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 27-MAR-2024, entry version 152. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000023072; -. DR ProteomicsDB; 294160; -. DR Pumba; Q9ES46; -. DR Antibodypedia; 27615; 274 antibodies from 27 providers. DR DNASU; 170736; -. DR Ensembl; ENSMUST00000023072.7; ENSMUSP00000023072.7; ENSMUSG00000022438.7. DR GeneID; 170736; -. DR KEGG; mmu:170736; -. DR UCSC; uc007xby.1; mouse. DR AGR; MGI:2153063; -. 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; HKFHLAP; -. DR OrthoDB; 1328998at2759; -. 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 76 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 205 other cell types or tissues. DR ExpressionAtlas; Q9ES46; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; ISO:MGI. 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:0030036; P:actin cytoskeleton organization; 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 CDD; cd21336; CH_PARVB_rpt1; 1. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR028433; Parvin. DR PANTHER; PTHR12114:SF7; BETA-PARVIN; 1. DR PANTHER; PTHR12114; PARVIN; 1. DR Pfam; PF00307; CH; 2. DR PIRSF; PIRSF039131; Parvin; 1. DR SMART; SM00033; CH; 2. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR PROSITE; PS50021; CH; 2. DR Genevisible; Q9ES46; MM. 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 //