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Vasodilator-stimulated phosphoprotein (VASP)

 VASP_CANLF              Reviewed;         384 AA.
P50551;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 119.
RecName: Full=Vasodilator-stimulated phosphoprotein;
Short=VASP;
Name=VASP;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Cocker spaniel; TISSUE=Kidney;
PubMed=7828592;
Haffner C., Jarchau T., Reinhard M., Hoppe J., Lohmann S.M.,
Walter U.;
"Molecular cloning, structural analysis and functional expression of
the proline-rich focal adhesion and microfilament-associated protein
VASP.";
EMBO J. 14:19-27(1995).
[2]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-160 BY PKA.
PubMed=15096524; DOI=10.1083/jcb.200312118;
Koehler K., Louvard D., Zahraoui A.;
"Rab13 regulates PKA signaling during tight junction assembly.";
J. Cell Biol. 165:175-180(2004).
-!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved
in a range of processes dependent on cytoskeleton remodeling and
cell polarity such as axon guidance, lamellipodial and filopodial
dynamics, platelet activation and cell migration. VASP promotes
actin filament elongation. It protects the barbed end of growing
actin filaments against capping and increases the rate of actin
polymerization in the presence of capping protein. VASP stimulates
actin filament elongation by promoting the transfer of profilin-
bound actin monomers onto the barbed end of growing actin
filaments. Plays a role in actin-based mobility of Listeria
monocytogenes in host cells. Regulates actin dynamics in platelets
and plays an important role in regulating platelet aggregation (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Homotetramer. Interacts with PFN1, PFN2, LPP, ACTN1 and
ACTG1. Interacts, via the EVH1 domain, with the Pro-rich regions
of ZYX. This interaction is important for targeting to focal
adhesions and the formation of actin-rich structures at the apical
surface of cells. Interacts, via the EVH1 domain, with the Pro-
rich domain of Listeria monocytogenes actA. Interacts with
APBB1IP. Interacts, via the Pro-rich domain, with the C-terminal
SH3 domain of DNMBP. Interacts weakly with MEFV (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15096524}.
Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, focal
adhesion {ECO:0000250}. Cell junction, tight junction
{ECO:0000269|PubMed:15096524}. Cell projection, lamellipodium
membrane {ECO:0000250}. Cell projection, filopodium membrane
{ECO:0000250}. Note=Targeted to stress fibers and focal adhesions
through interaction with a number of proteins including MRL family
members. Localizes to the plasma membrane in protruding
lamellipodia and filopodial tips. Stimulation by thrombin or PMA,
also translocates VASP to focal adhesions. Localized along the
sides of actin filaments throughout the peripheral cytoplasm under
basal conditions. In pre-apoptotic cells, colocalizes with MEFV in
large specks (pyroptosomes) (By similarity). {ECO:0000250}.
-!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a
thymosin-like domain required for G-actin binding. The KLKR motif
within this block is essential for the G-actin binding and for
actin polymerization. Block B is required for F-actin binding and
subcellular location, and Block C for tetramerization.
-!- DOMAIN: The WH1 domain mediates interaction with XIRP1.
{ECO:0000250}.
-!- PTM: Major substrate for cAMP-dependent (PKA) and cGMP-dependent
protein kinase (PKG) in platelets. The preferred site for PKA is
Ser-160, the preferred site for PKG/PRKG1, Ser-242. In ADP-
activated platelets, phosphorylation by PKA or PKG on Ser-160
leads to fibrinogen receptor inhibition. Phosphorylation on Thr-
281 requires prior phosphorylation on Ser-160 and Ser-242. In
response to phorbol ester (PMA) stimulation, phosphorylated by
PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and
ROCK1. Phosphorylation at Thr-281 by AMPK does not require prior
phosphorylation at Ser-160 or Ser-242. Phosphorylation at Ser-160
by PKA is required for localization to the tight junctions in
epithelial cells. Phosphorylation modulates F-actin binding, actin
filament elongation and platelet activation. Phosphorylation at
Ser-326 by AMPK also alters actin filament binding. Carbon
monoxide (CO) promotes phosphorylation at Ser-160, while nitric
oxide (NO) promotes phosphorylation at Ser-160, but also at Ser-
242 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
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EMBL; Z46388; CAA86522.1; -; mRNA.
PIR; S51796; S51796.
RefSeq; NP_001003256.1; NM_001003256.1.
UniGene; Cfa.3797; -.
ProteinModelPortal; P50551; -.
SMR; P50551; -.
STRING; 9615.ENSCAFP00000006594; -.
iPTMnet; P50551; -.
PaxDb; P50551; -.
PRIDE; P50551; -.
GeneID; 403936; -.
KEGG; cfa:403936; -.
CTD; 7408; -.
eggNOG; KOG4590; Eukaryota.
eggNOG; ENOG41101TS; LUCA.
HOGENOM; HOG000013015; -.
HOVERGEN; HBG006655; -.
InParanoid; P50551; -.
KO; K06274; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR034367; VASP.
InterPro; IPR017354; VASP/EVL.
InterPro; IPR038023; VASP_sf.
InterPro; IPR014885; VASP_tetra.
InterPro; IPR000697; WH1/EVH1_dom.
PANTHER; PTHR11202:SF12; PTHR11202:SF12; 1.
Pfam; PF08776; VASP_tetra; 1.
Pfam; PF00568; WH1; 1.
PIRSF; PIRSF038010; Vasodilator_Phospo; 1.
SMART; SM00461; WH1; 1.
SUPFAM; SSF118370; SSF118370; 1.
PROSITE; PS50229; WH1; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; Cell junction; Cell membrane;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; Repeat;
SH3-binding; Tight junction.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P50552}.
CHAIN 2 384 Vasodilator-stimulated phosphoprotein.
/FTId=PRO_0000065766.
DOMAIN 2 113 WH1. {ECO:0000255|PROSITE-
ProRule:PRU00410}.
REPEAT 348 362 1.
REPEAT 363 377 2.
REGION 228 381 EVH2.
REGION 228 248 EVH2 block A.
REGION 262 281 EVH2 block B.
REGION 347 381 EVH2 block C.
REGION 348 377 2 X 15 AA tandem repeats of L-[EQ]-[KR]
[MV]-K-[EQ]-E-[IL]-[IL]-E-[AEV]-[FV]-
[KRV]-[KQ]-E.
COILED 344 377 {ECO:0000255}.
MOTIF 237 240 KLKR.
COMPBIAS 118 219 Pro-rich.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 39 39 Phosphotyrosine.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 160 160 Phosphoserine; by PKA, PKG/PRKG1, PKC and
ROCK1. {ECO:0000269|PubMed:15096524}.
MOD_RES 242 242 Phosphoserine; by PKA and PKG/PRKG1.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 281 281 Phosphothreonine; by PKA, PKG/PRKG1 and
AMPK. {ECO:0000250|UniProtKB:P50552}.
MOD_RES 286 286 N6-acetyllysine.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 320 320 Phosphothreonine.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 326 326 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000250|UniProtKB:P70460}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000250|UniProtKB:P70460}.
SEQUENCE 384 AA; 40413 MW; 266BB3C46FB4397F CRC64;
MSETVICSSW ATVMLYDDSN KRWLPAGTGP QSFSRVQIYH NPTANSFRVV GWKMQPDQQV
VINCAIVRGI KYNQATPTFH QWRDARQVWG LNFGSKEDAT QFAAAMASAL EALEGGGPPP
PPPPAAPPTW SVQNGPASEE VEQQKRQQPG PPEHLERRVS NAGGPPAPPA GGPPPPPGPP
PPPGPPPPPG VSLSGGSAAG HGAGGGPPPA PPLPTAQGTS GGGTGAPGLA AAIAGAKLRK
VSKQEEASGG PPVPKAESTR STGGGLMEEM NAMLARRRKA TQVGEKPPKD ESANEEPEAR
VPVPAQSETV RRPWEKNSTT LPRMKSSSSV TTSEAHPSTP SSSDESDLER VKQELLEEVR
KELQKVKEEI IEAFVQELRK RGSP


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