ID G1KE69_ANOCA Unreviewed; 862 AA.
AC G1KE69;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Villin like {ECO:0000313|Ensembl:ENSACAP00000005395.3};
GN Name=VILL {ECO:0000313|Ensembl:ENSACAP00000005395.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000005395.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000005395.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000005395.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000005395.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family.
CC {ECO:0000256|ARBA:ARBA00008418}.
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DR RefSeq; XP_008110418.1; XM_008112211.2.
DR AlphaFoldDB; G1KE69; -.
DR STRING; 28377.ENSACAP00000005395; -.
DR Ensembl; ENSACAT00000005512.4; ENSACAP00000005395.3; ENSACAG00000005301.4.
DR GeneID; 100567463; -.
DR KEGG; acs:100567463; -.
DR CTD; 50853; -.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000160253; -.
DR HOGENOM; CLU_002568_3_1_1; -.
DR InParanoid; G1KE69; -.
DR OrthoDB; 25995at2759; -.
DR TreeFam; TF313468; -.
DR Proteomes; UP000001646; Chromosome 6.
DR Bgee; ENSACAG00000005301; Expressed in kidney and 13 other cell types or tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
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 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:SF30; VILLIN-LIKE PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000001646}.
FT DOMAIN 796..862
FT /note="HP"
FT /evidence="ECO:0000259|PROSITE:PS51089"
FT REGION 749..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 97015 MW; A5FF595D0867ACC3 CRC64;
MTDAEADVGL PTIERKPGLQ IWTIEKMKMV PVPEKAYGSF FEGDCYIIVN NTKTRTGFAT
DLHYWIGRES SQDEQGAAAF YVTQLDDLLG GNPVQHREVQ GHESAAFKSY FKKGIIYKKG
GVASGFKHVE TNMYNVKRLL HVKGKKHVTA TEVDLSWNSF NQGDVFLLDL GKVIIQWNGP
SCNVAEKSRG MVLARSIRDG ERGGRAQIGI VDDEKDSVDL MQIMKAALGE RQGELSPALP
DEKADELQKA NVRLYHVYEN GKDLVVQEIA TRPLTQDLLR HEDCHILDQG GFKIYVWRGK
DSSKEEKKAA FSRAVGFIQA KGYPASTNVE VINDGAESAM FKQLFQKWTG KDETHGLGKA
YSVNKIAKVD QVKFDITQLH ARPELAAEQR MADDASGTVE VWRIENLEMV PVSPKTYGQF
YGGDCYLVLY TYIKSGRPHY IIYMWLGRHA SVDEVTACAF NAVELDRKYN DEPVQVRVMM
GKEPRHFLAI FKGNLIIYEG GTSRAEKTEP EPAVRLFQVR GADEFNTKTI EVPARASSLN
SNDVFLLKTN QVCYLWCGKG CSGDEREMAK NVADTISKRD KQTILEGQEP ADFWAALGGK
APYASDKRFQ EEVAHYQPRL FECSNQTGRF IMTEIMDFGQ DDLDEDDVML LDTWEEIFLW
IGKGSNSYEK SEAISSARDY LKTHPAGRDQ ATSIIMVKQG HEPLNFTGWF TAWDPYKWSD
GKTYEEMKSS LGNVSAISEI TVDLKNANLS NKNTSNKPTV TNSAASRTGT TLPTHQTNPD
KSNSNYNNSN APLLQTGGNG VFARDLLINK AVDELPEGVD PTQKERYLSD EDFYDIFGKT
RDEFYQMPKW KQQNEKKQHG IF
//
