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Q5RAY1

- P3C2A_PONAB

UniProt

Q5RAY1 - P3C2A_PONAB

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Protein
Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
Gene
PIK3C2A
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Calcium or magnesium. Manganese cannot be used By similarity.

Enzyme regulationi

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

GO - Molecular functioni

  1. 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW
  3. phosphatidylinositol binding Source: InterPro

GO - Biological processi

  1. endocytosis Source: UniProtKB
  2. exocytosis Source: UniProtKB-KW
  3. phosphatidylinositol-mediated signaling Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Endocytosis, Exocytosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha (EC:2.7.1.154)
Short name:
PI3K-C2-alpha
Short name:
PtdIns-3-kinase C2 subunit alpha
Alternative name(s):
Phosphoinositide 3-kinase-C2-alpha
Gene namesi
Name:PIK3C2A
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-SubCell
  2. clathrin-coated vesicle Source: UniProtKB-SubCell
  3. cytoplasm Source: UniProtKB
  4. nucleus Source: UniProtKB-SubCell
  5. plasma membrane Source: UniProtKB
  6. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 16851684Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
PRO_0000088797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei60 – 601Phosphoserine By similarity
Modified residuei108 – 1081Phosphoserine By similarity
Modified residuei259 – 2591Phosphoserine By similarity
Modified residuei327 – 3271Phosphoserine By similarity
Modified residuei338 – 3381Phosphoserine By similarity

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Phosphoprotein

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ5RAY1.
SMRiQ5RAY1. Positions 1419-1530, 1560-1681.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini419 – 50789PI3K-RBD
Add
BLAST
Domaini680 – 839160C2 PI3K-type
Add
BLAST
Domaini859 – 1035177PIK helical
Add
BLAST
Domaini1131 – 1395265PI3K/PI4K
Add
BLAST
Domaini1420 – 1536117PX
Add
BLAST
Domaini1558 – 1661104C2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 142141Interaction with clathrin; sufficient to induce clathrin assemby By similarity
Add
BLAST
Regioni1486 – 14916Interaction with PtdIns(4,5)P2-containing membranes By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1607 – 161812Nuclear localization signal By similarity
Add
BLAST

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.
Contains 1 C2 domain.
Contains 1 PI3K-RBD domain.
Contains 1 PI3K/PI4K domain.
Contains 1 PIK helical domain.

Phylogenomic databases

HOVERGENiHBG082099.
InParanoidiQ5RAY1.
KOiK00923.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 2 hits.
3.30.1520.10. 1 hit.
InterProiIPR016024. 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]
PANTHERiPTHR10048. PTHR10048. 1 hit.
PfamiPF00168. 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]
SMARTiSM00239. 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]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50004. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5RAY1-1 [UniParc]FASTAAdd to Basket

