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Database: UniProt
Entry: A0A3Q1LSS3_BOVIN
LinkDB: A0A3Q1LSS3_BOVIN
Original site: A0A3Q1LSS3_BOVIN 
ID   A0A3Q1LSS3_BOVIN        Unreviewed;       370 AA.
AC   A0A3Q1LSS3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Vasodilator stimulated phosphoprotein {ECO:0000313|Ensembl:ENSBTAP00000060074.1};
GN   Name=VASP {ECO:0000313|Ensembl:ENSBTAP00000060074.1,
GN   ECO:0000313|VGNC:VGNC:36769};
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:ENSBTAP00000060074.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000060074.1, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000060074.1,
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:ENSBTAP00000060074.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000060074.1};
RG   Ensembl;
RL   Submitted (NOV-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
CC       {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR038010}.
CC   -!- SIMILARITY: Belongs to the Ena/VASP family.
CC       {ECO:0000256|ARBA:ARBA00009785, ECO:0000256|PIRNR:PIRNR038010}.
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DR   RefSeq; XP_005219323.1; XM_005219266.3.
DR   RefSeq; XP_005219324.1; XM_005219267.3.
DR   AlphaFoldDB; A0A3Q1LSS3; -.
DR   Ensembl; ENSBTAT00000068531.1; ENSBTAP00000060074.1; ENSBTAG00000019604.6.
DR   GeneID; 514902; -.
DR   CTD; 7408; -.
DR   VEuPathDB; HostDB:ENSBTAG00000019604; -.
DR   VGNC; VGNC:36769; VASP.
DR   GeneTree; ENSGT00940000156765; -.
DR   OMA; TSEAHPC; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000019604; Expressed in neutrophil and 106 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q1LSS3; baseline and differential.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005856; C:cytoskeleton; 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   CDD; cd22185; WH2_hVASP-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; SPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR11202:SF12; VASODILATOR-STIMULATED PHOSPHOPROTEIN; 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   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|PeptideAtlas:A0A3Q1LSS3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          1..100
FT                   /note="WH1"
FT                   /evidence="ECO:0000259|PROSITE:PS50229"
FT   REGION          99..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..118
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..179
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   370 AA;  39098 MW;  D6FE18099003F2CF CRC64;
     MLYDDSNKRW LPAGTGPQAF SRVQIYHNPT ANSFRVVGRK MQPDQQVVIN CAIVRGVKYN
     QATPNFHQWR DARQVWGLNF GSKEDATQFA NGMASALEAL EGGGPLPPPP PTAPPTWSAQ
     NGPSPEEMEQ QKRQQQSELM ERERRASNAG GPPAASAGAP PPPPGPPPPP GPPPPPGLSS
     SGVSAATQGA GGGPPPAPPL PTAQGPSGGG TGAPSLASAI AGAKLRKVSK QEEASAGPVA
     PKAESSRSTG GGLMEEMNAM LARRRKATQV GEKPAKDESA NQEESDARVP AHSESVRRPW
     EKNSTTLPRM KSSSSVTTSE AHPATPSSSD ESDLERVKQE LLEEVRKELQ KVKEEIIEAF
     VQELRKRGAP
//
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