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D3ZSI8 (PI51A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha

Short name=PIP5K1-alpha
Short name=PtdIns(4)P-5-kinase 1 alpha
EC=2.7.1.68
Alternative name(s):
68 kDa type I phosphatidylinositol 4-phosphate 5-kinase
Phosphatidylinositol 4-phosphate 5-kinase type I alpha
Short name=PIP5KIalpha
Gene names
Name:Pip5k1a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 actin cytoskeleton organization, cell adhesion, migration and phagocytosis. Required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of RAC1 to the plasma membrane. Together with PIP5K1C is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle ingestion by activating WAS that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B is required after stimulation of G-protein coupled receptors for stable platelet adhesion. Plays a role during calcium-induced keratinocyte differentiation. Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, diacylglycerol and inositol 1,4,5-trisphosphate that mobilize internal calcium and drive keratinocyte differentiation. Together with PIP5K1C have a role during embryogenesis. Functions also in the nucleus where it acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs By similarity.

Catalytic activity

ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.

Subunit structure

Interacts with RAC1. Interacts with TUT1. Forms a complex with CDH1/E-cadherin, CTNNB1/beta-catenin and CTNND1 at the plasma membrane upon calcium stimulation By similarity.

Subcellular location

Cell membrane By similarity. Nucleus speckle By similarity. Cytoplasm. Cell projectionruffle By similarity.

Sequence similarities

Contains 1 PIPK domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cytoplasm
Membrane
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from electronic annotation. Source: Ensembl

activation of Rac GTPase activity

Inferred from electronic annotation. Source: Ensembl

cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

fibroblast migration

Inferred from electronic annotation. Source: Ensembl

focal adhesion assembly

Inferred from electronic annotation. Source: Ensembl

phospholipid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

protein targeting to plasma membrane

Inferred from electronic annotation. Source: Ensembl

ruffle assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

lamellipodium

Inferred from electronic annotation. Source: Ensembl

mRNA cleavage and polyadenylation specificity factor complex

Inferred from electronic annotation. Source: Ensembl

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

ruffle membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_function1-phosphatidylinositol-4-phosphate 5-kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 546546Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
PRO_0000424437

Regions

Domain65 – 433369PIPK

Amino acid modifications

Cross-link87Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
D3ZSI8 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: F0DF7489A100D9C3

FASTA54660,605
        10         20         30         40         50         60 
MASASSGPAA AGFSPLDSGV PAGTAASGIK RGTVSEGPYA SLMPVKKIGH RSVDSSGETT 

        70         80         90        100        110        120 
YKKTTSSALK GAIQLGITHT VGSLSTKPER DVLMQDFYVV ESIFFPSEGS NLTPAHHYND 

       130        140        150        160        170        180 
FRFKTYAPVA FRYFRELFGI RPDDYLYSLC SEPLIELSNS GASGSLFYVS SDDEFIIKTV 

       190        200        210        220        230        240 
QHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCVQAGG KNIRIVVMNN LLPRSVKMHM 

       250        260        270        280        290        300 
KYDLKGSTYK RRASQKEREK TLPTFKDLDF LQDIPDGLFL DADMYSALCK TLQRDCLVLQ 

       310        320        330        340        350        360 
SFKIMDYSLL MSIHNMDHAQ REPMNSETQY SIDTRRPAPQ KALYSTAMES IQGEARRGGT 

       370        380        390        400        410        420 
VETEDHMGGI PARNNKGERL LLYIGIIDIL QSYRFVKKLE HSWKALVHDG DTVSVHRPGF 

       430        440        450        460        470        480 
YAERFQRFMC NTVFKKIPLK PSPTKKFRSG PSFSRRSGPS GNSCTPSQPT ASGEHKAQVT 

       490        500        510        520        530        540 
TKAEVEPDIH LGRPDVLPQT PPLEEISEGS PVPGPSFSPA VGQPLQILNL SSTLEKLDVA 


ESELTH 

« Hide

References

[1]Soares M.B., Casavant T.L., Sheffield V.C., Bonaldo M.F., Bair T.B., Scheetz T.E., Snir E., Akabogu I., Bair J.L., Berger B., Crouch K., Davis A., Eystone M.E., Keppel C., Kucaba T.A., Lebeck M., Lin J.L., de Melo A.I.R. expand/collapse author list , Rehmann J., Reiter R.S., Schaefer K., Smith C., Tack D., Trout K., Lin J.J.-C.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY724476 mRNA. No translation available.
AABR06019271 Genomic DNA. No translation available.
UniGeneRn.1836.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000028609; ENSRNOP00000028609; ENSRNOG00000021068.
UCSCRGD:1306127. rat.

Organism-specific databases

RGD1306127. Pip5k1a.

Phylogenomic databases

GeneTreeENSGT00690000101870.
OMAETEDHMG.
OrthoDBEOG70W3DM.
PhylomeDBD3ZSI8.
TreeFamTF319618.

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

NextBio35569837.

Entry information

Entry namePI51A_RAT
AccessionPrimary (citable) accession number: D3ZSI8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2013
Last sequence update: April 20, 2010
Last modified: April 16, 2014
This is version 31 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