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Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein-like)

 EVL_MOUSE               Reviewed;         414 AA.
P70429; Q9ERU8;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
15-NOV-2002, sequence version 2.
12-SEP-2018, entry version 153.
RecName: Full=Ena/VASP-like protein;
AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like;
Name=Evl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=8861907; DOI=10.1016/S0092-8674(00)81341-0;
Gertler F.B., Niebuhr K., Reinhard M., Wehland J., Soriano P.;
"Mena, a relative of VASP and Drosophila Enabled, is implicated in the
control of microfilament dynamics.";
Cell 87:227-239(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
PFN2; LYN; APBB1; ABL1 AND SRC, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND PHOSPHORYLATION BY PKA.
STRAIN=C57BL/6J;
PubMed=10945997; DOI=10.1074/jbc.M006274200;
Lambrechts A., Kwiatkowski A.V., Lanier L.M., Bear J.E.,
Vandekerckhove J., Ampe C., Gertler F.B.;
"cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP
relative, regulates its interaction with actin and SH3 domains.";
J. Biol. Chem. 275:36143-36151(2000).
[3]
ROLE IN L.MONOCYTOGENES MOBILITY, MISCELLANEOUS, AND INTERACTION WITH
L.MONOCYTOGENES ACTA.
PubMed=10087267; DOI=10.1083/jcb.144.6.1245;
Laurent V., Loisel T.P., Harbeck B., Wehman A., Groebe L.,
Jockusch B.M., Wehland J., Gertler F.B., Carlier M.-F.;
"Role of proteins of the Ena/VASP family in actin-based motility of
Listeria monocytogenes.";
J. Cell Biol. 144:1245-1258(1999).
[4]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=10069337; DOI=10.1016/S0896-6273(00)81092-2;
Lanier L.M., Gates M.A., Witke W., Menzies A.S., Wehman A.M.,
Macklis J.D., Kwiatkowski D., Soriano P., Gertler F.B.;
"Mena is required for neurulation and commissure formation.";
Neuron 22:313-325(1999).
[5]
INTERACTION WITH SEMA6A.
PubMed=10993894; DOI=10.1074/jbc.M006316200;
Klostermann A., Lutz B., Gertler F., Behl C.;
"The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-
1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-
like protein (EVL) via a novel carboxyl-terminal zyxin-like domain.";
J. Biol. Chem. 275:39647-39653(2000).
[6]
INTERACTION WITH DNMBP.
PubMed=14506234; DOI=10.1074/jbc.M308104200;
Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
"Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
domains, links dynamin to regulation of the actin cytoskeleton.";
J. Biol. Chem. 278:49031-49043(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329 AND SER-367, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-130 IN COMPLEX WITH A
SYNTHETIC PRO-RICH PEPTIDE.
PubMed=10404224; DOI=10.1038/10717;
Fedorov A.A., Fedorov E., Gertler F., Almo S.C.;
"Structure of EVH1, a novel proline-rich ligand-binding module
involved in cytoskeletal dynamics and neural function.";
Nat. Struct. Biol. 6:661-665(1999).
-!- 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 and lamellipodial and
filopodial dynamics in migrating cells. EVL enhances actin
nucleation and polymerization. {ECO:0000269|PubMed:10087267,
ECO:0000269|PubMed:10945997}.
-!- SUBUNIT: Homotetramer (By similarity). Binds to the SH3 domains of
ABL1, LYN and SRC (PubMed:10945997). Also binds to profilin, with
preference for isoform IIa of PFN2, and the WW domain of
APBB1/FE65 (PubMed:10945997). Binds to SEMA6A (PubMed:10993894).
Interacts, via the Pro-rich region, with the C-terminal SH3 domain
of DNMBP (PubMed:14506234). Interacts with RAPH1 (By similarity).
