ID G3REI7_GORGO Unreviewed; 827 AA.
AC G3REI7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Villin-1 {ECO:0000256|ARBA:ARBA00017436};
GN Name=VIL1 {ECO:0000313|Ensembl:ENSGGOP00000013974.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000013974.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000013974.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000013974.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000013974.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, filopodium tip
CC {ECO:0000256|ARBA:ARBA00004495}. Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}. Cell projection, microvillus
CC {ECO:0000256|ARBA:ARBA00004105}. Cell projection, ruffle
CC {ECO:0000256|ARBA:ARBA00004466}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family.
CC {ECO:0000256|ARBA:ARBA00008418}.
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DR EMBL; CABD030018661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004033253.1; XM_004033205.2.
DR AlphaFoldDB; G3REI7; -.
DR STRING; 9593.ENSGGOP00000013974; -.
DR Ensembl; ENSGGOT00000014377.3; ENSGGOP00000013974.2; ENSGGOG00000014322.3.
DR GeneID; 101126593; -.
DR KEGG; ggo:101126593; -.
DR CTD; 7429; -.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000160544; -.
DR HOGENOM; CLU_002568_3_1_1; -.
DR InParanoid; G3REI7; -.
DR OMA; EMFFLVF; -.
DR OrthoDB; 25995at2759; -.
DR TreeFam; TF313468; -.
DR Proteomes; UP000001519; Chromosome 2B.
DR Bgee; ENSGGOG00000014322; Expressed in adult mammalian kidney and 1 other cell type or tissue.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0032432; C:actin filament bundle; IEA:Ensembl.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032433; C:filopodium tip; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0035727; F:lysophosphatidic acid binding; IEA:Ensembl.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:Ensembl.
DR GO; GO:0030041; P:actin filament polymerization; IEA:Ensembl.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR GO; GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0001951; P:intestinal D-glucose absorption; IEA:Ensembl.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IEA:Ensembl.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IEA:Ensembl.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; IEA:Ensembl.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0051125; P:regulation of actin nucleation; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:2000392; P:regulation of lamellipodium morphogenesis; IBA:GO_Central.
DR GO; GO:0032532; P:regulation of microvillus length; IEA:Ensembl.
DR GO; GO:0061041; P:regulation of wound healing; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:1902896; P:terminal web assembly; IEA:Ensembl.
DR CDD; cd11290; gelsolin_S1_like; 1.
DR CDD; cd11289; gelsolin_S2_like; 1.
DR CDD; cd11292; gelsolin_S3_like; 1.
DR CDD; cd11293; gelsolin_S4_like; 1.
DR CDD; cd11288; gelsolin_S5_like; 1.
DR CDD; cd11291; gelsolin_S6_like; 1.
DR Gene3D; 3.40.20.10; Severin; 6.
DR Gene3D; 1.10.950.10; Villin headpiece domain; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR007122; Villin/Gelsolin.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR PANTHER; PTHR11977; VILLIN; 1.
DR PANTHER; PTHR11977:SF35; VILLIN-1; 1.
DR Pfam; PF00626; Gelsolin; 6.
DR Pfam; PF02209; VHP; 1.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF55753; Actin depolymerizing proteins; 4.
DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 2.
DR SUPFAM; SSF47050; VHP, Villin headpiece domain; 1.
DR PROSITE; PS51089; HP; 1.
PE 3: Inferred from homology;
KW Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT DOMAIN 761..827
FT /note="HP"
FT /evidence="ECO:0000259|PROSITE:PS51089"
SQ SEQUENCE 827 AA; 92756 MW; 83360696D0FE4CA0 CRC64;
MTKLSAQVKG SLNITTPGLQ IWRIEAMQMV PVPSSTFGSF FDGDCYIILA IHKTASNLSY
DIHYWIGQDS SLDEQGAAAI YTTQMDDFLK GRAVQHREVQ GNESEAFRGY FKQGLVIRKG
GVASGMKQVE TNSYDVQRLL HVKGKRNVVA GEVEMSWKSF NRGDVFLLDL GKLIIQWNGP
ESNRMERLRG MTLAKEIRDQ ERGGRTYVGV VDGENELASP KLMEVMNHVL GKRRELKAAV
PDTVVEPALK AALKLYHVSD SEGNLVVREV ATRPLTQDLL SHEDCYILDQ GGLKIYVWKG
KKANEQEKKG AMSHALNFIK AKQYPQSTQV EVQNDGAESA VFQQLFQKWT ASNRTSGLGK
THTVGSVAKV EQVKFDATSM HVKPQVAAQQ KMVDDGSGEV QVWRIENLEL VPVDSKWLGH
FYGGDCYLLL YTYLIGEKQH YLLYVWQGSQ ASQDEITASA YQAVILDQKY NGEPVQIRVP
MGKEPPHLMS IFKGRMVVYQ GGTSRTNNLE PGPSTRLFQV QGTGTNNTKA FEVPARASFL
NSNDVFVLKT QSCCYLWCGK GCSGDEREMA KMVADTISRT EKQVVVEGQE PANFWMALGG
KAPYANTKRL QEENLVITPR LFECSNKTGR FLATEIPDFN QDDLEEDDVF LLDVWDQVFF
WIGKHANEEE KKAAATTAQE YLKTHPSGRD PETPIIVVKQ GHEPPTFTGW FLAWDPFKWS
NTKSYEDLKA ELGNSRDWSQ ITAEVTSPKV DVFNANSNLS SGPLPIFPLE QLVNKPVEEL
PEGVDPSRKE EHLSIEDFTQ AFGMTPAAFS ALPRWKQQNL KKEKGLF
//
