EVL_PONAB
ID EVL_PONAB Reviewed; 422 AA.
AC Q5R896;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Ena/VASP-like protein;
DE AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like;
GN Name=EVL;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 and lamellipodial and filopodial
CC dynamics in migrating cells. EVL enhances actin nucleation and
CC polymerization (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer (By similarity). Binds to the SH3 domains of
CC ABL1, LYN and SRC. Also binds to profilin, with preference for isoform
CC IIa of PFN2, and the WW domain of APBB1/FE65. Binds to SEMA6A.
CC Interacts, via the Pro-rich region, with the C-terminal SH3 domain of
CC DNMBP. Interacts with RAPH1. Binds, via the EVH1 domain, the Pro-rich
CC domain of Listeria monocytogenes actA (By similarity). Binds, via the
CC EVH1 domain, the Pro-rich domain of ZYX. Interacts with FYB1. Interacts
CC with ZDHHC17 (By similarity). {ECO:0000250|UniProtKB:P70429,
CC ECO:0000250|UniProtKB:Q9UI08}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P70429}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:P70429}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P70429}. Note=Targeted to the leading edge of
CC lamellipodia and the distal tip of stress fibers through interaction
CC with a number of proteins. In activated T-cells, localizes to the F-
CC actin collar and the distal tip of microspikes.
CC {ECO:0000250|UniProtKB:P70429}.
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 -!- PTM: Phosphorylated by PKA; phosphorylation abolishes binding to SH3
CC domains of ABL and SRC. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
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DR EMBL; CR859858; CAH92014.1; -; mRNA.
DR RefSeq; NP_001126168.1; NM_001132696.1.
DR AlphaFoldDB; Q5R896; -.
DR SMR; Q5R896; -.
DR STRING; 9601.ENSPPYP00000006977; -.
DR Ensembl; ENSPPYT00000007252; ENSPPYP00000006977; ENSPPYG00000006138.
DR GeneID; 100173130; -.
DR KEGG; pon:100173130; -.
DR CTD; 51466; -.
DR eggNOG; KOG4590; Eukaryota.
DR GeneTree; ENSGT00940000157826; -.
DR HOGENOM; CLU_017790_0_0_1; -.
DR InParanoid; Q5R896; -.
DR OMA; RTHYGIN; -.
DR OrthoDB; 972128at2759; -.
DR TreeFam; TF321411; -.
DR Proteomes; UP000001595; Chromosome 14.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; 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:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR034319; ENA/VASP-like_protein.
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:SF4; PTHR11202:SF4; 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 Actin-binding; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; SH3-binding.
FT CHAIN 1..422
FT /note="Ena/VASP-like protein"
FT /id="PRO_0000227758"
FT DOMAIN 4..118
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REGION 120..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..419
FT /note="EVH2"
FT REGION 228..248
FT /note="EVH2 block A"
FT REGION 271..288
FT /note="EVH2 block B"
FT REGION 348..368
FT /note="Required for interaction with ZDHHC17"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT REGION 385..419
FT /note="EVH2 block C"
FT COILED 388..414
FT /evidence="ECO:0000255"
FT MOTIF 237..240
FT /note="KLKR"
FT COMPBIAS 184..214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08719"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08719"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI08"
SQ 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
