PARVA_MOUSE
ID PARVA_MOUSE Reviewed; 372 AA.
AC Q9EPC1; Q9JJ65;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Alpha-parvin;
DE AltName: Full=Actopaxin;
GN Name=Parva; Synonyms=Actp; ORFNames=MNCb-0301;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11171322; DOI=10.1242/jcs.114.3.525;
RA Olski T.M., Noegel A.A., Korenbaum E.;
RT "Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin
RT superfamily.";
RL J. Cell Sci. 114:525-538(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH ACTIN; PXN AND TGFB1I1.
RX PubMed=11134073; DOI=10.1083/jcb.151.7.1435;
RA Nikolopoulos S.N., Turner C.E.;
RT "Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and
RT actin and regulates cell adhesion.";
RL J. Cell Biol. 151:1435-1448(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH ARHGAP31.
RX PubMed=16860736; DOI=10.1016/j.cub.2006.05.057;
RA LaLonde D.P., Grubinger M., Lamarche-Vane N., Turner C.E.;
RT "CdGAP associates with actopaxin to regulate integrin-dependent changes in
RT cell morphology and motility.";
RL Curr. Biol. 16:1375-1385(2006).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19798050; DOI=10.1038/emboj.2009.295;
RA Montanez E., Wickstrom S.A., Altstatter J., Chu H., Fassler R.;
RT "Alpha-parvin controls vascular mural cell recruitment to vessel wall by
RT regulating RhoA/ROCK signalling.";
RL EMBO J. 28:3132-3144(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-8; SER-14 AND SER-19, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in sarcomere organization and in smooth muscle
CC cell contraction. Required for normal development of the embryonic
CC cardiovascular system, and for normal septation of the heart outflow
CC tract. Plays a role in sprouting angiogenesis and is required for
CC normal adhesion of vascular smooth muscle cells to endothelial cells
CC during blood vessel development. Plays a role in the reorganization of
CC the actin cytoskeleton, formation of lamellipodia and ciliogenesis.
CC Plays a role in the establishment of cell polarity, cell adhesion, cell
CC spreading, and directed cell migration. {ECO:0000269|PubMed:11134073,
CC ECO:0000269|PubMed:19798050}.
CC -!- SUBUNIT: Interacts with TGFB1I1 (PubMed:11134073). Interacts with LIMS1
CC (via LD motifs) (By similarity). Interacts with ARHGAP31
CC (PubMed:16860736). Interacts with the actin cytoskeleton
CC (PubMed:11134073). Interacts (via C-terminus) with ILK (By similarity).
CC Interacts (via C-terminus) with TESK1 (via C-terminus); the interaction
CC inhibits TESK1 kinase activity (By similarity). Interacts with
CC PXN/PAXILLIN (via LD motif 4) (PubMed:11134073).
CC {ECO:0000250|UniProtKB:Q9NVD7, ECO:0000269|PubMed:11134073,
CC ECO:0000269|PubMed:16860736}.
CC -!- INTERACTION:
CC Q9EPC1; O55222: Ilk; NbExp=7; IntAct=EBI-6690233, EBI-6690138;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton.
CC Cytoplasm, myofibril, sarcomere, Z line. Note=Constituent of focal
CC adhesions.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality, due to severe cardiovascular
CC defects causing whole body edema and severe bleeding due to vessel
CC rupture. Embryos show defects in the septation of the heart outflow
CC tract. Their cardiomyocytes are round and fail to align in a parallel
CC manner. Blood vessels are frequently enlarged and show numerous
CC microaneurisms. Besides, blood vessels show abnormal constrictions and
CC increased vascular sprouting. Vascular mural cells and pericytes
CC display a rounded shape and impaired adhesion to the underlying
CC vascular endothelium. Cells display highly dynamic formation of
CC membrane ruffles with increased random motility, but impaired
CC chemotaxis. {ECO:0000269|PubMed:19798050}.
CC -!- SIMILARITY: Belongs to the parvin family. {ECO:0000305}.
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DR EMBL; AF237774; AAG27175.1; -; mRNA.
DR EMBL; AF264766; AAG09803.1; -; mRNA.
DR EMBL; AB045321; BAA97981.1; -; mRNA.
DR EMBL; BC059236; AAH59236.1; -; mRNA.
DR CCDS; CCDS40091.1; -.
