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Q5I6B8 (PI51C_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length688 AA.
Sequence statusComplete.
Protein existenceEvidence 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 junctionfocal adhesion. Cell junctionadherens junction. Cell projectionruffle membrane. Cell projectionphagocytic cup. Cell projectionuropodium 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 688688Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
PRO_0000185464

Regions

Domain75 – 443369PIPK

Amino acid modifications

Modified residue2651N6-acetyllysine By similarity
Modified residue2681N6-acetyllysine By similarity
Modified residue6351Phosphotyrosine; by EGFR By similarity
Modified residue6711Phosphotyrosine; by CSK By similarity
Modified residue6721Phosphoserine; by CDK5, MAPK1 and CDK1 By similarity

Experimental info

Mutagenesis1881K → A: Reduces activity by over 99%. Ref.1
Mutagenesis3161D → K: Loss of kinase activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5I6B8 [UniParc].

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

FASTA68875,594
        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 

« Hide

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.
RefSeqNP_001009967.2. NM_001009967.2.
NP_001029142.1. NM_001033970.1.
UniGeneRn.2928.

3D structure databases

ProteinModelPortalQ5I6B8.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ5I6B8.
PRIDEQ5I6B8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID314641.
KEGGrno:314641.
UCSCRGD:1309938. rat.

Organism-specific databases

CTD23396.
RGD1309938. Pip5k1c.

Phylogenomic databases

eggNOGCOG5253.
HOGENOMHOG000193876.
HOVERGENHBG052818.
InParanoidQ5I6B8.
KOK00889.
PhylomeDBQ5I6B8.

Gene expression databases

GenevestigatorQ5I6B8.

Family and domain databases

Gene3D3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProIPR023610. PInositol-4-P-5-kinase.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR016034. PInositol-4P-5-kinase_core_sub.
[Graphical view]
PANTHERPTHR23086. PTHR23086. 1 hit.
PfamPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEPS51455. PIPK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio668018.

Entry information

Entry namePI51C_RAT
AccessionPrimary (citable) accession number: Q5I6B8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families