EVL_XENLA
ID EVL_XENLA Reviewed; 692 AA.
AC Q64GL0; Q64GL1; Q64GL2;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Ena/VASP-like protein;
DE AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like;
GN Name=evl {ECO:0000250|UniProtKB:P70429};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAU20373.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:15661649};
RX PubMed=15661649; DOI=10.1016/j.modgep.2004.09.004;
RA Wanner S.J., Danos M.C., Lohr J.L., Miller J.R.;
RT "Molecular cloning and expression of Ena/Vasp-like (Evl) during Xenopus
RT development.";
RL Gene Expr. Patterns 5:423-428(2005).
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 -!- 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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3 {ECO:0000269|PubMed:15661649}; Synonyms=H
CC {ECO:0000269|PubMed:15661649};
CC IsoId=Q64GL0-1; Sequence=Displayed;
CC Name=1 {ECO:0000269|PubMed:15661649};
CC IsoId=Q64GL0-3; Sequence=VSP_052379, VSP_052380;
CC Name=2 {ECO:0000269|PubMed:15661649}; Synonyms=I
CC {ECO:0000269|PubMed:15661649};
CC IsoId=Q64GL0-2; Sequence=VSP_052379, VSP_052380, VSP_052381;
CC -!- TISSUE SPECIFICITY: During embryonic and tadpole development, expressed
CC in the cement gland, brain, neural tube, myotome and neural placodes,
CC including the otic, lateral line and olfactory placodes. All isoforms
CC show similar spatial expression patterns.
CC {ECO:0000269|PubMed:15661649}.
CC -!- DEVELOPMENTAL STAGE: First expressed at stage 18. Expression increases
CC through the early tailbud stage (stage 23) and remains relatively high
CC throughout the remainder of development. All isoforms show similar
CC temporal expression patterns. {ECO:0000269|PubMed:15661649}.
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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000255}.
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DR EMBL; AY686697; AAU20371.1; -; mRNA.
DR EMBL; AY686698; AAU20372.1; -; mRNA.
DR EMBL; AY686699; AAU20373.1; -; mRNA.
DR RefSeq; NP_001089020.1; NM_001095551.1. [Q64GL0-1]
DR AlphaFoldDB; Q64GL0; -.
DR SMR; Q64GL0; -.
DR MaxQB; Q64GL0; -.
DR PRIDE; Q64GL0; -.
DR GeneID; 496406; -.
DR KEGG; xla:496406; -.
DR CTD; 496406; -.
DR Xenbase; XB-GENE-988627; evl.L.
DR OrthoDB; 972128at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 496406; Expressed in brain and 17 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005522; F:profilin binding; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0008154; P:actin polymerization or depolymerization; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR034319; ENA/VASP-like_protein.
DR InterPro; IPR011993; PH-like_dom_sf.
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 SMART; SM00461; WH1; 1.
DR SUPFAM; SSF118370; SSF118370; 1.
DR PROSITE; PS50229; WH1; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Alternative splicing; Cell projection; Cytoplasm;
KW Cytoskeleton; Reference proteome; SH3-binding.
FT CHAIN 1..692
FT /note="Ena/VASP-like protein"
FT /id="PRO_0000284709"
FT DOMAIN 1..112
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REGION 116..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..689
FT /note="EVH2"
FT /evidence="ECO:0000255"
FT REGION 522..542
FT /note="EVH2 block A"
FT /evidence="ECO:0000255"
FT REGION 531..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..580
FT /note="EVH2 block B"
FT /evidence="ECO:0000255"
FT REGION 655..689
FT /note="EVH2 block C"
FT /evidence="ECO:0000255"
FT MOTIF 531..534
FT /note="KLKR"
FT /evidence="ECO:0000255"
FT COMPBIAS 116..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..507
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 162
FT /note="V -> G (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:15661649"
FT /id="VSP_052379"
FT VAR_SEQ 163..456
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:15661649"
FT /id="VSP_052380"
FT VAR_SEQ 639
FT /note="R -> RTPPVVKSPEAKSPIQSQPPSR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15661649"
FT /id="VSP_052381"
SQ SEQUENCE 692 AA; 73921 MW; FE7505502E8BE9EC CRC64;
MSEQSICQAR ASVMIYDDTS KKWVPIKPGQ QGFSRINIYH NTANNTFRVV GVKLQDQQVV
INYSLVKGLK YNQATPTFHQ WRDARQVYGL NFASKEEATT FSNAMLFALN IMNSQDGGPA
AQRQAQNIQN GPSPDDMEIQ RRQMLEQQQR QETLERRTST TVSTLQINVS SSPSHCQSPP
PDYSNFSASP STGAVPPPSY AKVISSAAAS PELSSKSTNK SSNRTSEPPE LQNSHCGSEP
STSQSSAFSP IRPSNGTVSR SIKQISLSPP PAPGSHSPLS LHQSVRHPSL SFSPCSSSPP
VSVTSSVQKN ISPQSPIPVV LPVIPVQNSR IRGCSDKMVQ NPIVPQTGPS DQAEEPLTSQ
ISLSSPRTQV KCVDRSFLSY IETVPVAQLP MITSPFGILT QASPQPFQSS THPSQQSYQS
MSHFVSLPPP YAAVSELTLP KRTTPYMTSS TITQFSPVLP PGHPSSAAMV ASVGSAPAPA
SGPPPPPPPG PPPPSGGTPP PAPPLPAGGS QGVVYEESPA SGLAAALAGA KLRKVQRPED
GSSSPCGATK TDANRTSSGG GGGGLMEEMN KLLAKRRKAA SYTDKPGDKK EEECQNEDAS
LSSSPVTRGP TPQNSSDLGK KPWERSNSVE KPVPSLLSRM KPVSSSNDVS TDALDFDRMK
QEILEEVVRE LHKVKEEIID AIRQELSRIS TT
