ID A0A3Q1LY87_BOVIN Unreviewed; 779 AA.
AC A0A3Q1LY87;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2025, entry version 31.
DE RecName: Full=Protein enabled homolog {ECO:0000256|ARBA:ARBA00072571};
GN Name=ENAH {ECO:0000313|Ensembl:ENSBTAP00000060596.1,
GN ECO:0000313|VGNC:VGNC:59333};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000060596.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000060596.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000060596.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000060596.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000060596.1};
RG Ensembl;
RL Submitted (MAR-2025) 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 and lamellipodial and filopodial
CC dynamics in migrating cells. ENAH induces the formation of F-actin rich
CC outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and
CC downstream of NTN1 to promote filipodia formation.
CC {ECO:0000256|ARBA:ARBA00056269}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Cell projection, filopodium
CC {ECO:0000256|ARBA:ARBA00004486}. Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family.
CC {ECO:0000256|ARBA:ARBA00009785}.
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DR AlphaFoldDB; A0A3Q1LY87; -.
DR Ensembl; ENSBTAT00000084831.2; ENSBTAP00000060596.1; ENSBTAG00000016185.7.
DR VEuPathDB; HostDB:ENSBTAG00000016185; -.
DR VGNC; VGNC:59333; ENAH.
DR GeneTree; ENSGT00940000157376; -.
DR OMA; XDILDEM; -.
DR OrthoDB; 31170at2759; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000016185; Expressed in gluteus medius and 110 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; 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 CDD; cd01207; EVH1_Ena_VASP-like; 1.
DR CDD; cd22185; WH2_hVASP-like; 1.
DR FunFam; 1.20.5.1160:FF:000003; protein enabled homolog isoform X2; 1.
DR FunFam; 2.30.29.30:FF:000047; vasodilator-stimulated phosphoprotein isoform X2; 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; IPR038023; VASP_sf.
DR InterPro; IPR014885; VASP_tetra.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR PANTHER; PTHR11202:SF1; PROTEIN ENABLED HOMOLOG; 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 PRINTS; PR01217; PRICHEXTENSN.
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 1: Evidence at protein level;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A3Q1LY87};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 1..111
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT REGION 115..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..397
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..418
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..439
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..450
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..481
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..652
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 84164 MW; E5FE81E9447F5DE6 CRC64;
MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI
NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQETGPTL
PRQNSQLPAQ VQNGPSQEEL EIQRRQLQEQ QRQKELERER LERERMERER MERERLERER
LERERLEQEQ LERERQERER QDRLERERQE RERLERLDRE RQERERQEQL EREQLEWERE
RRISNAAPSS DSSLYSAPLP EYASCQPPSA PPPSYAKVIS APVSEATPEY AVVTALPPTS
TPPTPPLRHP ATRFATSLGS AFHPVLPHYA TVPRPLNKNS RPSSPVNTPS PQPPATKPCA
WPTPNFSPLP PSPPVMISSP PGKATGPRPV LPVCVSSPVP PMPPSPTAPS GLLDSVPHPV
SPPPTSGPAA PPPPPPLPSL APLSHCGSQA SPPPPPSTPL ASTPSSKPSV LPSPSAAAPA
SVETPLNSVL GDSSAPEPGL QAASQPAETP AQQGIVLGPP APPPPPPLPP GPAQAPAILP
PPPGPPPPPP LPSSGPPPPP PPPPLPNQVP PPPPPPPAPP LPASGFFSGS MSEDNRPLTG
LAAAIAGAKL RKVSRMEDAS FPSGGNTTGV NSASSKTDTG RGNGPLPLGG SGLMEEMSAL
LARRRRIAEK GSTIETEQKE DKNEDSEPVT SKASSTTTPE PIRKPWERTN TMNGSKSPVI
SRPKSAPSSQ PSANGVQTEG LDYDRLKQDI LDEMRKELTK LKEELIDAIR QELSKSNTA
//
