Reviewed, UniProtKB/Swiss-Prot Q5I6B8 (PI51C_RAT)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma
      Short name=PtdIns(4)P-5-kinase 1 gamma
      Short name=PIP5K1-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)

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	Mediates RAC1-dependent reorganization of actin filaments By similarity. Plays a role in membrane ruffling and assembly of clathrin-coated pits at the synapse. Participates in the biosynthesis of phosphatidylinositol-4,5-bisphosphate. 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, TLN2 and CSK By similarity. Interacts with ARF6. Interacts with AP2B1. Interacts with AP2M1; phosphorylation of PIP5K1C by CSK disrupts the interaction; clathrin competes with PIP5K1C By similarity. Ref.2
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Cytoplasmic, associated with the plasma membrane. Detected in focal adhesion plaques, membrane ruffles and plasma membrane invaginations. Ref.2
Sequence similarities	Contains 1 PIPK domain.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
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	671	1	Phosphotyrosine; by CSK By similarity
Experimental info
	Mutagenesis	188	1	K → A: Reduces activity by over 99%. Ref.1
	Mutagenesis	316	1	D → K: Loss of kinase activity. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q5I6B8-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: F34E175EFFF54D5D	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

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: 14741049] [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: 12847086] [Abstract] Cited for: INTERACTION WITH ARF6, SUBCELLULAR LOCATION, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY850259 mRNA. Translation: AAW34235.1.
IPI	IPI00389614.
RefSeq	NP_001009967.2. NP_001029142.1.
UniGene	Rn.2928
3D structure databases
SMR	Q5I6B8. Positions 75-442.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5I6B8.
Genome annotation databases
Ensembl	ENSRNOT00000061159; ENSRNOP00000057873; ENSRNOG00000020577; Rattus norvegicus. [Genome view]
GeneID	314641.
KEGG	rno:314641.
Organism-specific databases
CTD	314641.
RGD	1309938. Pip5k1c.
Phylogenomic databases
HOVERGEN	Q5I6B8.
InParanoid	Q5I6B8.
Enzyme and pathway databases
BRENDA	2.7.1.68. 248.
Gene expression databases
Genevestigator	Q5I6B8.
Family and domain databases
InterPro	IPR002498. PInositol-4-P-5-kinase_core. IPR016034. PInositol-4P-5-kinase_core_sub. [Graphical view]
PANTHER	PTHR23086. PIP5K. 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 Resources
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:	February 9, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)