ID M3XED8_FELCA Unreviewed; 420 AA.
AC M3XED8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Ena/VASP-like protein {ECO:0000256|ARBA:ARBA00017156};
DE AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like {ECO:0000256|ARBA:ARBA00033193};
GN Name=EVL {ECO:0000313|Ensembl:ENSFCAP00000024995.2,
GN ECO:0000313|VGNC:VGNC:61991};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000024995.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000024995.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000024995.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000024995.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000024995.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000024995.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000024995.2};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a
CC range of processes dependent on cytoskeleton remodeling and cell
CC polarity such as axon guidance, lamellipodial and filopodial dynamics,
CC platelet activation and cell migration.
CC {ECO:0000256|PIRNR:PIRNR038010}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000256|ARBA:ARBA00004529}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family.
CC {ECO:0000256|ARBA:ARBA00009785, ECO:0000256|PIRNR:PIRNR038010}.
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DR EMBL; AANG04004659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003988072.2; XM_003988023.4.
DR AlphaFoldDB; M3XED8; -.
DR Ensembl; ENSFCAT00000030493.4; ENSFCAP00000024995.2; ENSFCAG00000025054.4.
DR GeneID; 101080297; -.
DR KEGG; fca:101080297; -.
DR CTD; 51466; -.
DR VGNC; VGNC:61991; EVL.
DR eggNOG; KOG4590; Eukaryota.
DR GeneTree; ENSGT00940000157826; -.
DR HOGENOM; CLU_017790_0_0_1; -.
DR OrthoDB; 2884005at2759; -.
DR Proteomes; UP000011712; Chromosome B3.
DR Bgee; ENSFCAG00000025054; Expressed in embryonic head and 9 other cell types or tissues.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:UniProtKB-UniRule.
DR GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
DR CDD; cd01207; EVH1_Ena_VASP-like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR017354; VASP/EVL.
DR InterPro; IPR038023; VASP_sf.
DR InterPro; IPR014885; VASP_tetra.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR PANTHER; PTHR11202:SF4; ENA_VASP-LIKE PROTEIN; 1.
DR PANTHER; PTHR11202; SPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 1.
DR Pfam; PF08776; VASP_tetra; 1.
DR Pfam; PF00568; WH1; 1.
DR PIRSF; PIRSF038010; Vasodilator_Phospo; 1.
DR SMART; SM00461; WH1; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF118370; Vasodilator-stimulated phosphoprotein, VASP, tetramerisation domain; 1.
DR PROSITE; PS50229; WH1; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW ECO:0000256|PIRNR:PIRNR038010};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273,
KW ECO:0000256|PIRNR:PIRNR038010};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR038010};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR038010};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 1..114
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT REGION 143..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..212
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 44817 MW; BE1B003E545679ED CRC64;
MATGEQSICQ ARASVMVYDD TSKKWVPIKA GQQGFSRINI YHNTASNTFR VVGVKLQDQQ
VVINYSIVKG LKYNQATPTF HQWRDARQVY GLNFASKEEA TTFSNAMLFA LNIMNSQEGG
PSTQRQVQNG PSPDEMDIQR RQVMEQTQHQ QQRQESLERR TSATGPILPP GHPSSAASAP
LSCSGPPPPP PPPVPPPPAG ATPPPPPPLP AGGAQGASHD ESSVSGLAAA LAGAKLRRVQ
RPEDASGGSS PSGTSKSDAN RASSGGGGGG LMEEMNKLLA KRRKAASQTD KPADKKEDES
QTEELSTSPS PGTRAASQPP NSSEAGRKPW ERSNSVEKPV SSLLSRTPSV AKSPEAKSPL
QAQPHSRMKP VGGVNDVALD ALDLDRMKQE ILEEVVRELH KVKEEIIDAI RQELSGISTS
//