Binds, via the EVH1 domain, the Pro-rich domain of Listeria
monocytogenes actA (PubMed:10087267). Binds, via the EVH1 domain,
the Pro-rich domain of ZYX. Interacts with FYB1. Interacts with
ZDHHC17 (By similarity). {ECO:0000250|UniProtKB:Q9UI08,
ECO:0000269|PubMed:10087267, ECO:0000269|PubMed:10404224,
ECO:0000269|PubMed:10945997, ECO:0000269|PubMed:10993894,
ECO:0000269|PubMed:14506234}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:10945997}. Cytoplasm, cytoskeleton, stress
fiber {ECO:0000269|PubMed:10945997}. Cell projection,
lamellipodium {ECO:0000269|PubMed:10945997}. Note=Targeted to the
leading edge of lamellipodia and the distal tip of stress fibers
through interaction with a number of proteins. In activated T-
cells, localizes to the F-actin collar and the distal tip of
microspikes. {ECO:0000269|PubMed:10945997}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2; Synonyms=EVL-I;
IsoId=P70429-1; Sequence=Displayed;
Name=1;
IsoId=P70429-2; Sequence=VSP_004045;
-!- TISSUE SPECIFICITY: Highest expression in thymus and spleen (at
protein level). Low levels in placenta, ovary, testis, fat and
lung (at protein level). Isoform 1 and isoform 2 are expressed in
cortical neurons and glial cells. {ECO:0000269|PubMed:10069337,
ECO:0000269|PubMed:10945997}.
-!- DEVELOPMENTAL STAGE: At an early stage, highly expressed in the
branchial and pharyngeal arches, but not in the brain. Expression
in the brain starts at 15 dpc (at protein level).
{ECO:0000269|PubMed:10069337}.
-!- 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.
-!- PTM: Phosphorylated by PKA; phosphorylation abolishes binding to
SH3 domains of ABL and SRC. {ECO:0000269|PubMed:10945997}.
-!- MISCELLANEOUS: Required to transform actin polymerization into
active movement for the propulsive force of Listeria
monocytogenes.
-!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U72519; AAC52862.1; -; mRNA.
EMBL; AF279662; AAG23653.1; -; mRNA.
CCDS; CCDS26161.1; -. [P70429-2]
CCDS; CCDS49167.1; -. [P70429-1]
RefSeq; NP_001156866.1; NM_001163394.1. [P70429-1]
RefSeq; NP_031991.3; NM_007965.3. [P70429-2]
UniGene; Mm.238841; -.
PDB; 1QC6; X-ray; 2.60 A; A/B=1-130.
PDBsum; 1QC6; -.
ProteinModelPortal; P70429; -.
SMR; P70429; -.
BioGrid; 199547; 2.
DIP; DIP-40886N; -.
ELM; P70429; -.
IntAct; P70429; 2.
STRING; 10090.ENSMUSP00000021689; -.
iPTMnet; P70429; -.
PhosphoSitePlus; P70429; -.
MaxQB; P70429; -.
PaxDb; P70429; -.
PRIDE; P70429; -.
Ensembl; ENSMUST00000021689; ENSMUSP00000021689; ENSMUSG00000021262. [P70429-1]
Ensembl; ENSMUST00000077735; ENSMUSP00000076916; ENSMUSG00000021262. [P70429-2]
GeneID; 14026; -.
KEGG; mmu:14026; -.
UCSC; uc007ozv.1; mouse. [P70429-2]
UCSC; uc007ozw.1; mouse. [P70429-1]
CTD; 51466; -.
MGI; MGI:1194884; Evl.
eggNOG; ENOG410KD2J; Eukaryota.
eggNOG; ENOG410YM7V; LUCA.
GeneTree; ENSGT00730000110272; -.
HOGENOM; HOG000013015; -.
HOVERGEN; HBG006655; -.
InParanoid; P70429; -.
OMA; STQRQVQ; -.
OrthoDB; EOG091G0QTE; -.
PhylomeDB; P70429; -.
TreeFam; TF321411; -.
Reactome; R-MMU-376176; Signaling by ROBO receptors.
Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
EvolutionaryTrace; P70429; -.
PRO; PR:P70429; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000021262; Expressed in 287 organ(s), highest expression level in brain.
CleanEx; MM_EVL; -.
ExpressionAtlas; P70429; baseline and differential.
Genevisible; P70429; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005522; F:profilin binding; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB.
GO; GO:0030048; P:actin filament-based movement; NAS:UniProtKB.
GO; GO:0045010; P:actin nucleation; NAS:UniProtKB.
GO; GO:0008154; P:actin polymerization or depolymerization; IDA:UniProtKB.
GO; GO:0007411; P:axon guidance; NAS:UniProtKB.
GO; GO:0051016; P:barbed-end actin filament capping; NAS:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:MGI.
GO; GO:1900028; P:negative regulation of ruffle assembly; ISO:MGI.
GO; GO:0030168; P:platelet activation; NAS:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR034319; ENA/VASP-like_protein.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR017354; VASP/EVL.
InterPro; IPR038023; VASP_sf.
InterPro; IPR014885; VASP_tetra.
InterPro; IPR000697; WH1/EVH1_dom.
PANTHER; PTHR11202:SF4; PTHR11202:SF4; 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;
3D-structure; Actin-binding; Alternative splicing; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein;
Reference proteome; SH3-binding.
CHAIN 1 414 Ena/VASP-like protein.
/FTId=PRO_0000087105.
DOMAIN 1 112 WH1. {ECO:0000255|PROSITE-
ProRule:PRU00410}.
REGION 220 411 EVH2.
REGION 220 240 EVH2 block A.
REGION 263 280 EVH2 block B.
REGION 340 360 Required for interaction with ZDHHC17.
{ECO:0000250|UniProtKB:Q9UI08}.
REGION 377 411 EVH2 block C.
MOTIF 229 232 KLKR.
COMPBIAS 160 204 Pro-rich.
MOD_RES 130 130 Phosphoserine.
{ECO:0000250|UniProtKB:O08719}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000250|UniProtKB:O08719}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 339 339 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 339 359 Missing (in isoform 1).
{ECO:0000303|PubMed:8861907}.
/FTId=VSP_004045.
STRAND 4 17 {ECO:0000244|PDB:1QC6}.
TURN 18 21 {ECO:0000244|PDB:1QC6}.
STRAND 22 25 {ECO:0000244|PDB:1QC6}.
STRAND 34 41 {ECO:0000244|PDB:1QC6}.
TURN 42 45 {ECO:0000244|PDB:1QC6}.
STRAND 46 52 {ECO:0000244|PDB:1QC6}.
TURN 54 56 {ECO:0000244|PDB:1QC6}.
STRAND 59 64 {ECO:0000244|PDB:1QC6}.
STRAND 70 75 {ECO:0000244|PDB:1QC6}.
STRAND 78 82 {ECO:0000244|PDB:1QC6}.
STRAND 87 93 {ECO:0000244|PDB:1QC6}.
HELIX 95 111 {ECO:0000244|PDB:1QC6}.
SEQUENCE 414 AA; 44337 MW; 146A018BCD6CA370 CRC64;
MSEQSICQAR ASVMVYDDTS KKWVPIKPGQ QGFSRINIYH NTASSTFRVV GVKLQDQQVV
INYSIVKGLK YNQATPTFHQ WRDARQVYGL NFASKEEATT FSNAMLFALN IMNSQEGGPS
TQRQVQNGPS PEEMDIQRRQ VMEQQHRQES LERRISATGP ILPPGHPSSA ASTTLSCSGP
PPPPPPPVPP PPTGSTPPPP PPLPAGGAQG TNHDESSASG LAAALAGAKL RRVQRPEDAS
GGSSPSGTSK SDANRASSGG GGGGLMEEMN KLLAKRRKAA SQTDKPADRK EDESQTEDPS
TSPSPGTRAT SQPPNSSEAG RKPWERSNSV EKPVSSLLSR TPSVAKSPEA KSPLQSQPHS
RVKPAGSVND VGLDALDLDR MKQEILEEVV RELHKVKEEI IDAIRQELSG ISTT


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