ID A0A455BTW3_PHYMC Unreviewed; 419 AA.
AC A0A455BTW3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Ena/VASP-like protein {ECO:0000256|ARBA:ARBA00017156};
DE AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like {ECO:0000256|ARBA:ARBA00033193};
GN Name=EVL {ECO:0000313|RefSeq:XP_028352187.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028352187.1};
RN [1] {ECO:0000313|RefSeq:XP_028352187.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028352187.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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, lamellipodial and filopodial dynamics,
CC platelet activation and cell migration.
CC {ECO:0000256|PIRNR:PIRNR038010}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000256|ARBA:ARBA00004529}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family.
CC {ECO:0000256|ARBA:ARBA00009785, ECO:0000256|PIRNR:PIRNR038010}.
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DR RefSeq; XP_028352187.1; XM_028496386.2.
DR AlphaFoldDB; A0A455BTW3; -.
DR InParanoid; A0A455BTW3; -.
DR OrthoDB; 2884005at2759; -.
DR Proteomes; UP000248484; Chromosome 11.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0001725; C:stress fiber; 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:0008154; P:actin polymerization or depolymerization; IEA:UniProtKB-UniRule.
DR GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
DR CDD; cd01207; EVH1_Ena_VASP-like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
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; ENA_VASP-LIKE PROTEIN; 1.
DR PANTHER; PTHR11202; SPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 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; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF118370; Vasodilator-stimulated phosphoprotein, VASP, tetramerisation domain; 1.
DR PROSITE; PS50229; WH1; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW ECO:0000256|PIRNR:PIRNR038010};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273,
KW ECO:0000256|PIRNR:PIRNR038010};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR038010};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR038010};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 4..118
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT REGION 121..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 419 AA; 44567 MW; 90C9C8092B368EBC CRC64;
MFAFEEFSEQ SICQARASVM VYDDTSKKWV PIKPGQQGFS RINIYHNTAS NTFRVVGVKL
QDQQVVINYS IVKGLKYNQA TPTFHQWRDA RQVYGLNFAS KEEATTFSNA MLFALNIMNS
QEGGSSSQRQ VQNGPSPDEM DIQRRQVMEQ QRQESLERRA SATGPTLPAG HPSAAAGAPL
SCSGPPPPPP PPVPPPPTGA APPPPPPLPA GGAQGASHDE GSVSGLAAAL AGAKLRRVPR
PEDASGGSSP SGTSKSDANR ASSGGGGGGL MEEMNKLLAK RRKAASQTDK PADKKEDESQ
TEEPSTSPSP GTRAASQPPN SSEAGRKPWE RSSSAEKPVS SLLSRTPSVA KSPEAKSPLQ
SQPHSRMKPA GSVNDVALDA LDLDRMKQEI LEEVVRELHK VKEEIIDAIR QELGGISTS
//
