ID A0A287AF78_PIG Unreviewed; 782 AA.
AC A0A287AF78;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ENAH actin regulator {ECO:0000313|Ensembl:ENSSSCP00000042496.2};
GN Name=ENAH {ECO:0000313|Ensembl:ENSSSCP00000042496.2,
GN ECO:0000313|VGNC:VGNC:108271};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000042496.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000042496.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000042496.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000042496.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family.
CC {ECO:0000256|ARBA:ARBA00009785}.
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DR AlphaFoldDB; A0A287AF78; -.
DR SMR; A0A287AF78; -.
DR STRING; 9823.ENSSSCP00000042496; -.
DR PaxDb; 9823-ENSSSCP00000011569; -.
DR Ensembl; ENSSSCT00000040992.2; ENSSSCP00000042496.2; ENSSSCG00000038646.3.
DR VGNC; VGNC:108271; ENAH.
DR GeneTree; ENSGT00940000157376; -.
DR InParanoid; A0A287AF78; -.
DR Proteomes; UP000008227; Chromosome 10.
DR Bgee; ENSSSCG00000038646; Expressed in ovary and 43 other cell types or tissues.
DR ExpressionAtlas; A0A287AF78; baseline and differential.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005522; F:profilin binding; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR GO; GO:0050699; F:WW domain binding; IEA:Ensembl.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0070358; P:actin polymerization-dependent cell motility; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR CDD; cd01207; EVH1_Ena_VASP-like; 1.
DR CDD; cd22185; WH2_hVASP-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; IPR038023; VASP_sf.
DR InterPro; IPR014885; VASP_tetra.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR PANTHER; PTHR11202:SF1; PROTEIN ENABLED HOMOLOG; 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 PRINTS; PR01217; PRICHEXTENSN.
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 1: Evidence at protein level;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A287AF78};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 1..111
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT REGION 129..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..451
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..591
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 84524 MW; 0481C445BC7C2555 CRC64;
MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI
NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQEAVFYL
GPTLPRQNSQ LPAQVQNGPS QEELEIQRRQ LQEQQRQKEL ERERLERERM ERERLERERL
ERERLERERL EQEQLERERQ ERERQERQER LERERQERER LERLERLDRE RQERERQEQL
EREQLEWERE RRVSSAAPSS DSSLYNAPLP EYASCQPPSA PPPSYAKVIS APVSDASPDY
AVVTALPPTS TPPTPPLRHS ATRFATSLGS AFHPVLPHYA TVPRPLNKGS RPSSPVNTPS
PQPPAAKPCA WAASNFSPLP PSPPVMISSP PGKAAGPRPV LPVCVSSPGP QMPPSPTAPS
GLLDSVPCPV SPPPTSGPAP PPPPPPLPSL VPLSHCGSQA SPPPSTPLAS TPSSKPSVLP
SPSAAAPASV ETPLNSVLGD SSASEPGLQA ASQPAETPAQ QGIVLGPPAP PPPPPLPPGP
AQASAILPPP PGPPPPPPLP SSGPPPPPPP PPLPNQAPPP PPPPPAPPLP ASGFFSGSMS
EDNRPLTGLA AAIAGAKLRK VSRMEDGSFP SGVNAASSKT DTGRGNGPLP LGGSGLMEEM
SALLARRRRI AEKGSTIETE QKEDKNEDSE PQTSKASSTS TPEPTRKPWE RTNTMNGSKS
PVISRPKSAP SSQPSANGVQ TEGLDYDRLK QDILDEMRKE LTKLKEELID AIRQELSKSN
TA
//
