VASP_BOVIN
ID VASP_BOVIN Reviewed; 383 AA.
AC Q2TA49;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Vasodilator-stimulated phosphoprotein;
DE Short=VASP;
GN Name=VASP;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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. VASP promotes actin filament
CC elongation. It protects the barbed end of growing actin filaments
CC against capping and increases the rate of actin polymerization in the
CC presence of capping protein. VASP stimulates actin filament elongation
CC by promoting the transfer of profilin-bound actin monomers onto the
CC barbed end of growing actin filaments. Plays a role in actin-based
CC mobility of Listeria monocytogenes in host cells. Regulates actin
CC dynamics in platelets and plays an important role in regulating
CC platelet aggregation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. Interacts with PFN1, PFN2, LPP, ACTN1 and ACTG1.
CC Interacts, via the EVH1 domain, with the Pro-rich regions of ZYX. This
CC interaction is important for targeting to focal adhesions and the
CC formation of actin-rich structures at the apical surface of cells.
CC Interacts, via the EVH1 domain, with the Pro-rich domain of Listeria
CC monocytogenes actA. Interacts with APBB1IP. Interacts, via the Pro-rich
CC domain, with the C-terminal SH3 domain of DNMBP. Interacts weakly with
CC MEFV (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Cell junction, focal adhesion {ECO:0000250}. Cell junction, tight
CC junction {ECO:0000250}. Cell projection, lamellipodium membrane
CC {ECO:0000250}. Cell projection, filopodium membrane {ECO:0000250}.
CC Note=Targeted to stress fibers and focal adhesions through interaction
CC with a number of proteins including MRL family members. Localizes to
CC the plasma membrane in protruding lamellipodia and filopodial tips.
CC Stimulation by thrombin or PMA, also translocates VASP to focal
CC adhesions. Localized along the sides of actin filaments throughout the
CC peripheral cytoplasm under basal conditions. In pre-apoptotic cells,
CC colocalizes with MEFV in large specks (pyroptosomes) (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a
CC thymosin-like domain required for G-actin binding. The KLKR motif
CC within this block is essential for the G-actin binding and for actin
CC polymerization. Block B is required for F-actin binding and subcellular
CC location, and Block C for tetramerization.
CC -!- DOMAIN: The WH1 domain mediates interaction with XIRP1. {ECO:0000250}.
CC -!- PTM: Major substrate for cAMP-dependent (PKA) and cGMP-dependent
CC protein kinase (PKG) in platelets. The preferred site for PKA is Ser-
CC 160, the preferred site for PKG/PRKG1, Ser-242. In ADP-activated
CC platelets, phosphorylation by PKA or PKG on Ser-160 leads to fibrinogen
CC receptor inhibition. Phosphorylation on Thr-281 requires prior
CC phosphorylation on Ser-160 and Ser-242. In response to phorbol ester
CC (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to
CC thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-
CC 281 by AMPK does not require prior phosphorylation at Ser-160 or Ser-
CC 242. Phosphorylation at Ser-160 by PKA is required for localization to
CC the tight junctions in epithelial cells. Phosphorylation modulates F-
CC actin binding, actin filament elongation and platelet activation.
CC Phosphorylation at Ser-325 by AMPK also alters actin filament binding.
CC Carbon monoxide (CO) promotes phosphorylation at Ser-160, while nitric
CC oxide (NO) promotes phosphorylation at Ser-160, but also at Ser-242 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
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DR EMBL; BC111116; AAI11117.1; -; mRNA.
DR RefSeq; NP_001033199.1; NM_001038110.2.
DR AlphaFoldDB; Q2TA49; -.
DR SMR; Q2TA49; -.
DR IntAct; Q2TA49; 1.
DR STRING; 9913.ENSBTAP00000026119; -.
DR PaxDb; Q2TA49; -.
DR PeptideAtlas; Q2TA49; -.
