CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014441
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Villin-1 
Protein Synonyms/Alias
  
Gene Name
 Vil1 
Gene Synonyms/Alias
 Vil 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
237LGPRKELKAAISDSVubiquitination[1]
250SVVEPAAKAALKLYHubiquitination[1]
264HVSDSEGKLVVREVAubiquitination[1]
281PLTQDLLKHEDCYILubiquitination[1]
320SQALNFIKAKQYPPSubiquitination[1]
506YQGGTSRKNNLEPVPubiquitination[1]
529GTNADNTKAFEVTARubiquitination[1]
672HANEEEKKAAATTVQubiquitination[1]
683TTVQEYLKTHPGNRDubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Epithelial cell-specific Ca(2+)-regulated actin- modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination. 
Sequence Annotation
 REPEAT 27 76 Gelsolin-like 1.
 REPEAT 148 188 Gelsolin-like 2.
 REPEAT 265 309 Gelsolin-like 3.
 REPEAT 407 457 Gelsolin-like 4.
 REPEAT 528 568 Gelsolin-like 5.
 REPEAT 631 672 Gelsolin-like 6.
 DOMAIN 761 827 HP.
 REGION 2 734 Core.
 REGION 2 126 Necessary for homodimerization (By
 REGION 112 119 LPA/PIP2-binding site 1 (By similarity).
 REGION 138 146 LPA/PIP2-binding site 2 (By similarity).
 REGION 735 827 Headpiece.
 REGION 816 824 LPA/PIP2-binding site 3 (By similarity).  
Keyword
 Actin capping; Actin-binding; Apoptosis; Calcium; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Metal-binding; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 827 AA 
Protein Sequence
MTKLNAQVKG SLNITTPGIQ IWRIEAMQMV PVPSSTFGSF FDGDCYVVLA IHKTSSTLSY 60
DIHYWIGQDS SQDEQGAAAI YTTQMDDYLK GRAVQHREVQ GNESETFRSY FKQGLVIRKG 120
GVASGMKHVE TNSCDVQRLL HVKGKRNVLA GEVEMSWKSF NRGDVFLLDL GKLIIQWNGP 180
ESNRMERLRG MALAKEIRDQ ERGGRTYVGV VDGEKEGDSP QLMAIMNHVL GPRKELKAAI 240
SDSVVEPAAK AALKLYHVSD SEGKLVVREV ATRPLTQDLL KHEDCYILDQ GGLKIFVWKG 300
KNANAQERSG AMSQALNFIK AKQYPPSTQV EVQNDGAESP IFQQLFQKWT VPNRTSGLGK 360
THTVGSVAKV EQVKFDALTM HVQPQVAAQQ KMVDDGSGEV QVWRIEDLEL VPVESKWLGH 420
FYGGDCYLLL YTYLIGEKQH YLLYIWQGSQ ASQDEIAASA YQAVLLDQKY NDEPVQIRVT 480
MGKEPPHLMS IFKGRMVVYQ GGTSRKNNLE PVPSTRLFQV RGTNADNTKA FEVTARATSL 540
NSNDVFILKT PSCCYLWCGK GCSGDEREMA KMVADTISRT EKQVVVEGQE PANFWMALGG 600
KAPYANTKRL QEENQVITPR LFECSNQTGR FLATEIFDFN QDDLEEEDVF LLDVWDQVFF 660
WIGKHANEEE KKAAATTVQE YLKTHPGNRD LETPIIVVKQ GHEPPTFTGW FLAWDPFKWS 720
NTKSYDDLKA ELGNSGDWSQ IADEVMSPKV DVFTANTSLS SGPLPTFPLE QLVNKSVEDL 780
PEGVDPSRKE EHLSTEDFTR ALGMTPAAFS ALPRWKQQNI KKEKGLF 827 
Gene Ontology
 GO:0032432; C:actin filament bundle; ISS:UniProtKB.
 GO:0005903; C:brush border; TAS:MGI.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0032433; C:filopodium tip; IDA:UniProtKB.
 GO:0030027; C:lamellipodium; IDA:UniProtKB.
 GO:0005902; C:microvillus; ISS:UniProtKB.
 GO:0001726; C:ruffle; ISS:UniProtKB.
 GO:0051015; F:actin filament binding; ISS:UniProtKB.
 GO:0005509; F:calcium ion binding; ISS:UniProtKB.
 GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
 GO:0035727; F:lysophosphatidic acid binding; ISS:UniProtKB.
 GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
 GO:0051693; P:actin filament capping; ISS:UniProtKB.
 GO:0030042; P:actin filament depolymerization; ISS:UniProtKB.
 GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
 GO:0051014; P:actin filament severing; IEA:Compara.
 GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
 GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:UniProtKB.
 GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; IEA:Compara.
 GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
 GO:0032233; P:positive regulation of actin filament bundle assembly; ISS:UniProtKB.
 GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
 GO:0051125; P:regulation of actin nucleation; ISS:UniProtKB.
 GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
 GO:2000392; P:regulation of lamellipodium morphogenesis; IDA:UniProtKB.
 GO:0061041; P:regulation of wound healing; IDA:UniProtKB.
 GO:0009617; P:response to bacterium; IEA:Compara. 
Interpro
 IPR007123; Gelsolin_dom.
 IPR015627; Villin.
 IPR007122; Villin/Gelsolin.
 IPR003128; Villin_headpiece. 
Pfam
 PF00626; Gelsolin
 PF02209; VHP 
SMART
 SM00262; GEL 
PROSITE
 PS51089; HP 
PRINTS
 PR00597; GELSOLIN.