Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha

Sequence or UniProt identifier

>sp|Q5RAY1|P3C2A_PONAB Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha OS=Pongo abelii GN=PIK3C2A PE=2 SV=1 MAQISSNSGFKECPSSHPEPTRAKDVDKEEALQMEAEALAKLQKDRQVTDNQRGFELSSS TRKKAQVYNKQDYDLMVFPESDSQKRALDIDVEKLTQAELEKLLLDDSLETRKTPVLPVT PILSPSFSAQLYFRPTIQRGQWPPGLSGPSTYALPSIYPSTYSKQAAFQNGFNPRMPTFP STEPIYLSLPGQSPYFSYPLTPATPFHPQGSLPIYRPVVSPDMAKLFDKIASTSEFLKNG KARADLEITDSKVSNLQVSPKSEDISKFDWLDLDPLSKPKVDNVEVLDHEEEKNVSSLLA KDPWDAVLLEERSTANCHLERKMNGKSLSVATVTRSQSLNIRTTQLAKAHISQKDPNGTS SLPTGSSLLQEVEVQNEEMAAFSRSITKLKTKFPYTNHHTNPGYLLSPVTAQRNICGENA SVKVSIDIEGFQLPVTFTCDVSSTVEIIIMQALCWVHDDLNQVDVGSYVLKVCGQEEVLQ NNHCLGSHEHIQNCRKWDTEIRLQLLTFSAMCQNLARTAEDDETPVDLNKHLYQIEKPYK EAMTRHPVEELLDSYHNQVELALQIENQHRAVDQVIKAVRKICSALDGVETLAITESVKK LKRAVNLPRSKTADVASLFGGEDTSKSSTRGSLNPENPVQVSINQLTAAIYDLLRLHANS GRSPTDCAQSSKSVKEAWTTTEQLQFTIFAAHGISSNWVSNYEKYYLICSLSHNGKDLFK PIQSKKVGTYKNFFYLIKWDELIIFPIQISQLPLESLLHLTLFGILNQSSGSSPDSNKQR KGPEALGKVSLPLFDFKRFLTCGTKLLYLWTSSHTNSVPGAVTKKGYVMERIVLQVDFPS PAFDIIYTTPQVDRSIIQQHNLETLENDVKGKLLDILHKDSSLGLSKEDKAFLWEKRYYC FKHPNCLPKILASAPNWKWVNLAKTYSLLHQWPALYPLIALELLDSKFADQEVRSLAVTW IEAISDDELTDLLPQFVQALKYEIYLNSSLVQFLLSRALGNIQIAHNLYWLLKDALHDVQ FSTRYEHVLGALLSVGGKRLREELRKQTKLVQLLGGVAEKVRQASGSARQVVLQRSMERV QSFFQKNKCRLPLKPSLVAKELSIKSCSFFSSNAVPLKVTMVNADPMGEEINVMFKVGED LRQDMLALQMIKIMDKIWLKEGLDLRMVIFKCLSTGRDRGMVELVPASDTLRKIQVEYGV TGSFKDKPLAEWLRKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRSTG HMFHIDFGKFLGHAQMFGTFKRDRAPFVLTSDMAYVINGGEKPTIRFQLFVDLCCQAYNL IRKQTNLFLNLLSLMIPSGLPELTSIQDLKYVRDALQPQTTDAEATIFFTRLIESSLGSI ATKFNFLIHNLAQLRFSGLPSNDEPILSFSPKTYSFKQDGRIKEVSVFTYHKKYNPDKHY IYVVRILREGQIEPSFVFRTFDEFQELHNKLSIIFPLWKLPGFPNRMVLGRTHIKDVAAK RKIELNSYLQSLMNASTDVAECDLVCTFFHPLLRDEKAEGIARSADAGSFSPPTPGQIGG AVKLSISYRNGTLFIMVMHTKDLVTEDGADPNPYVKTYLLPDNHKTSKRKTKISRKTRNP TFNEMLVYSGYSKETLRQRELQLSVLSAESLRENFFLGGVTLPLKDFNLSKETVKWYQLT AATYL

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Q5RAY1 (P3C2A_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 65. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	1685 AA.
Sequence status	Complete.
Protein existence	Evidence 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 vesicle › clathrin-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.

Ontologies

Keywords
Biological process	Endocytosis Exocytosis
Cellular component	Cell membrane Cytoplasm Cytoplasmic vesicle Golgi apparatus Membrane Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endocytosis Inferred from sequence or structural similarity. Source: UniProtKB exocytosis Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol-mediated signaling Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell clathrin-coated vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB vesicle Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	1-phosphatidylinositol-4-phosphate 3-kinase activity Inferred from electronic annotation. Source: EC ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1685

1685

Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha

PRO_0000088797

Regions

Domain

419 – 507

PI3K-RBD

Domain

680 – 839

160

C2 PI3K-type

Domain

859 – 1035

177

PIK helical

Domain

1131 – 1395

265

PI3K/PI4K

Domain

1420 – 1536

117

Domain

1558 – 1661

104

Region

1 – 142

142

Interaction with clathrin; sufficient to induce clathrin assemby By similarity

Region

1486 – 1491

Interaction with PtdIns(4,5)P2-containing membranes By similarity

Motif

1607 – 1618

Nuclear localization signal By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

108

Phosphoserine By similarity

Modified residue

259

Phosphoserine By similarity

Modified residue

327

Phosphoserine By similarity

Modified residue

338

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q5RAY1 [UniParc].

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

FASTA

1,685

190,466

        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.
RefSeq	NP_001125626.1. NM_001132154.1.
UniGene	Pab.799.
3D structure databases
ProteinModelPortal	Q5RAY1.
SMR	Q5RAY1. Positions 1419-1530, 1560-1681.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100457125.
KEGG	pon:100457125.
Organism-specific databases
CTD	5286.
Phylogenomic databases
HOVERGEN	HBG082099.
InParanoid	Q5RAY1.
KO	K00923.
Family and domain databases
Gene3D	1.10.1070.11. 1 hit. 1.25.40.70. 1 hit. 3.30.1520.10. 1 hit.
InterPro	IPR016024. ARM-type_fold. IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. 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. [Graphical view]
PANTHER	PTHR10048. PTHR10048. 1 hit.
Pfam	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]
SMART	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]
SUPFAM	SSF48371. ARM-type_fold. 1 hit. SSF49562. C2_CaLB. 2 hits. SSF56112. Kinase_like. 1 hit. SSF64268. PX. 1 hit.
PROSITE	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]
ProtoNet	Search...

Entry information

Entry name

P3C2A_PONAB

Accession

Primary (citable) accession number: Q5RAY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	December 21, 2004
Last modified:	March 6, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents