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

 EVL_PONAB               Reviewed;         422 AA.
Q5R896;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
28-MAR-2018, entry version 80.
RecName: Full=Ena/VASP-like protein;
AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like;
Name=EVL;
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homotetramer (By similarity). Binds to the SH3 domains of
ABL1, LYN and SRC. Also binds to profilin, with preference for
isoform IIa of PFN2, and the WW domain of APBB1/FE65. Binds to
SEMA6A. Interacts, via the Pro-rich region, with the C-terminal
SH3 domain of DNMBP. Interacts with RAPH1. Binds, via the EVH1
domain, the Pro-rich domain of Listeria monocytogenes actA (By
similarity). Binds, via the EVH1 domain, the Pro-rich domain of
ZYX. Interacts with FYB1. Interacts with ZDHHC17 (By similarity).
{ECO:0000250|UniProtKB:P70429, ECO:0000250|UniProtKB:Q9UI08}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P70429}. Cell projection, lamellipodium
{ECO:0000250|UniProtKB:P70429}. Note=Targeted to the leading edge
of lamellipodia and the dital 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:0000250|UniProtKB:P70429}.
-!- 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:0000250}.
-!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
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EMBL; CR859858; CAH92014.1; -; mRNA.
RefSeq; NP_001126168.1; NM_001132696.1.
UniGene; Pab.2210; -.
ProteinModelPortal; Q5R896; -.
SMR; Q5R896; -.
STRING; 9601.ENSPPYP00000006977; -.
PRIDE; Q5R896; -.
Ensembl; ENSPPYT00000007252; ENSPPYP00000006977; ENSPPYG00000006138.
GeneID; 100173130; -.
KEGG; pon:100173130; -.
CTD; 51466; -.
eggNOG; ENOG410IQ1Z; Eukaryota.
eggNOG; ENOG410YM7V; LUCA.
GeneTree; ENSGT00730000110272; -.
HOVERGEN; HBG006655; -.
InParanoid; Q5R896; -.
OMA; STQRQVQ; -.
OrthoDB; EOG091G0QTE; -.
TreeFam; TF321411; -.
Proteomes; UP000001595; Chromosome 14.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005522; F:profilin binding; IEA:Ensembl.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0045010; P:actin nucleation; IEA:InterPro.
GO; GO:0008154; P:actin polymerization or depolymerization; IEA:Ensembl.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0010633; P:negative regulation of epithelial cell migration; IEA:Ensembl.
GO; GO:1900028; P:negative regulation of ruffle assembly; IEA:Ensembl.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
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.
2: Evidence at transcript level;
Actin-binding; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome;
SH3-binding.
CHAIN 1 422 Ena/VASP-like protein.
/FTId=PRO_0000227758.
DOMAIN 4 118 WH1. {ECO:0000255|PROSITE-
ProRule:PRU00410}.
REGION 228 419 EVH2.
REGION 228 248 EVH2 block A.
REGION 271 288 EVH2 block B.
REGION 348 368 Required for interaction with ZDHHC17.
{ECO:0000250|UniProtKB:Q9UI08}.
REGION 385 419 EVH2 block C.
COILED 388 414 {ECO:0000255}.
MOTIF 237 240 KLKR.
COMPBIAS 168 212 Pro-rich.
COMPBIAS 267 272 Poly-Gly.
MOD_RES 136 136 Phosphoserine.
{ECO:0000250|UniProtKB:O08719}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000250|UniProtKB:O08719}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 312 312 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 360 360 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UI08}.
SEQUENCE 422 AA; 45314 MW; ACB6E9F6CBA77D99 CRC64;
MFAFEEFSEQ SICQARASVM VYDDTSKKWV PIKPGQQGFS RINIYHNTAS NTFRVVGVKL
QDQQVVINYS IVKGLKYNQA TPTFHQWRDA RQVYGLNFAS KEEATTFSNA MLFALNIMNS
QEGGPSSQRQ VQNGPSPDEM DIQRRQVMEQ HQQQRQESLE RRTSATGPIL PPGHPSSAAS
APVSCSGPPP PPPPPVPPPP TGATPPPPPP LPAGGAQGSS HDESSVSGLA AAIAGAKLRR
VQRPEDASGG SSPSGTSKSD ANRASSGGGG GGLMEEMNKL LAKRRKAASQ SDKPAEKKED
ESQTEDPSTS PSPGTRAASQ PPNSSEAGRK PWERSNSVEK PVSSILSRTP SVAKSPEAKS
PLQSQPHSRM KPAGSVNDMA LDAFDLDRMK QEILEEVVRE LHKVKDEIID AIRQELSGIS
TT


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