Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alpha-parvin

Gene

Parva

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

GO - Molecular functioni

  • actin binding Source: UniProtKB-KW
  • protein domain specific binding Source: RGD

GO - Biological processi

Keywordsi

Molecular functionActin-binding
Biological processAngiogenesis, Cell adhesion, Cell shape, Chemotaxis, Cilium biogenesis/degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-parvin
Alternative name(s):
Actopaxin
Gene namesi
Name:Parva
Synonyms:Actp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71021 Parva

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001215822 – 372Alpha-parvinAdd BLAST371

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei8PhosphoserineBy similarity1
Modified residuei14PhosphoserineBy similarity1
Modified residuei19PhosphoserineCombined sources1
Modified residuei28PhosphoserineBy similarity1
Modified residuei62PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9HB97
PRIDEiQ9HB97

PTM databases

iPTMnetiQ9HB97
PhosphoSitePlusiQ9HB97

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Interactioni

Subunit structurei

Interacts with ARHGAP31. Interacts with TGFB1I1. Interacts with ILK, LIMS1 and PXN (via LD motifs). Interacts with the actin cytoskeleton.1 Publication

GO - Molecular functioni

  • actin binding Source: UniProtKB-KW
  • protein domain specific binding Source: RGD

Protein-protein interaction databases

BioGridi248617, 1 interactor
IntActiQ9HB97, 2 interactors
STRINGi10116.ENSRNOP00000021671

Structurei

3D structure databases

ProteinModelPortaliQ9HB97
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini95 – 202Calponin-homology (CH) 1PROSITE-ProRule annotationAdd BLAST108
Domaini262 – 369Calponin-homology (CH) 2PROSITE-ProRule annotationAdd BLAST108

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 25Interaction with ARHGAP31By similarity5

Sequence similaritiesi

Belongs to the parvin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3631 Eukaryota
ENOG410XQWH LUCA
HOGENOMiHOG000247027
HOVERGENiHBG053517
InParanoidiQ9HB97
KOiK06275
PhylomeDBiQ9HB97

Family and domain databases

Gene3Di1.10.418.10, 2 hits
InterProiView protein in InterPro
IPR001715 CH-domain
IPR036872 CH_dom_sf
IPR028433 Parvin
PANTHERiPTHR12114 PTHR12114, 1 hit
PfamiView protein in Pfam
PF00307 CH, 2 hits
PIRSFiPIRSF039131 Parvin, 1 hit
SMARTiView protein in SMART
SM00033 CH, 2 hits
SUPFAMiSSF47576 SSF47576, 2 hits
PROSITEiView protein in PROSITE
PS50021 CH, 2 hits

Sequencei

Sequence statusi: Complete.

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

Q9HB97-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSPQKSPS VPKSPTPKSP PSRKKDDSFL GKLGGTLARR KKAKEVSEFQ
60 70 80 90 100
EEGMNAINLP LSPISFELDP EDTMLEENEV RTMVDPNSRN DPKLQELMKV
110 120 130 140 150
LIDWINDVLV GERIIVKDLA EDLYDGQVLQ KLFEKLESEK LNVAEVTQSE
160 170 180 190 200
IAQKQKLQTV LEKINEALKL 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):42,292
Last modified:June 1, 2001 - v2
Checksum:i7AAD24EBC25D094C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF264765 mRNA Translation: AAG09802.2
RefSeqiNP_065707.2, NM_020656.2
UniGeneiRn.92564

Genome annotation databases

GeneIDi57341
KEGGirno:57341
UCSCiRGD:71021 rat

Similar proteinsi

Entry informationi

Entry nameiPARVA_RAT
AccessioniPrimary (citable) accession number: Q9HB97
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: May 23, 2018
This is version 117 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health