ID A0A5F8A383_MACMU Unreviewed; 805 AA.
AC A0A5F8A383;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 18-JUN-2025, entry version 26.
DE RecName: Full=Protein enabled homolog {ECO:0000256|ARBA:ARBA00072571};
GN Name=ENAH {ECO:0000313|Ensembl:ENSMMUP00000072354.1,
GN ECO:0000313|VGNC:VGNC:99903};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000072354.1, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000072354.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000072354.1};
RA Dutcher S., Fulton R., Lindsay T.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSMMUP00000072354.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000072354.1};
RA Graves T., Eichler E.E., Wilson R.K.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSMMUP00000072354.1}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000072354.1};
RG Ensembl;
RL Submitted (MAR-2025) 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 and lamellipodial and filopodial
CC dynamics in migrating cells. ENAH induces the formation of F-actin rich
CC outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and
CC downstream of NTN1 to promote filipodia formation.
CC {ECO:0000256|ARBA:ARBA00056269}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Cell projection, filopodium
CC {ECO:0000256|ARBA:ARBA00004486}. Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family.
CC {ECO:0000256|ARBA:ARBA00009785}.
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DR AlphaFoldDB; A0A5F8A383; -.
DR SMR; A0A5F8A383; -.
DR FunCoup; A0A5F8A383; 798.
DR STRING; 9544.ENSMMUP00000072354; -.
DR Ensembl; ENSMMUT00000093922.1; ENSMMUP00000072354.1; ENSMMUG00000002227.4.
DR VEuPathDB; HostDB:ENSMMUG00000002227; -.
DR VGNC; VGNC:99903; ENAH.
DR GeneTree; ENSGT00940000157376; -.
DR InParanoid; A0A5F8A383; -.
DR OMA; XDILDEM; -.
DR Proteomes; UP000006718; Chromosome 1.
DR Bgee; ENSMMUG00000002227; Expressed in fibroblast and 21 other cell types or tissues.
DR ExpressionAtlas; A0A5F8A383; baseline.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IEA:UniProtKB-KW.
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 FunFam; 1.20.5.1160:FF:000003; protein enabled homolog isoform X2; 1.
DR FunFam; 2.30.29.30:FF:000047; vasodilator-stimulated phosphoprotein isoform X2; 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 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 1..111
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT REGION 142..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..281
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..427
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..507
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..558
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..608
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..678
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 805 AA; 87200 MW; E88BD8ACA753E0E3 CRC64;
MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI
NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQETAQSK
VTATQDSTNL RCIFCGPTLP RQNSQLPAQV QNGPSQEELE IQRRQLQEQQ RQKELERERL
ERERMERERL ERERLERERL ERERLEQEQL ERERQERERQ ERLERQERLD RERQERQERE
RLERLERERQ ERERQEQLER EQLEWERERR ISSAAPSSDS SLYNAPLPEY SSCQPPSAPP
PSYAKVISAP VSDATPDYAV VTALPPTSTP PTPPLRHSAT RFATSLGSAF HPVLPHYATV
PRPLNKNSRP SSPVNTPSSQ PPATKPCAWS TSNFSPLPPS PPIMISSPPG KATGPRPVLP
VCVSSPVPQM PPSPTAPNGL VDSVTYPVSP PPTSGPAAPP PPPPLPSLAS LSHCGSQASP
PPSTPIASTP SSKPSVLPSP SAAAPASVET PLNSVLGDSS ASEPGLQAAS QPAETPAQQG
IVLGPLAPPP PPPLPPGPAQ ASVALPPPPG PPPPPPLPST GPPPPPPPPP LPNQVPPPPP
PPPAPPLPAS GFFLASVSED NRPLTGLAAA IAGAKLRKVS RMEDASFPSG GNAIGVNSAS
SKADTGRGNG PLPLGGSGLM EEMSALLARR RRIAEKGSTV ETEQKEDKGE DSEPVTSKAS
STSTPEPTRK PWERTNTMNG SKSPVISRPK STPLSQPSAN GVQTEGLDYD RLKQDILDEM
RKELTKLKEE LIDAIRQELS KSNTA
//
