Q61194 (P3C2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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):
Cpk-m
Phosphoinositide 3-kinase-C2-alpha
p170

Gene names

Name:	Pik3c2a
Synonyms:	Cpk

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1686 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. Ref.3 Ref.7 Ref.8
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	Activated by clathrin By similarity. Only slightly inhibited by wortmannin and LY294002. Activated by insulin. Ref.3 Ref.4
Subunit structure	Interacts with ERBB2 and EGFR. Interacts with clathrin trimers By similarity. Ref.9
Subcellular location	Cell membrane. Golgi apparatus. Cytoplasmic vesicle › clathrin-coated vesicle. Nucleus. Cytoplasm By similarity. Note: Has a preference for membranes containing PtdIns(4,5)P2 or PtdIns(3,4)P2.
Tissue specificity	Detected in podocytes. Ref.8
Post-translational modification	Phosphorylated on Ser-261 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation By similarity. Phosphorylated upon insulin stimulation; which may lead to enzyme activation. Ref.4
Disruption phenotype	Chronic renal failure and kidney lesions. Affects podocyte morphology and function. Ref.8
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 caution	The sequence AAB07682.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Endocytosis Exocytosis
Cellular component	Cell membrane Cytoplasm Cytoplasmic vesicle Golgi apparatus Membrane Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure 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 nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell phosphatidylinositol 3-kinase complex Inferred from Biological aspect of Ancestor. Source: RefGenome plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB vesicle Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	1-phosphatidylinositol-3-kinase activity Inferred from direct assay Ref.3. Source: MGI 1-phosphatidylinositol-4-phosphate 3-kinase activity Inferred from Biological aspect of Ancestor. Source: RefGenome ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q61194-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q61194-2)

The sequence of this isoform differs from the canonical sequence as follows:
     276-303: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1686

1686

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

PRO_0000088796

Regions

Domain

422 – 510

89

PI3K-RBD

Domain

682 – 841

160

C2 PI3K-type

Domain

861 – 1037

177

PIK helical

Domain

1133 – 1395

263

PI3K/PI4K

Domain

1420 – 1536

117

PX

Domain

1557 – 1660

104

C2

Region

1 – 142

142

Interaction with clathrin; sufficient to induce clathrin assemby By similarity

Region

1488 – 1493

6

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

Motif

1606 – 1617

12

Nuclear localization signal By similarity

Amino acid modifications

Modified residue

60

1

Phosphoserine By similarity

Modified residue

261

1

Phosphoserine Ref.5 Ref.6

Modified residue

328

1

Phosphoserine By similarity

Modified residue

339

1

Phosphoserine By similarity

Natural variations

Alternative sequence

276 – 303

28

Missing in isoform 2.

VSP_015254

Experimental info

Sequence conflict

140

1

G → V in AK049609. Ref.2

Sequence conflict

668

1

A → G in AAC52604. Ref.1

Sequence conflict

954

1

E → G in AAC52604. Ref.1

Sequence conflict

1206 – 1208

3

FKD → LR Ref.3

Sequence conflict

1211 – 1212

2

LA → TS Ref.3

Sequence conflict

1218

1

Y → N in AAB07682. Ref.3

Sequence conflict

1325 – 1326

2

KQ → T in AAB07682. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1686

Helix Strand Turn

Details...

Beta strand

1562 – 1570

9

Beta strand

1573 – 1582

10

Beta strand

1594 – 1602

9

Beta strand

1604 – 1606

3

Beta strand

1622 – 1631

10

Helix

1634 – 1637

4

Beta strand

1641 – 1648

8

Beta strand

1651 – 1653

3

Beta strand

1656 – 1664

9

Helix

1665 – 1667

3

Beta strand

1674 – 1679

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: E390BA7D730F4F87	FASTA	1,686	190,758
	10 20 30 40 50 60 MAQISNNSEF KQCSSSHPEP IRTKDVNKAE ALQMEAEALA KLQKDRQMTD SPRGFELSSS 70 80 90 100 110 120 TRQRTQGFNK QDYDLMVFPE LDSQKRAVDI DVEKLTQAEL EKILLDDNFE TRKPPALPVT 130 140 150 160 170 180 PVLSPSFSTQ LYLRPSGQRG QWPPGLCGPS TYTLPSTYPS AYSKQATFQN GFSPRMPTFP 190 200 210 220 230 240 STESVYLRLP GQSPYFSYPL TPATPFHPQG SLPVYRPLVS PDMAKLFEKI ASTSEFLKNG 250 260 270 280 290 300 KARTDLEIAN SKASVCNLQI SPKSEDINKF DWLDLDPLSK PKVDYVEVLE HEEEKKDPVL 310 320 330 340 350 360 LAEDPWDAVL LEERSPSCHL ERKVNGKSLS GATVTRSQSL IIRTAQFTKA QGQVSQKDPN 370 380 390 400 410 420 GTSSLPTGSS LLQEFEVQND EVAAFCQSIM KLKTKFPYTD HCTNPGYLLS PVTVQRNMCG 430 440 450 460 470 480 ENASVKVSIE IEGLQLPVTF TCDVSSTVEI IIMQALCWVH DDLNQVDVGS YILKVCGQEE 490 500 510 520 530 540 VLQNNHCLGS HEHIQNCRKW DTEIKLQLLT LSAMCQNLAR TAEDDEAPVD LNKYLYQIEK 550 560 570 580 590 600 PYKEVMTRHP VEELLDSYHY QVELALQTEN QHRAVDQVIK AVRKICSALD GVETPSVTEA 610 620 630 640 650 660 VKKLKRAVNL PRNKSADVTS LSGSDTRKNS TKGSLNPENP VQVSMDHLTT AIYDLLRLHA 670 680 690 700 710 720 NSSRCSTACP RGSRNIKEAW TATEQLQFTV YAAHGISSNW VSNYEKYYLI CSLSHNGKDL 730 740 750 760 770 780 FKPIQSKKVG TYKNFFYLIK WDELIIFPIQ ISQLPLESVL HLTLFGVLNQ SSGSSPDSNK 790 800 810 820 830 840 QRKGPEALGK VSLTLFDFKR FLTCGTKLLY LWTSSHTNSI PGAIPKKSYV MERIVLQVDF 850 860 870 880 890 900 PSPAFDIIYT SPQIDRNIIQ QDKLETLESD IKGKLLDIIH RDSSFGLSKE DKVFLWENRY 910 920 930 940 950 960 YCLKHPNCLP KILASAPNWK WANLAKTYSL LHQWPPLCPL AALELLDAKF ADQEVRSLAV 970 980 990 1000 1010 1020 SWMEAISDDE LADLLPQFVQ ALKYEIYLNS SLVRFLLSRA LGNIQIAHSL YWLLKDALHD 1030 1040 1050 1060 1070 1080 THFGSRYEHV LGALLSVGGK GLREELSKQM KLVQLLGGVA EKVRQASGST RQVVLQKSME 1090 1100 1110 1120 1130 1140 RVQSFFLRNK CRLPLKPSLV AKELNIKSCS FFSSNAMPLK VTMVNADPLG EEINVMFKVG 1150 1160 1170 1180 1190 1200 EDLRQDMLAL QMIKIMDKIW LKEGLDLRMV IFRCLSTGRD RGMVELVPAS DTLRKIQVEY 1210 1220 1230 1240 1250 1260 GVTGSFKDKP LAEWLRKYNP SEEEYEKASE NFIYSCAGCC VATYVLGICD RHNDNIMLRS 1270 1280 1290 1300 1310 1320 TGHMFHIDFG KFLGHAQMFG SFKRDRAPFV LTSDMAYVIN GGEKPTIRFQ LFVDLCCQAY 1330 1340 1350 1360 1370 1380 NLIRKQTNLF LNLLSLMIPS GLPELTSIQD LKYVRDALQP QTTDAEATIF FTRLIESSLG 1390 1400 1410 1420 1430 1440 SIATKFNFFI HNLAQLRFSG LPSNDEPILS FSPKTYSFRQ DGRIKEVSVF TYHKKYNPDK 1450 1460 1470 1480 1490 1500 HYIYVVRILR EGHLEPSFVF RTFDEFQELH NKLSIIFPLW KLPGFPNRMV LGRTHIKDVA 1510 1520 1530 1540 1550 1560 AKRKIELNSY LQSLMNASTD VAECDLVCTF FHPLLRDEKA EGIARSAGAV PFSPTLGQIG 1570 1580 1590 1600 1610 1620 GAVKLSVSYR NGTLFIMVMH IKDLVTEDGA DPNPYVKTYL LPDTHKTSKR KTKISRKTRN 1630 1640 1650 1660 1670 1680 PTFNEMLVYS GYSKETLRQR ELQLSVLSAE SLRENFFLGG ITLPLKDFNL SKETVKWYQL TAATYL
	Isoform 2 [UniParc]. Checksum: 4D18EBC1DDC2A57D	FASTA	1,658	187,526
	10 20 30 40 50 60 MAQISNNSEF KQCSSSHPEP IRTKDVNKAE ALQMEAEALA KLQKDRQMTD SPRGFELSSS 70 80 90 100 110 120 TRQRTQGFNK QDYDLMVFPE LDSQKRAVDI DVEKLTQAEL EKILLDDNFE TRKPPALPVT 130 140 150 160 170 180 PVLSPSFSTQ LYLRPSGQRG QWPPGLCGPS TYTLPSTYPS AYSKQATFQN GFSPRMPTFP 190 200 210 220 230 240 STESVYLRLP GQSPYFSYPL TPATPFHPQG SLPVYRPLVS PDMAKLFEKI ASTSEFLKNG 250 260 270 280 290 300 KARTDLEIAN SKASVCNLQI SPKSEDINKF DWLDLDPWDA VLLEERSPSC HLERKVNGKS 310 320 330 340 350 360 LSGATVTRSQ SLIIRTAQFT KAQGQVSQKD PNGTSSLPTG SSLLQEFEVQ NDEVAAFCQS 370 380 390 400 410 420 IMKLKTKFPY TDHCTNPGYL LSPVTVQRNM CGENASVKVS IEIEGLQLPV TFTCDVSSTV 430 440 450 460 470 480 EIIIMQALCW VHDDLNQVDV GSYILKVCGQ EEVLQNNHCL GSHEHIQNCR KWDTEIKLQL 490 500 510 520 530 540 LTLSAMCQNL ARTAEDDEAP VDLNKYLYQI EKPYKEVMTR HPVEELLDSY HYQVELALQT 550 560 570 580 590 600 ENQHRAVDQV IKAVRKICSA LDGVETPSVT EAVKKLKRAV NLPRNKSADV TSLSGSDTRK 610 620 630 640 650 660 NSTKGSLNPE NPVQVSMDHL TTAIYDLLRL HANSSRCSTA CPRGSRNIKE AWTATEQLQF 670 680 690 700 710 720 TVYAAHGISS NWVSNYEKYY LICSLSHNGK DLFKPIQSKK VGTYKNFFYL IKWDELIIFP 730 740 750 760 770 780 IQISQLPLES VLHLTLFGVL NQSSGSSPDS NKQRKGPEAL GKVSLTLFDF KRFLTCGTKL 790 800 810 820 830 840 LYLWTSSHTN SIPGAIPKKS YVMERIVLQV DFPSPAFDII YTSPQIDRNI IQQDKLETLE 850 860 870 880 890 900 SDIKGKLLDI IHRDSSFGLS KEDKVFLWEN RYYCLKHPNC LPKILASAPN WKWANLAKTY 910 920 930 940 950 960 SLLHQWPPLC PLAALELLDA KFADQEVRSL AVSWMEAISD DELADLLPQF VQALKYEIYL 970 980 990 1000 1010 1020 NSSLVRFLLS RALGNIQIAH SLYWLLKDAL HDTHFGSRYE HVLGALLSVG GKGLREELSK 1030 1040 1050 1060 1070 1080 QMKLVQLLGG VAEKVRQASG STRQVVLQKS MERVQSFFLR NKCRLPLKPS LVAKELNIKS 1090 1100 1110 1120 1130 1140 CSFFSSNAMP LKVTMVNADP LGEEINVMFK VGEDLRQDML ALQMIKIMDK IWLKEGLDLR 1150 1160 1170 1180 1190 1200 MVIFRCLSTG RDRGMVELVP ASDTLRKIQV EYGVTGSFKD KPLAEWLRKY NPSEEEYEKA 1210 1220 1230 1240 1250 1260 SENFIYSCAG CCVATYVLGI CDRHNDNIML RSTGHMFHID FGKFLGHAQM FGSFKRDRAP 1270 1280 1290 1300 1310 1320 FVLTSDMAYV INGGEKPTIR FQLFVDLCCQ AYNLIRKQTN LFLNLLSLMI PSGLPELTSI 1330 1340 1350 1360 1370 1380 QDLKYVRDAL QPQTTDAEAT IFFTRLIESS LGSIATKFNF FIHNLAQLRF SGLPSNDEPI 1390 1400 1410 1420 1430 1440 LSFSPKTYSF RQDGRIKEVS VFTYHKKYNP DKHYIYVVRI LREGHLEPSF VFRTFDEFQE 1450 1460 1470 1480 1490 1500 LHNKLSIIFP LWKLPGFPNR MVLGRTHIKD VAAKRKIELN SYLQSLMNAS TDVAECDLVC 1510 1520 1530 1540 1550 1560 TFFHPLLRDE KAEGIARSAG AVPFSPTLGQ IGGAVKLSVS YRNGTLFIMV MHIKDLVTED 1570 1580 1590 1600 1610 1620 GADPNPYVKT YLLPDTHKTS KRKTKISRKT RNPTFNEMLV YSGYSKETLR QRELQLSVLS 1630 1640 1650 AESLRENFFL GGITLPLKDF NLSKETVKWY QLTAATYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cpk is a novel class of Drosophila PtdIns 3-kinase containing a C2 domain." Molz L., Chen Y.-W., Hirano M., Williams L.T. J. Biol. Chem. 271:13892-13899(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: BALB/c.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-356 (ISOFORM 1). Tissue: Embryonic spinal cord.
[3]	"Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain." Virbasius J.V., Guilherme A., Czech M.P. J. Biol. Chem. 271:13304-13307(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 157-1686 (ISOFORM 1), FUNCTION, ENZYME REGULATION. Tissue: Adipocyte.
[4]	"Insulin activates the alpha isoform of class II phosphoinositide 3-kinase." Brown R.A., Domin J., Arcaro A., Waterfield M.D., Shepherd P.R. J. Biol. Chem. 274:14529-14532(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, PHOSPHORYLATION.
[5]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, MASS SPECTROMETRY. Tissue: Brain cortex.
[6]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, MASS SPECTROMETRY. Tissue: Macrophage.
[7]	"Insulin-feedback via PI3K-C2alpha activated PKBalpha/Akt1 is required for glucose-stimulated insulin secretion." Leibiger B., Moede T., Uhles S., Barker C.J., Creveaux M., Domin J., Berggren P.-O., Leibiger I.B. FASEB J. 24:1824-1837(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ISULIN SECRETION.
[8]	"Requirement for class II phosphoinositide 3-kinase C2alpha in maintenance of glomerular structure and function." Harris D.P., Vogel P., Wims M., Moberg K., Humphries J., Jhaver K.G., DaCosta C.M., Shadoan M.K., Xu N., Hansen G.M., Balakrishnan S., Domin J., Powell D.R., Oravecz T. Mol. Cell. Biol. 31:63-80(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN KIDNEY, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[9]	"Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2alpha." Liu L., Song X., He D., Komma C., Kita A., Virbasius J.V., Huang G., Bellamy H.D., Miki K., Czech M.P., Zhou G.W. J. Biol. Chem. 281:4254-4260(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1561-1686, INTERACTION WITH PHOSPHATIDYLINOSITIDE-CONTAINING MEMBRANES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U52193 mRNA. Translation: AAC52604.1.
AK049609 mRNA. No translation available.
U55772 mRNA. Translation: AAB07682.1. Different initiation.

IPI

IPI00117935.
IPI00408894.

PIR

T42642.

RefSeq

NP_035213.2. NM_011083.2.

UniGene

Mm.3810.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B3R	X-ray	2.30	A/B	1561-1686	[»]

ProteinModelPortal

Q61194.

SMR

Q61194. Positions 733-1391, 1421-1532, 1561-1682.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q61194. 1 interaction.

PTM databases

PhosphoSite

Q61194.

Proteomic databases

PaxDb

Q61194.

PRIDE

Q61194.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

18704.

KEGG

mmu:18704.

Organism-specific databases

CTD

5286.

MGI

MGI:1203729. Pik3c2a.

Phylogenomic databases

eggNOG

COG5032.

HOGENOM

HOG000006920.

HOVERGEN

HBG082099.

KO

K00923.

OrthoDB

EOG4933H0.

Enzyme and pathway databases

BRENDA

2.7.1.154. 3474.

Gene expression databases

Genevestigator

Q61194.

GermOnline

ENSMUSG00000030660. Mus musculus.

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. 1 hit.
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

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Other

ChiTaRS

PIK3C2A. mouse.

EvolutionaryTrace

Q61194.

NextBio

294759.

SOURCE

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Entry information

Entry name

P3C2A_MOUSE

Accession

Primary (citable) accession number: Q61194
Secondary accession number(s): Q61182

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	August 30, 2005
Last modified:	May 29, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program