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EVL_MOUSE
ID   EVL_MOUSE               Reviewed;         414 AA.
AC   P70429; Q9ERU8;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Ena/VASP-like protein;
DE   AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like;
GN   Name=Evl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=8861907; DOI=10.1016/s0092-8674(00)81341-0;
RA   Gertler F.B., Niebuhr K., Reinhard M., Wehland J., Soriano P.;
RT   "Mena, a relative of VASP and Drosophila Enabled, is implicated in the
RT   control of microfilament dynamics.";
RL   Cell 87:227-239(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH PFN2;
RP   LYN; APBB1; ABL1 AND SRC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   PHOSPHORYLATION BY PKA.
RC   STRAIN=C57BL/6J;
RX   PubMed=10945997; DOI=10.1074/jbc.m006274200;
RA   Lambrechts A., Kwiatkowski A.V., Lanier L.M., Bear J.E., Vandekerckhove J.,
RA   Ampe C., Gertler F.B.;
RT   "cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP
RT   relative, regulates its interaction with actin and SH3 domains.";
RL   J. Biol. Chem. 275:36143-36151(2000).
RN   [3]
RP   ROLE IN L.MONOCYTOGENES MOBILITY, MISCELLANEOUS, AND INTERACTION WITH
RP   L.MONOCYTOGENES ACTA.
RX   PubMed=10087267; DOI=10.1083/jcb.144.6.1245;
RA   Laurent V., Loisel T.P., Harbeck B., Wehman A., Groebe L., Jockusch B.M.,
RA   Wehland J., Gertler F.B., Carlier M.-F.;
RT   "Role of proteins of the Ena/VASP family in actin-based motility of
RT   Listeria monocytogenes.";
RL   J. Cell Biol. 144:1245-1258(1999).
RN   [4]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=10069337; DOI=10.1016/s0896-6273(00)81092-2;
RA   Lanier L.M., Gates M.A., Witke W., Menzies A.S., Wehman A.M., Macklis J.D.,
RA   Kwiatkowski D., Soriano P., Gertler F.B.;
RT   "Mena is required for neurulation and commissure formation.";
RL   Neuron 22:313-325(1999).
RN   [5]
RP   INTERACTION WITH SEMA6A.
RX   PubMed=10993894; DOI=10.1074/jbc.m006316200;
RA   Klostermann A., Lutz B., Gertler F., Behl C.;
RT   "The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-
RT   1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-like
RT   protein (EVL) via a novel carboxyl-terminal zyxin-like domain.";
RL   J. Biol. Chem. 275:39647-39653(2000).
RN   [6]
RP   INTERACTION WITH DNMBP.
RX   PubMed=14506234; DOI=10.1074/jbc.m308104200;
RA   Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
RA   Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
RT   "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
RT   domains, links dynamin to regulation of the actin cytoskeleton.";
RL   J. Biol. Chem. 278:49031-49043(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329 AND SER-367, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-130 IN COMPLEX WITH A SYNTHETIC
RP   PRO-RICH PEPTIDE.
RX   PubMed=10404224; DOI=10.1038/10717;
RA   Fedorov A.A., Fedorov E., Gertler F., Almo S.C.;
RT   "Structure of EVH1, a novel proline-rich ligand-binding module involved in
RT   cytoskeletal dynamics and neural function.";
RL   Nat. Struct. Biol. 6:661-665(1999).
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. {ECO:0000269|PubMed:10087267,
CC       ECO:0000269|PubMed:10945997}.
CC   -!- SUBUNIT: Homotetramer (By similarity). Binds to the SH3 domains of
CC       ABL1, LYN and SRC (PubMed:10945997). Also binds to profilin, with
CC       preference for isoform IIa of PFN2, and the WW domain of APBB1/FE65
CC       (PubMed:10945997). Binds to SEMA6A (PubMed:10993894). Interacts, via
CC       the Pro-rich region, with the C-terminal SH3 domain of DNMBP
CC       (PubMed:14506234). Interacts with RAPH1 (By similarity). Binds, via the
CC       EVH1 domain, the Pro-rich domain of Listeria monocytogenes actA
CC       (PubMed:10087267). Binds, via the EVH1 domain, the Pro-rich domain of
CC       ZYX. Interacts with FYB1. Interacts with ZDHHC17 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UI08, ECO:0000269|PubMed:10087267,
CC       ECO:0000269|PubMed:10404224, ECO:0000269|PubMed:10945997,
CC       ECO:0000269|PubMed:10993894, ECO:0000269|PubMed:14506234}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:10945997}. Cytoplasm, cytoskeleton, stress fiber
CC       {ECO:0000269|PubMed:10945997}. Cell projection, lamellipodium
CC       {ECO:0000269|PubMed:10945997}. 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:0000269|PubMed:10945997}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=EVL-I;
CC         IsoId=P70429-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=P70429-2; Sequence=VSP_004045;
CC   -!- TISSUE SPECIFICITY: Highest expression in thymus and spleen (at protein
CC       level). Low levels in placenta, ovary, testis, fat and lung (at protein
CC       level). Isoform 1 and isoform 2 are expressed in cortical neurons and
CC       glial cells. {ECO:0000269|PubMed:10069337,
CC       ECO:0000269|PubMed:10945997}.
CC   -!- DEVELOPMENTAL STAGE: At an early stage, highly expressed in the
CC       branchial and pharyngeal arches, but not in the brain. Expression in
CC       the brain starts at 15 dpc (at protein level).
CC       {ECO:0000269|PubMed:10069337}.
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:0000269|PubMed:10945997}.
CC   -!- MISCELLANEOUS: Required to transform actin polymerization into active
CC       movement for the propulsive force of Listeria monocytogenes.
CC   -!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
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DR   EMBL; U72519; AAC52862.1; -; mRNA.
DR   EMBL; AF279662; AAG23653.1; -; mRNA.
DR   CCDS; CCDS26161.1; -. [P70429-2]
DR   CCDS; CCDS49167.1; -. [P70429-1]
DR   RefSeq; NP_001156866.1; NM_001163394.1. [P70429-1]
DR   RefSeq; NP_031991.3; NM_007965.3. [P70429-2]
DR   PDB; 1QC6; X-ray; 2.60 A; A/B=1-130.
DR   PDBsum; 1QC6; -.
DR   AlphaFoldDB; P70429; -.
DR   SMR; P70429; -.
DR   BioGRID; 199547; 15.
DR   DIP; DIP-40886N; -.
DR   ELM; P70429; -.
DR   IntAct; P70429; 3.
DR   MINT; P70429; -.
DR   STRING; 10090.ENSMUSP00000021689; -.
DR   iPTMnet; P70429; -.
DR   PhosphoSitePlus; P70429; -.
DR   EPD; P70429; -.
DR   jPOST; P70429; -.
DR   MaxQB; P70429; -.
DR   PaxDb; P70429; -.
DR   PRIDE; P70429; -.
DR   ProteomicsDB; 275699; -. [P70429-1]
DR   ProteomicsDB; 275700; -. [P70429-2]
DR   Antibodypedia; 14371; 163 antibodies from 33 providers.
DR   DNASU; 14026; -.
DR   Ensembl; ENSMUST00000021689; ENSMUSP00000021689; ENSMUSG00000021262. [P70429-1]
DR   Ensembl; ENSMUST00000077735; ENSMUSP00000076916; ENSMUSG00000021262. [P70429-2]
DR   GeneID; 14026; -.
DR   KEGG; mmu:14026; -.
DR   UCSC; uc007ozv.1; mouse. [P70429-2]
DR   UCSC; uc007ozw.1; mouse. [P70429-1]
DR   CTD; 51466; -.
DR   MGI; MGI:1194884; Evl.
DR   VEuPathDB; HostDB:ENSMUSG00000021262; -.
DR   eggNOG; KOG4590; Eukaryota.
DR   GeneTree; ENSGT00940000157826; -.
DR   HOGENOM; CLU_017790_0_0_1; -.
DR   InParanoid; P70429; -.
DR   OMA; RTHYGIN; -.
DR   OrthoDB; 972128at2759; -.
DR   PhylomeDB; P70429; -.
DR   TreeFam; TF321411; -.
DR   Reactome; R-MMU-376176; Signaling by ROBO receptors.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   BioGRID-ORCS; 14026; 4 hits in 71 CRISPR screens.
DR   ChiTaRS; Evl; mouse.
DR   EvolutionaryTrace; P70429; -.
DR   PRO; PR:P70429; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; P70429; protein.
DR   Bgee; ENSMUSG00000021262; Expressed in peripheral lymph node and 254 other tissues.
DR   ExpressionAtlas; P70429; baseline and differential.
DR   Genevisible; P70429; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005522; F:profilin binding; IDA:UniProtKB.
DR   GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB.
DR   GO; GO:0030048; P:actin filament-based movement; NAS:UniProtKB.
DR   GO; GO:0045010; P:actin nucleation; NAS:UniProtKB.
DR   GO; GO:0008154; P:actin polymerization or depolymerization; IDA:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; NAS:UniProtKB.
DR   GO; GO:0051016; P:barbed-end actin filament capping; NAS:UniProtKB.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR   GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:MGI.
DR   GO; GO:1900028; P:negative regulation of ruffle assembly; ISO:MGI.
DR   GO; GO:0030168; P:platelet activation; NAS:UniProtKB.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR   GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
DR   DisProt; DP02387; -.
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   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; Cell projection;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; SH3-binding.
FT   CHAIN           1..414
FT                   /note="Ena/VASP-like protein"
FT                   /id="PRO_0000087105"
FT   DOMAIN          1..112
FT                   /note="WH1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT   REGION          157..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..411
FT                   /note="EVH2"
FT   REGION          220..240
FT                   /note="EVH2 block A"
FT   REGION          263..280
FT                   /note="EVH2 block B"
FT   REGION          340..360
FT                   /note="Required for interaction with ZDHHC17"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT   REGION          377..411
FT                   /note="EVH2 block C"
FT   MOTIF           229..232
FT                   /note="KLKR"
FT   COMPBIAS        177..206
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08719"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT   MOD_RES         257
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08719"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT   MOD_RES         304
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT   MOD_RES         327
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT   MOD_RES         329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         339
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         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI08"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         339..359
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:8861907"
FT                   /id="VSP_004045"
FT   STRAND          4..17
FT                   /evidence="ECO:0007829|PDB:1QC6"
FT   TURN            18..21
FT                   /evidence="ECO:0007829|PDB:1QC6"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:1QC6"
FT   STRAND          34..41
FT                   /evidence="ECO:0007829|PDB:1QC6"
FT   TURN            42..45
FT                   /evidence="ECO:0007829|PDB:1QC6"
FT   STRAND          46..52
FT                   /evidence="ECO:0007829|PDB:1QC6"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:1QC6"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:1QC6"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:1QC6"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:1QC6"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:1QC6"
FT   HELIX           95..111
FT                   /evidence="ECO:0007829|PDB:1QC6"
SQ   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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