DR RefSeq; NP_065631.3; NM_020606.5.
DR AlphaFoldDB; Q9EPC1; -.
DR BMRB; Q9EPC1; -.
DR SMR; Q9EPC1; -.
DR BioGRID; 208263; 14.
DR CORUM; Q9EPC1; -.
DR DIP; DIP-57658N; -.
DR IntAct; Q9EPC1; 3.
DR MINT; Q9EPC1; -.
DR STRING; 10090.ENSMUSP00000033030; -.
DR iPTMnet; Q9EPC1; -.
DR PhosphoSitePlus; Q9EPC1; -.
DR jPOST; Q9EPC1; -.
DR MaxQB; Q9EPC1; -.
DR PaxDb; Q9EPC1; -.
DR PeptideAtlas; Q9EPC1; -.
DR PRIDE; Q9EPC1; -.
DR ProteomicsDB; 287996; -.
DR Antibodypedia; 993; 458 antibodies from 32 providers.
DR DNASU; 57342; -.
DR Ensembl; ENSMUST00000033030; ENSMUSP00000033030; ENSMUSG00000030770.
DR Ensembl; ENSMUST00000106643; ENSMUSP00000102254; ENSMUSG00000030770.
DR GeneID; 57342; -.
DR KEGG; mmu:57342; -.
DR UCSC; uc009jgt.1; mouse.
DR CTD; 55742; -.
DR MGI; MGI:1931144; Parva.
DR VEuPathDB; HostDB:ENSMUSG00000030770; -.
DR eggNOG; KOG3631; Eukaryota.
DR GeneTree; ENSGT00950000183194; -.
DR InParanoid; Q9EPC1; -.
DR OrthoDB; 871306at2759; -.
DR PhylomeDB; Q9EPC1; -.
DR TreeFam; TF314025; -.
DR Reactome; R-MMU-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR Reactome; R-MMU-446353; Cell-extracellular matrix interactions.
DR Reactome; R-MMU-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR BioGRID-ORCS; 57342; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Parva; mouse.
DR PRO; PR:Q9EPC1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9EPC1; protein.
DR Bgee; ENSMUSG00000030770; Expressed in superior cervical ganglion and 261 other tissues.
DR ExpressionAtlas; Q9EPC1; baseline and differential.
DR Genevisible; Q9EPC1; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0070252; P:actin-mediated cell contraction; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:UniProtKB.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0071670; P:smooth muscle cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR028433; Parvin.
DR PANTHER; PTHR12114; PTHR12114; 1.
DR Pfam; PF00307; CH; 2.
DR PIRSF; PIRSF039131; Parvin; 1.
DR SMART; SM00033; CH; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 2.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Angiogenesis; Cell adhesion; Cell junction;
KW Cell membrane; Cell shape; Chemotaxis; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19131326"
FT CHAIN 2..372
FT /note="Alpha-parvin"
FT /id="PRO_0000121581"
FT DOMAIN 95..202
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 262..369
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..25
FT /note="Interaction with ARHGAP31"
FT /evidence="ECO:0000269|PubMed:16860736"
FT REGION 223..372
FT /note="Required for interaction with TESK1 and ILK"
FT /evidence="ECO:0000250|UniProtKB:Q9NVD7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVD7"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVD7"
FT CONFLICT 33
FT /note="L -> H (in Ref. 3; BAA97981)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="F -> S (in Ref. 3; BAA97981)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 42330 MW; 1251F2586A1ACBC6 CRC64;
MATSPQKSPL VPKSPTPKSP PSRKKDDSFL GKLGGTLARR KKAKEVSEFQ EEGMNAINLP
LSPISFELDP EDTLLEENEV RTMVDPNSRN DPKLQELMKV LIDWINDVLV GERIIVKDLA
EDLYDGQVLQ KLFEKLESEK LNVAEVTQSE IAQKQKLQTV LEKINETLKL PPRSIKWNVD
SVHAKNLVAI LHLLVALSQY FRAPIRLPDH VSIQVVVVQK REGILQSRQI QEEITGNTEA
LSGRHERDAF DTLFDHAPDK LNVVKKTLIT FVNKHLNKLN LEVTELETQF ADGVYLVLLM
GLLEGYFVPL HSFFLTPDSF EQKVLNVSFA FELMQDGGLE KPKPRPEDIV NCDLKSTLRV
LYNLFTKYRN VE
