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Q9NVD7 (PARVA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-parvin
Alternative name(s):
Actopaxin
CH-ILKBP
Calponin-like integrin-linked kinase-binding protein
Matrix-remodeling-associated protein 2
Gene names
Name:PARVA
Synonyms:MXRA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. 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. Ref.2 Ref.6 Ref.8 Ref.12

Subunit structure

Interacts with TGFB1I1 By similarity. Interacts with ILK, LIMS1 and PXN (via LD motifs). Interacts with ARHGAP31. Interacts with the actin cytoskeleton. Ref.2 Ref.8 Ref.9 Ref.16 Ref.17 Ref.18

Subcellular location

Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. CytoplasmmyofibrilsarcomereZ line By similarity. Note: Constituent of focal adhesions. Associates with the actin cytoskeleton. Ref.2 Ref.6 Ref.15

Tissue specificity

Widely expressed, with highest levels in heart, skeletal muscle, kidney and liver. Ref.2 Ref.6 Ref.7

Sequence similarities

Belongs to the parvin family.

Contains 2 CH (calponin-homology) domains.

Ontologies

Keywords
   Biological processAngiogenesis
Cell adhesion
Cell shape
Chemotaxis
Cilium biogenesis/degradation
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from electronic annotation. Source: InterPro

actin-mediated cell contraction

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction assembly

Traceable author statement. Source: Reactome

cilium morphogenesis

Inferred from mutant phenotype Ref.12. Source: UniProtKB

establishment or maintenance of cell polarity

Inferred from sequence or structural similarity. Source: UniProtKB

heterotypic cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

outflow tract septum morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

smooth muscle cell chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

sprouting angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

substrate adhesion-dependent cell spreading

Inferred from mutant phenotype Ref.2. Source: UniProtKB

   Cellular_componentZ disc

Inferred from electronic annotation. Source: UniProtKB-SubCell

actin cytoskeleton

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from direct assay Ref.2. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 12432066PubMed 16189514PubMed 17553790PubMed 21516116PubMed 23455922PubMed 23877428. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ILKQ134187EBI-747655,EBI-747644

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NVD7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NVD7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     134-182: EKLESEKLNV...RSIKWNVDSV → GRRVECCNGC...KCVEHGITAQ
     183-372: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 372371Alpha-parvin
PRO_0000121580

Regions

Domain95 – 201107CH 1
Domain262 – 369108CH 2
Region21 – 255Interaction with ARHGAP31

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue81Phosphoserine By similarity
Modified residue141Phosphoserine Ref.11
Modified residue191Phosphoserine Ref.11 Ref.14
Modified residue281Phosphoserine Ref.10
Modified residue621Phosphoserine Ref.10

Natural variations

Alternative sequence134 – 18249EKLES…NVDSV → GRRVECCNGCVFNCRWLDHL LVARRSYSQFTVAYLEMDYK CVEHGITAQ in isoform 2.
VSP_008884
Alternative sequence183 – 372190Missing in isoform 2.
VSP_008885

Experimental info

Sequence conflict111V → A in AAH14535. Ref.4

Secondary structure

.................. 372
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F48BB5B1E83F8CEF

FASTA37242,244
        10         20         30         40         50         60 
MATSPQKSPS VPKSPTPKSP PSRKKDDSFL GKLGGTLARR KKAKEVSELQ EEGMNAINLP 

        70         80         90        100        110        120 
LSPIPFELDP EDTMLEENEV RTMVDPNSRS DPKLQELMKV LIDWINDVLV GERIIVKDLA 

       130        140        150        160        170        180 
EDLYDGQVLQ KLFEKLESEK LNVAEVTQSE IAQKQKLQTV LEKINETLKL PPRSIKWNVD 

       190        200        210        220        230        240 
SVHAKSLVAI LHLLVALSQY FRAPIRLPDH VSIQVVVVQK REGILQSRQI QEEITGNTEA 

       250        260        270        280        290        300 
LSGRHERDAF DTLFDHAPDK LNVVKKTLIT FVNKHLNKLN LEVTELETQF ADGVYLVLLM 

       310        320        330        340        350        360 
GLLEGYFVPL HSFFLTPDSF EQKVLNVSFA FELMQDGGLE KPKPRPEDIV NCDLKSTLRV 

       370 
LYNLFTKYRN VE 

« Hide

Isoform 2 [UniParc].

