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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).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).By similarity

Enzyme regulationi

Only slightly inhibited by wortmannin and LY294002. Activated by clathrin and insulin (By similarity).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. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. Golgi apparatus Source: UniProtKB-KW
  4. nucleus Source: UniProtKB-KW
  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 – 11RemovedBy similarity
Chaini2 – 16851684Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alphaPRO_0000088797Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Interactioni

Subunit structurei

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

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini419 – 50789PI3K-RBDPROSITE-ProRule annotationAdd
BLAST
Domaini680 – 839160C2 PI3K-typePROSITE-ProRule annotationAdd
BLAST
Domaini859 – 1035177PIK helicalPROSITE-ProRule annotationAdd
BLAST
Domaini1131 – 1395265PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini1420 – 1536117PXPROSITE-ProRule annotationAdd
BLAST
Domaini1558 – 1661104C2PROSITE-ProRule annotationAdd
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1607 – 161812Nuclear localization signalBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation
Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 C2 PI3K-type domain.PROSITE-ProRule annotation
Contains 1 PI3K-RBD domain.PROSITE-ProRule annotation
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 1 PIK helical domain.PROSITE-ProRule annotation
Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQISSNSGF KECPSSHPEP TRAKDVDKEE ALQMEAEALA KLQKDRQVTD
60 70 80 90 100
NQRGFELSSS TRKKAQVYNK QDYDLMVFPE SDSQKRALDI DVEKLTQAEL
110 120 130 140 150
EKLLLDDSLE TRKTPVLPVT PILSPSFSAQ LYFRPTIQRG QWPPGLSGPS
160 170 180 190 200
TYALPSIYPS TYSKQAAFQN GFNPRMPTFP STEPIYLSLP GQSPYFSYPL
210 220 230 240 250
TPATPFHPQG SLPIYRPVVS PDMAKLFDKI ASTSEFLKNG KARADLEITD
260 270 280 290 300
SKVSNLQVSP KSEDISKFDW LDLDPLSKPK VDNVEVLDHE EEKNVSSLLA
310 320 330 340 350
KDPWDAVLLE ERSTANCHLE RKMNGKSLSV ATVTRSQSLN IRTTQLAKAH
360 370 380 390 400
ISQKDPNGTS SLPTGSSLLQ EVEVQNEEMA AFSRSITKLK TKFPYTNHHT
410 420 430 440 450
NPGYLLSPVT AQRNICGENA SVKVSIDIEG FQLPVTFTCD VSSTVEIIIM
460 470 480 490 500
QALCWVHDDL NQVDVGSYVL KVCGQEEVLQ NNHCLGSHEH IQNCRKWDTE
510 520 530 540 550
IRLQLLTFSA MCQNLARTAE DDETPVDLNK HLYQIEKPYK EAMTRHPVEE
560 570 580 590 600
LLDSYHNQVE LALQIENQHR AVDQVIKAVR KICSALDGVE TLAITESVKK
610 620 630 640 650
LKRAVNLPRS KTADVASLFG GEDTSKSSTR GSLNPENPVQ VSINQLTAAI
660 670 680 690 700
YDLLRLHANS GRSPTDCAQS SKSVKEAWTT TEQLQFTIFA AHGISSNWVS
710 720 730 740 750
NYEKYYLICS LSHNGKDLFK PIQSKKVGTY KNFFYLIKWD ELIIFPIQIS
760 770 780 790 800
QLPLESLLHL TLFGILNQSS GSSPDSNKQR KGPEALGKVS LPLFDFKRFL
810 820 830 840 850
TCGTKLLYLW TSSHTNSVPG AVTKKGYVME RIVLQVDFPS PAFDIIYTTP
860 870 880 890 900
QVDRSIIQQH NLETLENDVK GKLLDILHKD SSLGLSKEDK AFLWEKRYYC
910 920 930 940 950
FKHPNCLPKI LASAPNWKWV NLAKTYSLLH QWPALYPLIA LELLDSKFAD
960 970 980 990 1000
QEVRSLAVTW IEAISDDELT DLLPQFVQAL KYEIYLNSSL VQFLLSRALG
1010 1020 1030 1040 1050
NIQIAHNLYW LLKDALHDVQ FSTRYEHVLG ALLSVGGKRL REELRKQTKL
1060 1070 1080 1090 1100
VQLLGGVAEK VRQASGSARQ VVLQRSMERV QSFFQKNKCR LPLKPSLVAK
1110 1120 1130 1140 1150
ELSIKSCSFF SSNAVPLKVT MVNADPMGEE INVMFKVGED LRQDMLALQM
1160 1170 1180 1190 1200
IKIMDKIWLK EGLDLRMVIF KCLSTGRDRG MVELVPASDT LRKIQVEYGV
1210 1220 1230 1240 1250
TGSFKDKPLA EWLRKYNPSE EEYEKASENF IYSCAGCCVA TYVLGICDRH
1260 1270 1280 1290 1300
NDNIMLRSTG HMFHIDFGKF LGHAQMFGTF KRDRAPFVLT SDMAYVINGG
1310 1320 1330 1340 1350
EKPTIRFQLF VDLCCQAYNL IRKQTNLFLN LLSLMIPSGL PELTSIQDLK
1360 1370 1380 1390 1400
YVRDALQPQT TDAEATIFFT RLIESSLGSI ATKFNFLIHN LAQLRFSGLP
1410 1420 1430 1440 1450
SNDEPILSFS PKTYSFKQDG RIKEVSVFTY HKKYNPDKHY IYVVRILREG
1460 1470 1480 1490 1500
QIEPSFVFRT FDEFQELHNK LSIIFPLWKL PGFPNRMVLG RTHIKDVAAK
1510 1520 1530 1540 1550
RKIELNSYLQ SLMNASTDVA ECDLVCTFFH PLLRDEKAEG IARSADAGSF
1560 1570 1580 1590 1600
SPPTPGQIGG AVKLSISYRN GTLFIMVMHT KDLVTEDGAD PNPYVKTYLL
1610 1620 1630 1640 1650
PDNHKTSKRK TKISRKTRNP TFNEMLVYSG YSKETLRQRE LQLSVLSAES
1660 1670 1680
LRENFFLGGV TLPLKDFNLS KETVKWYQLT AATYL
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: October 29, 2014
This is version 71 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