DR PRIDE; Q2TA49; -.
DR Ensembl; ENSBTAT00000026119; ENSBTAP00000026119; ENSBTAG00000019604.
DR GeneID; 514902; -.
DR KEGG; bta:514902; -.
DR CTD; 7408; -.
DR VEuPathDB; HostDB:ENSBTAG00000019604; -.
DR VGNC; VGNC:36769; VASP.
DR eggNOG; KOG4590; Eukaryota.
DR GeneTree; ENSGT00940000156765; -.
DR HOGENOM; CLU_017790_0_0_1; -.
DR InParanoid; Q2TA49; -.
DR OMA; TSEAHPC; -.
DR OrthoDB; 972128at2759; -.
DR TreeFam; TF321411; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000019604; Expressed in neutrophil and 106 other tissues.
DR ExpressionAtlas; Q2TA49; baseline and differential.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005522; F:profilin binding; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0001843; P:neural tube closure; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR034367; VASP.
DR InterPro; IPR017354; VASP/EVL.
DR InterPro; IPR038023; VASP_sf.
DR InterPro; IPR014885; VASP_tetra.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR PANTHER; PTHR11202:SF12; PTHR11202:SF12; 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; SSF118370; SSF118370; 1.
DR PROSITE; PS50229; WH1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; SH3-binding; Tight junction.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P50552"
FT CHAIN 2..383
FT /note="Vasodilator-stimulated phosphoprotein"
FT /id="PRO_0000227759"
FT DOMAIN 2..113
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REPEAT 347..361
FT /note="1"
FT REPEAT 362..376
FT /note="2"
FT REGION 112..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..380
FT /note="EVH2"
FT REGION 228..248
FT /note="EVH2 block A"
FT REGION 262..281
FT /note="EVH2 block B"
FT REGION 346..380
FT /note="EVH2 block C"
FT REGION 347..361
FT /note="2 X 15 AA tandem repeats of L-[EQ]-[KR] [MV]-K-[EQ]-
FT E-[IL]-[IL]-E-[AEV]-[FV]-[KRV]-[KQ]-E"
FT COILED 343..376
FT /evidence="ECO:0000255"
FT MOTIF 237..240
FT /note="KLKR"
FT COMPBIAS 116..131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..192
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P50552"
FT MOD_RES 39
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P50552"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50552"
FT MOD_RES 160
FT /note="Phosphoserine; by PKA, PKG/PRKG1, PKC and ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P50551"
FT MOD_RES 242
FT /note="Phosphoserine; by PKA and PKG/PRKG1"
FT /evidence="ECO:0000250|UniProtKB:P50552"
FT MOD_RES 281
FT /note="Phosphothreonine; by PKA, PKG/PRKG1 and AMPK"
FT /evidence="ECO:0000250|UniProtKB:P50552"
FT MOD_RES 286
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50552"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50552"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50552"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P50552"
FT MOD_RES 325
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:P50552"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70460"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70460"
SQ SEQUENCE 383 AA; 40463 MW; 991EF24796BAACE0 CRC64;
MSETVVCTSR ATVMLYDDSN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV GRKMQPDQQV
VINCAIVRGV KYNQATPNFH QWRDARQVWG LNFGSKEDAT QFANGMASAL EALEGGGPLP
PPPPTAPPTW SAQNGPSPEE MEQQKRQQQS ELMERERRAS NAGGPPAASA GAPPPPPGPP
PPPGPPPPPG LSSSGVSAAT QGAGGGPPPA PPLPTAQGPS GGGTGAPSLA SAIAGAKLRK
VSKQEEASAG PVAPKAESSR STGGGLMEEM NAMLARRRKA TQVGEKPAKD ESANQEESDA
RVPAHSESVR RPWEKNSTTL PRMKSSSSVT TSEAHPATPS SSDESDLERV KQELLEEVRK
ELQKVKEEII EAFVQELRKR GAP