Checksum: B7D6685D209E628F
Show »

FASTA18220,625

References

« Hide 'large scale' 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] (ISOFORM 1).
[2]"A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading."
Tu Y., Huang Y., Zhang Y., Hua Y., Wu C.
J. Cell Biol. 153:585-598(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ILK; LIMS1 AND WITH ACTIN CYTOSKELETON, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Mammary gland.
[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] (ISOFORM 1).
Tissue: Brain.
[5]"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 118-131.
Tissue: Adipocyte.
[6]"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: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[7]"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.
[8]"Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival."
Zhang Y., Chen K., Tu Y., Wu C.
J. Biol. Chem. 279:41695-41705(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ILK.
[9]"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.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Functional genomic screen for modulators of ciliogenesis and cilium length."
Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G.
Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"LNK (SH2B3) is a key regulator of integrin signaling in endothelial cells and targets alpha-parvin to control cell adhesion and migration."
Devalliere J., Chatelais M., Fitau J., Gerard N., Hulin P., Velazquez L., Turner C.E., Charreau B.
FASEB J. 26:2592-2606(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[16]"The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly."
Wang X., Fukuda K., Byeon I.J., Velyvis A., Wu C., Gronenborn A., Qin J.
J. Biol. Chem. 283:21113-21119(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 244-372 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
[17]"Structural analysis of the interactions between paxillin LD motifs and alpha-parvin."
Lorenz S., Vakonakis I., Lowe E.D., Campbell I.D., Noble M.E., Hoellerer M.K.
Structure 16:1521-1531(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 242-372 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
[18]"The pseudoactive site of ILK is essential for its binding to alpha-parvin and localization to focal adhesions."
Fukuda K., Gupta S., Chen K., Wu C., Qin J.
Mol. Cell 36:819-830(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 248-372 IN COMPLEX WITH ILK, INTERACTION WITH ILK.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF237771 mRNA. Translation: AAG27173.1.
AF325830 mRNA. Translation: AAK49911.1.
AK001655 mRNA. Translation: BAA91815.1.
AK022316 mRNA. Translation: BAB14009.1.
BC016713 mRNA. Translation: AAH16713.1.
BC014535 mRNA. Translation: AAH14535.1.
RefSeqNP_060692.2. NM_018222.4.
UniGeneHs.432914.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K2RNMR-A244-372[»]
2VZCX-ray1.05A/B242-372[»]
2VZDX-ray2.10A/B242-372[»]
2VZGX-ray1.80B242-372[»]
2VZIX-ray2.20B242-372[»]
3KMUX-ray1.80B248-372[»]
3KMWX-ray2.00B248-372[»]
3REPX-ray1.80B248-372[»]
ProteinModelPortalQ9NVD7.
SMRQ9NVD7. Positions 246-372.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120860. 20 interactions.
IntActQ9NVD7. 11 interactions.
MINTMINT-1465264.
STRING9606.ENSP00000334008.

PTM databases

PhosphoSiteQ9NVD7.

Polymorphism databases

DMDM20139236.

Proteomic databases

MaxQBQ9NVD7.
PaxDbQ9NVD7.
PRIDEQ9NVD7.

Protocols and materials databases

DNASU55742.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000550549; ENSP00000447198; ENSG00000197702. [Q9NVD7-1]
GeneID55742.
KEGGhsa:55742.
UCSCuc001mkh.3. human. [Q9NVD7-2]

Organism-specific databases

CTD55742.
GeneCardsGC11P012398.
HGNCHGNC:14652. PARVA.
HPAHPA005964.
MIM608120. gene.
neXtProtNX_Q9NVD7.
PharmGKBPA32950.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG303418.
HOGENOMHOG000247027.
HOVERGENHBG053517.
InParanoidQ9NVD7.
KOK06275.
PhylomeDBQ9NVD7.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressQ9NVD7.
BgeeQ9NVD7.
CleanExHS_PARVA.
GenevestigatorQ9NVD7.

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

ChiTaRSPARVA. human.
EvolutionaryTraceQ9NVD7.
GeneWikiPARVA.
GenomeRNAi55742.
NextBio60703.
PROQ9NVD7.
SOURCESearch...

Entry information

Entry namePARVA_HUMAN
AccessionPrimary (citable) accession number: Q9NVD7
Secondary accession number(s): Q96C85, Q9HA48
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM