PARVB_MOUSE
ID PARVB_MOUSE Reviewed; 365 AA.
AC Q9ES46;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Beta-parvin;
GN Name=Parvb;
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 TISSUE SPECIFICITY.
RX PubMed=11722847; DOI=10.1016/s0378-1119(01)00743-0;
RA Korenbaum E., Olski T.M., Noegel A.A.;
RT "Genomic organization and expression profile of the parvin family of focal
RT adhesion proteins in mice and humans.";
RL Gene 279:69-79(2001).
RN [3]
RP INTERACTION WITH DYSF.
RX PubMed=15835269; DOI=10.1093/jnen/64.4.334;
RA Matsuda C., Kameyama K., Tagawa K., Ogawa M., Suzuki A., Yamaji S.,
RA Okamoto H., Nishino I., Hayashi Y.K.;
RT "Dysferlin interacts with affixin (beta-parvin) at the sarcolemma.";
RL J. Neuropathol. Exp. Neurol. 64:334-340(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, 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: Adapter protein that plays a role in integrin signaling via
CC ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange
CC factors, such as ARHGEF6. Is involved in the reorganization of the
CC actin cytoskeleton and formation of lamellipodia. Plays a role in cell
CC adhesion, cell spreading, establishment or maintenance of cell
CC polarity, and cell migration (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ILK, ARHGEF6, PXN (via LD motifs), ACTN2 and
CC actin (By similarity). Interacts with DYSF. {ECO:0000250,
CC ECO:0000269|PubMed:15835269}.
CC -!- INTERACTION:
CC Q9ES46; Q9ES28: Arhgef7; NbExp=2; IntAct=EBI-6914996, EBI-642580;
CC Q9ES46; Q64691: Capn3; NbExp=3; IntAct=EBI-6914996, EBI-21927513;
CC Q9ES46; O55222: Ilk; NbExp=3; IntAct=EBI-6914996, EBI-6690138;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC projection, lamellipodium {ECO:0000250}. Cytoplasm, myofibril,
CC sarcomere {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250}. Note=Constituent of focal adhesions. Detected at the
CC tips of the leading edge of cells. Colocalizes with F-actin at the tips
CC of lamellipodia (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in heart and moderately in
CC spleen, lung and skeletal muscle. {ECO:0000269|PubMed:11722847}.
CC -!- PTM: Phosphorylated by ILK. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the parvin family. {ECO:0000305}.
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DR EMBL; AF237770; AAG27172.1; -; mRNA.
DR CCDS; CCDS37167.1; -.
DR RefSeq; NP_573395.1; NM_133167.3.
DR AlphaFoldDB; Q9ES46; -.
DR SMR; Q9ES46; -.
DR BioGRID; 228403; 2.
DR DIP; DIP-57659N; -.
DR IntAct; Q9ES46; 3.
DR MINT; Q9ES46; -.
DR STRING; 10090.ENSMUSP00000023072; -.
DR iPTMnet; Q9ES46; -.
DR PhosphoSitePlus; Q9ES46; -.
DR jPOST; Q9ES46; -.
DR MaxQB; Q9ES46; -.
DR PaxDb; Q9ES46; -.
DR PRIDE; Q9ES46; -.
DR ProteomicsDB; 294160; -.
DR Antibodypedia; 27615; 228 antibodies from 27 providers.
DR DNASU; 170736; -.
DR Ensembl; ENSMUST00000023072; ENSMUSP00000023072; ENSMUSG00000022438.
DR GeneID; 170736; -.
DR KEGG; mmu:170736; -.
DR UCSC; uc007xby.1; mouse.
DR CTD; 29780; -.
DR MGI; MGI:2153063; Parvb.
DR VEuPathDB; HostDB:ENSMUSG00000022438; -.
DR eggNOG; KOG3631; Eukaryota.
DR GeneTree; ENSGT00950000183194; -.
DR HOGENOM; CLU_047624_2_0_1; -.
DR InParanoid; Q9ES46; -.
DR OMA; GWPLRWN; -.
DR OrthoDB; 871306at2759; -.
DR PhylomeDB; Q9ES46; -.
DR TreeFam; TF314025; -.
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; 170736; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Parvb; mouse.
DR PRO; PR:Q9ES46; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9ES46; protein.
DR Bgee; ENSMUSG00000022438; Expressed in blood and 202 other tissues.
DR ExpressionAtlas; Q9ES46; baseline and differential.
DR Genevisible; Q9ES46; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0030031; P:cell projection assembly; ISS:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; ISS:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
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 Actin-binding; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..365
FT /note="Beta-parvin"
FT /id="PRO_0000121584"
FT DOMAIN 88..195
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 255..362
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBI1"
SQ SEQUENCE 365 AA; 41669 MW; A3C6B8B3D5875CEA CRC64;
MSSAPPRSPT PRAPKMKKDE SFLGKLGGTL ARKKKTREVT DLQEEGKSAI NSPMAPALVD
IHPEDTQLEE NEERTMIDPT SREDPKFKEL VKVLLDWIND VLAEERIIVK QLEEDLYDGQ
VLQKLLEKLA HCKLNVAEVT QSEIGQKQKL QTVLEAVQDL LRPHGWPLRW NVDSIHGKNL
VAILHLLVSL AMHFRAPIHL PEHVTVQVVV VRKREGLLHS SHISEELTTT TEIMMGRFER
DAFDTLFDHA PDKLNLVKKS LITFVNKHLN KLNLEVTDLE TQFADGVYLV LLLGLLEDYF
VPLHNFYLTP DSFDQKVHNV AFAFELMLDG GLKKPKARPE DVVNLDLKST LRVLYTLFTK
YKDVE
