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Protein

Alpha-parvin

Gene

Parva

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development.2 Publications

GO - Molecular functioni

  • actin binding Source: MGI

GO - Biological processi

  • actin cytoskeleton reorganization Source: InterPro
  • actin-mediated cell contraction Source: UniProtKB
  • cell adhesion Source: MGI
  • cilium morphogenesis Source: UniProtKB
  • establishment or maintenance of cell polarity Source: UniProtKB
  • heterotypic cell-cell adhesion Source: UniProtKB
  • outflow tract septum morphogenesis Source: UniProtKB
  • regulation of cell shape Source: UniProtKB-KW
  • smooth muscle cell chemotaxis Source: UniProtKB
  • sprouting angiogenesis Source: UniProtKB
  • substrate adhesion-dependent cell spreading Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Angiogenesis, Cell adhesion, Cell shape, Chemotaxis, Cilium biogenesis/degradation

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-parvin
Alternative name(s):
Actopaxin
Gene namesi
Name:Parva
Synonyms:Actp
ORF Names:MNCb-0301
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1931144. Parva.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: Ensembl
  • cytoplasm Source: MGI
  • focal adhesion Source: MGI
  • lamellipodium Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
  • Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality, due to severe cardiovascular defects causing whole body edema and severe bleeding due to vessel rupture. Embryos show defects in the septation of the heart outflow tract. Their cardiomyocytes are round and fail to align in a parallel manner. Blood vessels are frequently enlarged and show numerous microaneurisms. Besides, blood vessels show abnormal constrictions and increased vascular sprouting. Vascular mural cells and pericytes display a rounded shape and impaired adhesion to the underlying vascular endothelium. Cells display highly dynamic formation of membrane ruffles with increased random motility, but impaired chemotaxis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 372371Alpha-parvinPRO_0000121581Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei8 – 81PhosphoserineCombined sources
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei19 – 191PhosphoserineCombined sources
Modified residuei28 – 281PhosphoserineBy similarity
Modified residuei62 – 621PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9EPC1.
MaxQBiQ9EPC1.
PaxDbiQ9EPC1.
PRIDEiQ9EPC1.

PTM databases

iPTMnetiQ9EPC1.
PhosphoSiteiQ9EPC1.

Expressioni

Gene expression databases

BgeeiQ9EPC1.
CleanExiMM_PARVA.
ExpressionAtlasiQ9EPC1. baseline and differential.
GenevisibleiQ9EPC1. MM.

Interactioni

Subunit structurei

Interacts with ARHGAP31. Interacts with TGFB1I1. Interacts with ILK, LIMS1 and PXN (via LD motifs). Interacts with the actin cytoskeleton.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IlkO552224EBI-6690233,EBI-6690138

GO - Molecular functioni

  • actin binding Source: MGI

Protein-protein interaction databases

BioGridi208263. 2 interactions.
DIPiDIP-57658N.
IntActiQ9EPC1. 3 interactions.
MINTiMINT-4106640.
STRINGi10090.ENSMUSP00000033030.

Structurei

3D structure databases

ProteinModelPortaliQ9EPC1.
SMRiQ9EPC1. Positions 246-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 201107CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini262 – 369108CH 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 255Interaction with ARHGAP31

Sequence similaritiesi

Belongs to the parvin family.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3631. Eukaryota.
ENOG410XQWH. LUCA.
GeneTreeiENSGT00390000009673.
HOGENOMiHOG000247027.
HOVERGENiHBG053517.
InParanoidiQ9EPC1.
KOiK06275.
OMAiHNVSFSF.
OrthoDBiEOG70KGPW.
PhylomeDBiQ9EPC1.
TreeFamiTF314025.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
InterProiIPR001715. CH-domain.
IPR028433. Parvin.
[Graphical view]
PANTHERiPTHR12114. PTHR12114. 1 hit.
PfamiPF00307. CH. 2 hits.
[Graphical view]
PIRSFiPIRSF039131. Parvin. 1 hit.
SMARTiSM00033. CH. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 2 hits.
PROSITEiPS50021. CH. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9EPC1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSPQKSPL VPKSPTPKSP PSRKKDDSFL GKLGGTLARR KKAKEVSEFQ
60 70 80 90 100
EEGMNAINLP LSPISFELDP EDTLLEENEV RTMVDPNSRN DPKLQELMKV
110 120 130 140 150
LIDWINDVLV GERIIVKDLA EDLYDGQVLQ KLFEKLESEK LNVAEVTQSE
160 170 180 190 200
IAQKQKLQTV LEKINETLKL PPRSIKWNVD SVHAKNLVAI LHLLVALSQY
210 220 230 240 250
FRAPIRLPDH VSIQVVVVQK REGILQSRQI QEEITGNTEA LSGRHERDAF
260 270 280 290 300
DTLFDHAPDK LNVVKKTLIT FVNKHLNKLN LEVTELETQF ADGVYLVLLM
310 320 330 340 350
GLLEGYFVPL HSFFLTPDSF EQKVLNVSFA FELMQDGGLE KPKPRPEDIV
360 370
NCDLKSTLRV LYNLFTKYRN VE
Length:372
Mass (Da):42,330
Last modified:March 1, 2001 - v1
Checksum:i1251F2586A1ACBC6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331L → H in BAA97981 (Ref. 3) Curated
Sequence conflicti66 – 661F → S in BAA97981 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237774 mRNA. Translation: AAG27175.1.
AF264766 mRNA. Translation: AAG09803.1.
AB045321 mRNA. Translation: BAA97981.1.
BC059236 mRNA. Translation: AAH59236.1.
CCDSiCCDS40091.1.
RefSeqiNP_065631.3. NM_020606.5.
UniGeneiMm.143763.

Genome annotation databases

EnsembliENSMUST00000033030; ENSMUSP00000033030; ENSMUSG00000030770.
ENSMUST00000106643; ENSMUSP00000102254; ENSMUSG00000030770.
GeneIDi57342.
KEGGimmu:57342.
UCSCiuc009jgt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237774 mRNA. Translation: AAG27175.1.
AF264766 mRNA. Translation: AAG09803.1.
AB045321 mRNA. Translation: BAA97981.1.
BC059236 mRNA. Translation: AAH59236.1.
CCDSiCCDS40091.1.
RefSeqiNP_065631.3. NM_020606.5.
UniGeneiMm.143763.

3D structure databases

ProteinModelPortaliQ9EPC1.
SMRiQ9EPC1. Positions 246-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208263. 2 interactions.
DIPiDIP-57658N.
IntActiQ9EPC1. 3 interactions.
MINTiMINT-4106640.
STRINGi10090.ENSMUSP00000033030.

PTM databases

iPTMnetiQ9EPC1.
PhosphoSiteiQ9EPC1.

Proteomic databases

EPDiQ9EPC1.
MaxQBiQ9EPC1.
PaxDbiQ9EPC1.
PRIDEiQ9EPC1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033030; ENSMUSP00000033030; ENSMUSG00000030770.
ENSMUST00000106643; ENSMUSP00000102254; ENSMUSG00000030770.
GeneIDi57342.
KEGGimmu:57342.
UCSCiuc009jgt.1. mouse.

Organism-specific databases

CTDi55742.
MGIiMGI:1931144. Parva.

Phylogenomic databases

eggNOGiKOG3631. Eukaryota.
ENOG410XQWH. LUCA.
GeneTreeiENSGT00390000009673.
HOGENOMiHOG000247027.
HOVERGENiHBG053517.
InParanoidiQ9EPC1.
KOiK06275.
OMAiHNVSFSF.
OrthoDBiEOG70KGPW.
PhylomeDBiQ9EPC1.
TreeFamiTF314025.

Miscellaneous databases

ChiTaRSiParva. mouse.
NextBioi313706.
PROiQ9EPC1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EPC1.
CleanExiMM_PARVA.
ExpressionAtlasiQ9EPC1. baseline and differential.
GenevisibleiQ9EPC1. MM.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
InterProiIPR001715. CH-domain.
IPR028433. Parvin.
[Graphical view]
PANTHERiPTHR12114. PTHR12114. 1 hit.
PfamiPF00307. CH. 2 hits.
[Graphical view]
PIRSFiPIRSF039131. Parvin. 1 hit.
SMARTiSM00033. CH. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 2 hits.
PROSITEiPS50021. CH. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion."
    Nikolopoulos S.N., Turner C.E.
    J. Cell Biol. 151:1435-1448(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ACTIN; PXN AND TGFB1I1.
  3. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
    Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "CdGAP associates with actopaxin to regulate integrin-dependent changes in cell morphology and motility."
    LaLonde D.P., Grubinger M., Lamarche-Vane N., Turner C.E.
    Curr. Biol. 16:1375-1385(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGAP31.
  6. "Alpha-parvin controls vascular mural cell recruitment to vessel wall by regulating RhoA/ROCK signalling."
    Montanez E., Wickstrom S.A., Altstatter J., Chu H., Fassler R.
    EMBO J. 28:3132-3144(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION.
  7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-14 AND SER-19, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPARVA_MOUSE
AccessioniPrimary (citable) accession number: Q9EPC1
Secondary accession number(s): Q9JJ65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: March 1, 2001
Last modified: March 16, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.