Search Results

Overview

Uniprot IDP09327
Protein NameVillin-1
Gene NameVIL1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
232 VMNHVLGKRRELKAA
254 PALKAALKLYHVSDS
3 *****MTKLSAQVKG
360 NRTSGLGKTHTVGSV
369 HTVGSVAKVEQVKFD
374 VAKVEQVKFDATSMH
627 RLFECSNKTGRFLAT

Function

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

Protein Sequence

10 MTKLSAQVKG 20 SLNITTPGLQ 30 IWRIEAMQMV 40 PVPSSTFGSF 50 FDGDCYIILA 60 IHKTASSLSY 70 DIHYWIGQDS 80 SLDEQGAAAI 90 YTTQMDDFLK 100 GRAVQHREVQ 110 GNESEAFRGY 120 FKQGLVIRKG 130 GVASGMKHVE 140 TNSYDVQRLL 150 HVKGKRNVVA 160 GEVEMSWKSF 170 NRGDVFLLDL 180 GKLIIQWNGP 190 ESTRMERLRG 200 MTLAKEIRDQ 210 ERGGRTYVGV 220 VDGENELASP 230 KLMEVMNHVL 240 GKRRELKAAV 250 PDTVVEPALK 260 AALKLYHVSD 270 SEGNLVVREV 280 ATRPLTQDLL 290 SHEDCYILDQ 300 GGLKIYVWKG 310 KKANEQEKKG 320 AMSHALNFIK 330 AKQYPPSTQV 340 EVQNDGAESA 350 VFQQLFQKWT 360 ASNRTSGLGK 370 THTVGSVAKV 380 EQVKFDATSM 390 HVKPQVAAQQ 400 KMVDDGSGEV 410 QVWRIENLEL 420 VPVDSKWLGH 430 FYGGDCYLLL 440 YTYLIGEKQH 450 YLLYVWQGSQ 460 ASQDEITASA 470 YQAVILDQKY 480 NGEPVQIRVP 490 MGKEPPHLMS 500 IFKGRMVVYQ 510 GGTSRTNNLE 520 TGPSTRLFQV 530 QGTGANNTKA 540 FEVPARANFL 550 NSNDVFVLKT 560 QSCCYLWCGK 570 GCSGDEREMA 580 KMVADTISRT 590 EKQVVVEGQE 600 PANFWMALGG 610 KAPYANTKRL 620 QEENLVITPR 630 LFECSNKTGR 640 FLATEIPDFN 650 QDDLEEDDVF 660 LLDVWDQVFF 670 WIGKHANEEE 680 KKAAATTAQE 690 YLKTHPSGRD 700 PETPIIVVKQ 710 GHEPPTFTGW 720 FLAWDPFKWS 730 NTKSYEDLKA 740 ELGNSRDWSQ 750 ITAEVTSPKV 760 DVFNANSNLS 770 SGPLPIFPLE 780 QLVNKPVEEL 790 PEGVDPSRKE 800 EHLSIEDFTQ 810 AFGMTPAAFS 820 ALPRWKQQNL KKEKGLF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Biological Process GO:0040018 positive regulation of multicellular organism growth
Biological Process GO:1903078 positive regulation of protein localization to plasma membrane
Biological Process GO:0065003 protein-containing complex assembly
Biological Process GO:0051125 regulation of actin nucleation
Biological Process GO:0008360 regulation of cell shape
Biological Process GO:2000392 regulation of lamellipodium morphogenesis
Biological Process GO:0032532 regulation of microvillus length
Biological Process GO:0061041 regulation of wound healing
Biological Process GO:0009617 response to bacterium
Biological Process GO:1902896 terminal web assembly
Cellular Component GO:0032432 actin filament bundle
Cellular Component GO:0005903 brush border
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0030175 filopodium
Cellular Component GO:0032433 filopodium tip
Cellular Component GO:0030027 lamellipodium
Cellular Component GO:0005902 microvillus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0001726 ruffle
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0043027 cysteine-type endopeptidase inhibitor activity involved in apoptotic process
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0035727 lysophosphatidic acid binding
Molecular Function GO:0005546 phosphatidylinositol-4,5-bisphosphate binding
Molecular Function GO:0042803 protein homodimerization activity
Biological Process GO:0051693 actin filament capping
Biological Process GO:0030042 actin filament depolymerization
Biological Process GO:0030041 actin filament polymerization
Biological Process GO:0051014 actin filament severing
Biological Process GO:0008154 actin polymerization or depolymerization
Biological Process GO:0006915 apoptotic process
Biological Process GO:0051016 barbed-end actin filament capping
Biological Process GO:0071364 cellular response to epidermal growth factor stimulus
Biological Process GO:0035729 cellular response to hepatocyte growth factor stimulus
Biological Process GO:0060327 cytoplasmic actin-based contraction involved in cell motility
Biological Process GO:0007173 epidermal growth factor receptor signaling pathway
Biological Process GO:0030855 epithelial cell differentiation
Biological Process GO:0001951 intestinal D-glucose absorption
Biological Process GO:0032233 positive regulation of actin filament bundle assembly
Biological Process GO:0030836 positive regulation of actin filament depolymerization
Biological Process GO:0030335 positive regulation of cell migration
Biological Process GO:0010634 positive regulation of epithelial cell migration
Biological Process GO:2000394 positive regulation of lamellipodium morphogenesis

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.