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MAQISSNSGF KECPSSHPEP TRAKDVDKEE ALQMEAEALA KLQKDRQVTD     50
NQRGFELSSS TRKKAQVYNK QDYDLMVFPE SDSQKRALDI DVEKLTQAEL 100
EKLLLDDSLE TRKTPVLPVT PILSPSFSAQ LYFRPTIQRG QWPPGLSGPS 150
TYALPSIYPS TYSKQAAFQN GFNPRMPTFP STEPIYLSLP GQSPYFSYPL 200
TPATPFHPQG SLPIYRPVVS PDMAKLFDKI ASTSEFLKNG KARADLEITD 250
SKVSNLQVSP KSEDISKFDW LDLDPLSKPK VDNVEVLDHE EEKNVSSLLA 300
KDPWDAVLLE ERSTANCHLE RKMNGKSLSV ATVTRSQSLN IRTTQLAKAH 350
ISQKDPNGTS SLPTGSSLLQ EVEVQNEEMA AFSRSITKLK TKFPYTNHHT 400
NPGYLLSPVT AQRNICGENA SVKVSIDIEG FQLPVTFTCD VSSTVEIIIM 450
QALCWVHDDL NQVDVGSYVL KVCGQEEVLQ NNHCLGSHEH IQNCRKWDTE 500
IRLQLLTFSA MCQNLARTAE DDETPVDLNK HLYQIEKPYK EAMTRHPVEE 550
LLDSYHNQVE LALQIENQHR AVDQVIKAVR KICSALDGVE TLAITESVKK 600
LKRAVNLPRS KTADVASLFG GEDTSKSSTR GSLNPENPVQ VSINQLTAAI 650
YDLLRLHANS GRSPTDCAQS SKSVKEAWTT TEQLQFTIFA AHGISSNWVS 700
NYEKYYLICS LSHNGKDLFK PIQSKKVGTY KNFFYLIKWD ELIIFPIQIS 750
QLPLESLLHL TLFGILNQSS GSSPDSNKQR KGPEALGKVS LPLFDFKRFL 800
TCGTKLLYLW TSSHTNSVPG AVTKKGYVME RIVLQVDFPS PAFDIIYTTP 850
QVDRSIIQQH NLETLENDVK GKLLDILHKD SSLGLSKEDK AFLWEKRYYC 900
FKHPNCLPKI LASAPNWKWV NLAKTYSLLH QWPALYPLIA LELLDSKFAD 950
QEVRSLAVTW IEAISDDELT DLLPQFVQAL KYEIYLNSSL VQFLLSRALG 1000
NIQIAHNLYW LLKDALHDVQ FSTRYEHVLG ALLSVGGKRL REELRKQTKL 1050
VQLLGGVAEK VRQASGSARQ VVLQRSMERV QSFFQKNKCR LPLKPSLVAK 1100
ELSIKSCSFF SSNAVPLKVT MVNADPMGEE INVMFKVGED LRQDMLALQM 1150
IKIMDKIWLK EGLDLRMVIF KCLSTGRDRG MVELVPASDT LRKIQVEYGV 1200
TGSFKDKPLA EWLRKYNPSE EEYEKASENF IYSCAGCCVA TYVLGICDRH 1250
NDNIMLRSTG HMFHIDFGKF LGHAQMFGTF KRDRAPFVLT SDMAYVINGG 1300
EKPTIRFQLF VDLCCQAYNL IRKQTNLFLN LLSLMIPSGL PELTSIQDLK 1350
YVRDALQPQT TDAEATIFFT RLIESSLGSI ATKFNFLIHN LAQLRFSGLP 1400
SNDEPILSFS PKTYSFKQDG RIKEVSVFTY HKKYNPDKHY IYVVRILREG 1450
QIEPSFVFRT FDEFQELHNK LSIIFPLWKL PGFPNRMVLG RTHIKDVAAK 1500
RKIELNSYLQ SLMNASTDVA ECDLVCTFFH PLLRDEKAEG IARSADAGSF 1550
SPPTPGQIGG AVKLSISYRN GTLFIMVMHT KDLVTEDGAD PNPYVKTYLL 1600
PDNHKTSKRK TKISRKTRNP TFNEMLVYSG YSKETLRQRE LQLSVLSAES 1650
LRENFFLGGV TLPLKDFNLS KETVKWYQLT AATYL 1685
Length:1,685
Mass (Da):190,466
Last modified:December 21, 2004 - v1
Checksum:i2C48ED378DE0C2BD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR858880 mRNA. Translation: CAH91079.1.
RefSeqiNP_001125626.1. NM_001132154.1.
UniGeneiPab.799.

Genome annotation databases

GeneIDi100457125.
KEGGipon:100457125.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR858880 mRNA. Translation: CAH91079.1 .
RefSeqi NP_001125626.1. NM_001132154.1.
UniGenei Pab.799.

3D structure databases

ProteinModelPortali Q5RAY1.
SMRi Q5RAY1. Positions 1419-1530, 1560-1681.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100457125.
KEGGi pon:100457125.

Organism-specific databases

CTDi 5286.

Phylogenomic databases

HOVERGENi HBG082099.
InParanoidi Q5RAY1.
KOi K00923.

Family and domain databases

Gene3Di 1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 2 hits.
3.30.1520.10. 1 hit.
InterProi IPR016024. 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 ]
PANTHERi PTHR10048. PTHR10048. 1 hit.
Pfami PF00168. 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 ]
SMARTi SM00239. 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 ]
SUPFAMi SSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEi PS50004. 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 ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiP3C2A_PONAB
AccessioniPrimary (citable) accession number: Q5RAY1
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi