Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma

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Q5I6B8 (PI51C_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 67. History...

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

Documents (1) |

Third-party data

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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 5-kinase type-1 gamma
Short name=PIP5K1-gamma
Short name=PtdIns(4)P-5-kinase 1 gamma
EC=2.7.1.68

Alternative name(s):
Phosphatidylinositol 4-phosphate 5-kinase type I gamma
Short name=PIP5KIgamma

Gene names

Name:

Pip5k1c

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	688 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as vesicle mediated transport, cell adhesion, cell polarization and cell migration. Together with PIP5K1A is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport. Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis. Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2). Required for clathrin-coated pits assembly at the synapse. Participates in cell junction assembly. Modulates adherens junctions formation by facilitating CDH1 trafficking. Required for focal adhesion dynamics. Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions. Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins. Required for uropodium formation and retraction of the cell rear during directed migration. Has a role in growth factor- stimulated directional cell migration and adhesion. Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor. Negative regulator of T-cell activation and adhesion. Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor. Together with PIP5K1A have a role during embryogenesis and together with PIP5K1B may have a role immediately after birth By similarity. Ref.2
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Enzyme regulation	Activated by interaction with ARF6.
Subunit structure	Interacts with TLN1 By similarity. Interacts with TLN2; interaction stimulates lipid kinase activity By similarity. May compete with beta-integrins for the same binding site on TLN1 and TLN2 By similarity. Interacts with ARF6. Interacts with AP2B1 By similarity. Interacts with AP2M1; phosphorylation of PIP5K1C by CSK disrupts the interaction; clathrin competes with PIP5K1C By similarity. Interacts with CDH1 By similarity. Interacts with CSK By similarity. Interacts with PLCG1; interaction is abolished upon EGF stimulation By similarity. Ref.2
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endomembrane system. Cytoplasm. Cell junction › focal adhesion. Cell junction › adherens junction. Cell projection › ruffle membrane. Cell projection › phagocytic cup. Cell projection › uropodium Ref.2.
Post-translational modification	Phosphorylation on Ser-672 negatively regulates binding to TLN2 and is strongly stimulated in mitosis By similarity. Phosphorylation on Tyr-671 is necessary for targeting to focal adhesions By similarity. Phosphorylation on Ser-672 and Tyr-671 are mutually exclusive By similarity. Phosphorylated by SYK and CSK By similarity. Tyrosine phosphorylation is enhanced by PTK2 signaling By similarity. Phosphorylated at Tyr-635 upon EGF stimulation By similarity. Some studies suggest that phosphorylation on Tyr-671 enhances binding to tailins (TLN1 and TLN2) By similarity; others that phosphorylation at Tyr-671 does not directly enhance binding to tailins (TLN1 and TLN2) but may act indirectly by inhibiting phosphorylation at Ser-672 By similarity. Acetylation at Lys-265 and Lys-268 seems to decrease lipid kinase activity. Deacetylation of these sites by SIRT1 positively regulates the exocytosis of TSH-containing granules from pituitary cells By similarity.
Sequence similarities	Contains 1 PIPK domain.

Ontologies

Keywords
Biological process	Cell adhesion Chemotaxis Endocytosis Exocytosis Phagocytosis
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW exocytosis Inferred from electronic annotation. Source: UniProtKB-KW phagocytosis Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell phagocytic cup Inferred from electronic annotation. Source: UniProtKB-SubCell ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell uropod Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	1-phosphatidylinositol-4-phosphate 5-kinase activity Inferred from electronic annotation. Source: EC ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 688

688

Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma

PRO_0000185464

Regions

Domain

75 – 443

369

PIPK

Amino acid modifications

Modified residue

265

N6-acetyllysine By similarity

Modified residue

268

N6-acetyllysine By similarity

Modified residue

635

Phosphotyrosine; by EGFR By similarity

Modified residue

671

Phosphotyrosine; by CSK By similarity

Modified residue

672

Phosphoserine; by CDK5, MAPK1 and CDK1 By similarity

Experimental info

Mutagenesis

188

K → A: Reduces activity by over 99%. Ref.1

Mutagenesis

316

D → K: Loss of kinase activity. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q5I6B8 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: F34E175EFFF54D5D
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FASTA

688

75,594

        10         20         30         40         50         60 
MELEVPDEAE SAEAGAVTAE AAWSAESGAA AGMTQKKAIL AEAPLVTGQP GPGHGKKLGH 

        70         80         90        100        110        120 
RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGNLSSKPER DVLMQDFYVV ESIFFPSEGS 

       130        140        150        160        170        180 
NLTPAHHFQD FRFKTYAPVA FRYFRELFGI RPDDYLYSLC NEPLIELSNP GASGSVFYVT 

       190        200        210        220        230        240 
SDDEFIIKTV MHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN 

       250        260        270        280        290        300 
VLPRVVKMHL KFDLKGSTYK RRASKKEKEK SLPTYKDLDF MQDMPEGLLL DSDTFGALVK 

       310        320        330        340        350        360 
TLQRDCLVLE SFKIMDYSLL LGVHNIDQQE RERQAEGAQS KADEKRPVAQ KALYSTARES 

       370        380        390        400        410        420 
IQGGAARGEA IETDDTMGGI PAVNGRGERL LLHIGIIDIL QSYRFIKKLE HTWKALVHDG 

       430        440        450        460        470        480 
DTVSVHRPSF YAERFFKFMS STVFRKSSSL KSSPSKKGRG ALLAVKPLGP TAAFSASQIP 

       490        500        510        520        530        540 
SEREDVQYDL RGARSYPTLE DEGRPDLLPC TPPSFEEATT ASIATTLSST SLSIPERSPS 

       550        560        570        580        590        600 
DTSEQPRYRR RTQSSGQDGR PQEELHAEDL QKITVQVEPV CGVGVVVPKE QGAGVEVPPS 

       610        620        630        640        650        660 
GASAAATVEV DAASQASEPA SQASDEEDAP STDIYFFAHG RYWLFSPRRR RLRAVTPSHT 

       670        680 
GAPTDGRSWV YSPLHYSARP ASDGESDT

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References

[1]	"A novel neuronal-specific splice variant of Type I phosphatidylinositol 4-phosphate 5-kinase isoform gamma." Giudici M.-L., Emson P.C., Irvine R.F. Biochem. J. 379:489-496(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-188 AND ASP-316, TISSUE SPECIFICITY. Tissue: Hippocampus.
[2]	"ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Igamma." Krauss M., Kinuta M., Wenk M.R., De Camilli P., Takei K., Haucke V. J. Cell Biol. 162:113-124(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ARF6, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY850259 mRNA. Translation: AAW34235.1.
IPI	IPI00389614.
RefSeq	NP_001009967.2. NM_001009967.2. NP_001029142.1. NM_001033970.1.
UniGene	Rn.2928.
3D structure databases
ProteinModelPortal	Q5I6B8.
ModBase	Search...
Proteomic databases
PaxDb	Q5I6B8.
PRIDE	Q5I6B8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	314641.
KEGG	rno:314641.
UCSC	RGD:1309938. rat.
Organism-specific databases
CTD	23396.
RGD	1309938. Pip5k1c.
Phylogenomic databases
eggNOG	COG5253.
HOGENOM	HOG000193876.
HOVERGEN	HBG052818.
InParanoid	Q5I6B8.
KO	K00889.
OrthoDB	EOG4JQ3Z0.
Gene expression databases
ArrayExpress	Q5I6B8.
Genevestigator	Q5I6B8.
Family and domain databases
InterPro	IPR023610. PInositol-4-P-5-kinase. IPR002498. PInositol-4-P-5-kinase_core. IPR016034. PInositol-4P-5-kinase_core_sub. [Graphical view]
PANTHER	PTHR23086. PTHR23086. 1 hit.
Pfam	PF01504. PIP5K. 1 hit. [Graphical view]
SMART	SM00330. PIPKc. 1 hit. [Graphical view]
PROSITE	PS51455. PIPK. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	668018.

Entry information

Entry name

PI51C_RAT

Accession

Primary (citable) accession number: Q5I6B8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	February 15, 2005
Last modified:	April 3, 2013
This is version 67 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents