citable) accession number: Q5RAY1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: December 21, 2004
Last modified: June 11, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families