Serine/threonine-protein kinase PAK 3 - Rattus norvegicus (Rat)

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Q62829 (PAK3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 100. 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:
Serine/threonine-protein kinase PAK 3
EC=2.7.11.1

Alternative name(s):
Beta-PAK
p21-activated kinase 3
Short name=PAK-3
p65-PAK

Gene names

Name:

Pak3

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	544 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, or cell cycle regulation. Plays a role in dendrite spine morphogenesis as well as synapse formation and plasticity. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Additionally, phosphorylates TNNI3/troponin I to modulate calcium sensitivity and relaxation kinetics of thin myofilaments. Ref.2
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Activated by binding small G proteins. Binding of GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers from the autoinhibited dimer, enables phosphorylation of Thr-421 and allows the kinase domain to adopt an active structure By similarity.
Subunit structure	Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1. Shows highly specific binding to the SH3 domains of phospholipase C-gamma and of adapter protein NCK. Interacts with the C-terminal of APP. Interacts with ARHGEF6 and ARHGEF7 By similarity. Ref.2
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Detected at high levels in the brain and at low levels in the testis. Ref.2
Developmental stage	Found in the embryonic CNS with little expression elsewhere.
Post-translational modification	Autophosphorylated when activated by CDC42/p21. Ref.3
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily. Contains 1 CRIB domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	SH3-binding
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	axonogenesis Inferred from sequence or structural similarity. Source: UniProtKB dendrite development Inferred from sequence or structural similarity. Source: UniProtKB intracellular protein kinase cascade Traceable author statement. Source: RGD regulation of actin filament polymerization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase binding Inferred from direct assay Ref.1. Source: RGD MAP kinase kinase activity Inferred from sequence or structural similarity. Source: UniProtKB SH3 domain binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity 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 – 544

544

Serine/threonine-protein kinase PAK 3

PRO_0000086473

Regions

Domain

70 – 83

CRIB

Domain

268 – 519

252

Protein kinase

Nucleotide binding

274 – 282

ATP By similarity

Region

65 – 135

Autoregulatory region By similarity

Region

65 – 108

GTPase-binding By similarity

Region

84 – 267

184

Linker

Compositional bias

172 – 182

Poly-Glu

Sites

Active site

387

Proton acceptor By similarity

Binding site

297

ATP Probable

Amino acid modifications

Modified residue

Phosphoserine; by autocatalysis Ref.3

Modified residue

139

Phosphoserine; by autocatalysis Ref.3

Modified residue

421

Phosphothreonine; by autocatalysis Ref.3

Modified residue

520

N6-acetyllysine By similarity

Experimental info

Mutagenesis

297

K → A: Loss of kinase activity. Ref.2

Mutagenesis

421

T → E: Constitutively active. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q62829 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7B940FC204A2B48B
Show »

FASTA

544

60,711

        10         20         30         40         50         60 
MSDSLDNEEK PPAPPLRMNS NNRDSSALNH SSKPLPMAPE EKNKKARLRS IFPGGGDKTN 

        70         80         90        100        110        120 
KKKEKERPEI SLPSDFEHTI HVGFDAVTGE FTGIPEQWAR LLQTSNITKL EQKKNPQAVL 

       130        140        150        160        170        180 
DVLKFYDSKE TVNNQKYMSF TSGDKSAHGY IAAHQSNTKT ASEPPLAPPV SEEEDEEEEE 

       190        200        210        220        230        240 
EEDDNEPPPV IAPRPEHTKS IYTRSVVESI ASPAAPNKEA TPPSAENANS STLYRNTDRQ 

       250        260        270        280        290        300 
RKKSKMTDEE ILEKLRSIVS VGDPKKKYTR FEKIGQGASG TVYTALDIAT GQEVAIKQMN 

       310        320        330        340        350        360 
LQQQPKKELI INEILVMREN KNPNIVNYLD SYLVGDELWV VMEYLAGGSL TDVVTETCMD 

       370        380        390        400        410        420 
EGQIAAVCRE CLQALDFLHS NQVIHRDIKS DNILLGMDGS VKLTDFGFCA QITPEQSKRS 

       430        440        450        460        470        480 
TMVGTPYWMA PEVVTRKAYG PKVDIWSLGI MAIEMVEGEP PYLNENPLRA LYLIATNGTP 

       490        500        510        520        530        540 
ELQNPERLSA VFRDFLNRCL EMDVDRRGSA KELLQHPFLK LAKPLSSLTP LILAAKEAIK 


NSSR

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References

[1]	"Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family." Manser E., Chong C., Zhao Z.-S., Leung T., Michael G., Hall C., Lim L. J. Biol. Chem. 270:25070-25078(1995) [PubMed: 7559638] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-56. Tissue: Brain.
[2]	"DNA synthesis and neuronal apoptosis caused by familial Alzheimer disease mutants of the amyloid precursor protein are mediated by the p21 activated kinase PAK3." McPhie D.L., Coopersmith R., Hines-Peralta A., Chen Y., Ivins K.J., Manly S.P., Kozlowski M.R., Neve K.A., Neve R.L. J. Neurosci. 23:6914-6927(2003) [PubMed: 12890786] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH APP, MUTAGENESIS OF LYS-297 AND THR-421.
[3]	"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity." Chong C., Tan L., Lim L., Manser E. J. Biol. Chem. 276:17347-17353(2001) [PubMed: 11278486] [Abstract] Cited for: PHOSPHORYLATION AT SER-50; SER-139 AND THR-421.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U33314 mRNA. Translation: AAC52268.1.
IPI	IPI00327030.
PIR	A57597.
RefSeq	NP_062083.1. NM_019210.1.
UniGene	Rn.10128.
3D structure databases
ProteinModelPortal	Q62829.
SMR	Q62829. Positions 73-141, 247-538.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-126419.
STRING	Q62829.
PTM databases
PhosphoSite	Q62829.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000006459; ENSRNOP00000006459; ENSRNOG00000004676.
GeneID	29433.
KEGG	rno:29433.
UCSC	NM_019210. rat.
Organism-specific databases
CTD	5063.
RGD	3251. Pak3.
Phylogenomic databases
eggNOG	roNOG10184.
GeneTree	ENSGT00580000081260.
HOVERGEN	HBG108518.
PhylomeDB	Q62829.
Enzyme and pathway databases
BRENDA	2.7.11.1. 5301.
Gene expression databases
ArrayExpress	Q62829.
Genevestigator	Q62829.
GermOnline	ENSRNOG00000004676. Rattus norvegicus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000095. PAK_box_Rho-bd. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K05733.
Pfam	PF00786. PBD. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00285. PBD. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS50108. CRIB. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	609162.

Entry information

Entry name

PAK3_RAT

Accession

Primary (citable) accession number: Q62829

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 100 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

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents