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Q9ES46 (PARVB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-parvin
Gene names
Name:Parvb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration By similarity.

Subunit structure

Interacts with ILK, ARHGEF6, PXN (via LD motifs), ACTN2 and actin By similarity. Interacts with DYSF. Ref.3

Subcellular location

Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmcytoskeleton By similarity. Cell projectionlamellipodium By similarity. Cytoplasmmyofibrilsarcomere By similarity. CytoplasmmyofibrilsarcomereZ line By similarity. Note: Constituent of focal adhesions. Detected at the tips of the leading edge of cells. Colocalizes with F-actin at the tips of lamellipodia By similarity.

Tissue specificity

Expressed predominantly in heart and moderately in spleen, lung and skeletal muscle. Ref.2

Post-translational modification

Phosphorylated by ILK By similarity.

Sequence similarities

Belongs to the parvin family.

Contains 2 CH (calponin-homology) domains.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Beta-parvin
PRO_0000121584

Regions

Domain88 – 195108CH 1
Domain255 – 362108CH 2

Sequences

Sequence LengthMass (Da)Tools
Q9ES46 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: A3C6B8B3D5875CEA

FASTA36541,669
        10         20         30         40         50         60 
MSSAPPRSPT PRAPKMKKDE SFLGKLGGTL ARKKKTREVT DLQEEGKSAI NSPMAPALVD 

        70         80         90        100        110        120 
IHPEDTQLEE NEERTMIDPT SREDPKFKEL VKVLLDWIND VLAEERIIVK QLEEDLYDGQ 

       130        140        150        160        170        180 
VLQKLLEKLA HCKLNVAEVT QSEIGQKQKL QTVLEAVQDL LRPHGWPLRW NVDSIHGKNL 

       190        200        210        220        230        240 
VAILHLLVSL AMHFRAPIHL PEHVTVQVVV VRKREGLLHS SHISEELTTT TEIMMGRFER 

       250        260        270        280        290        300 
DAFDTLFDHA PDKLNLVKKS LITFVNKHLN KLNLEVTDLE TQFADGVYLV LLLGLLEDYF 

       310        320        330        340        350        360 
VPLHNFYLTP DSFDQKVHNV AFAFELMLDG GLKKPKARPE DVVNLDLKST LRVLYTLFTK 


YKDVE 

« Hide

References

[1]"Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily."
Olski T.M., Noegel A.A., Korenbaum E.
J. Cell Sci. 114:525-538(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Genomic organization and expression profile of the parvin family of focal adhesion proteins in mice and humans."
Korenbaum E., Olski T.M., Noegel A.A.
Gene 279:69-79(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[3]"Dysferlin interacts with affixin (beta-parvin) at the sarcolemma."
Matsuda C., Kameyama K., Tagawa K., Ogawa M., Suzuki A., Yamaji S., Okamoto H., Nishino I., Hayashi Y.K.
J. Neuropathol. Exp. Neurol. 64:334-340(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYSF.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF237770 mRNA. Translation: AAG27172.1.
CCDSCCDS37167.1.
RefSeqNP_573395.1. NM_133167.3.
UniGeneMm.323892.

3D structure databases

ProteinModelPortalQ9ES46.
SMRQ9ES46. Positions 236-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-57659N.
IntActQ9ES46. 2 interactions.
MINTMINT-7978697.

PTM databases

PhosphoSiteQ9ES46.

Proteomic databases

MaxQBQ9ES46.
PaxDbQ9ES46.
PRIDEQ9ES46.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023072; ENSMUSP00000023072; ENSMUSG00000022438.
GeneID170736.
KEGGmmu:170736.
UCSCuc007xby.1. mouse.

Organism-specific databases

CTD29780.
MGIMGI:2153063. Parvb.

Phylogenomic databases

eggNOGNOG303418.
GeneTreeENSGT00390000009673.
HOGENOMHOG000247027.
HOVERGENHBG053517.
InParanoidQ9ES46.
KOK06275.
OMALAMHFQA.
OrthoDBEOG70KGPW.
PhylomeDBQ9ES46.
TreeFamTF314025.

Gene expression databases

ArrayExpressQ9ES46.
BgeeQ9ES46.
CleanExMM_PARVB.
GenevestigatorQ9ES46.

Family and domain databases

Gene3D1.10.418.10. 2 hits.
InterProIPR001715. CH-domain.
IPR028433. Parvin.
[Graphical view]
PANTHERPTHR12114. PTHR12114. 1 hit.
PfamPF00307. CH. 2 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 2 hits.
PROSITEPS50021. CH. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio370282.
PROQ9ES46.
SOURCESearch...

Entry information

Entry namePARVB_MOUSE
AccessionPrimary (citable) accession number: Q9ES46
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 96 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot