ID A0A6I9YQU2_9SAUR Unreviewed; 772 AA.
AC A0A6I9YQU2;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE RecName: Full=Protein enabled homolog {ECO:0000256|ARBA:ARBA00072571};
GN Name=ENAH {ECO:0000313|RefSeq:XP_013926898.1};
OS Thamnophis sirtalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Natricinae; Thamnophis.
OX NCBI_TaxID=35019 {ECO:0000313|Proteomes:UP000504617, ECO:0000313|RefSeq:XP_013926898.1};
RN [1] {ECO:0000313|RefSeq:XP_013926898.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_013926898.1; XM_014071423.1.
DR AlphaFoldDB; A0A6I9YQU2; -.
DR GeneID; 106553010; -.
DR CTD; 55740; -.
DR OrthoDB; 31170at2759; -.
DR Proteomes; UP000504617; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005522; F:profilin binding; IEA:TreeGrafter.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:TreeGrafter.
DR GO; GO:0070358; P:actin polymerization-dependent cell motility; IEA:TreeGrafter.
DR GO; GO:0007411; P:axon guidance; IEA:TreeGrafter.
DR CDD; cd01207; EVH1_Ena_VASP-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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000504617};
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 114..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 737..768
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 114..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..380
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..484
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 84755 MW; 902DBF83C41496C7 CRC64;
MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI
NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQDSGPTL
PRQNAQIPPQ VQNGPAQEDL ESQRRQLQEQ QRQKELERER MERDRMERER LERDRLERER
LERERLEKER LERERLEQEQ LERERQERER REREWQERLE RERQERERQE RERLEWEKQE
RERQDQLERE QLEWERERKL SSAAPSFDNS LYNPSLPEYA SCQPPSAPPP SYAKAMSDST
PDYAIVTSAQ SISSPPTPPL RHPASRFATS LGSAFHPVLP HYATVPRPVN KNSQPPSPVN
PPPSLPPTTK STTWSASSFA PLPPSPPVMI SSPPGKATGP KPVLPIPVTV QLSQMSPTAP
NGLPELANYS VSSPPTSGPA QLPPSSFQPL SVSGLQASSP TSPNASAPSS KPSVLPSPSA
APPAFVENSL NSVLGDSSAS EPVLQTASQP AEPTSQQGVT QGPPAPPPPP PLPSGPVQSP
SAVPPPPGPP PPPPLPSLGP PPPPPLPTQV PLPPPAPPLP ATGFSMGMMY EDYRPLTGLA
AALAGAKLRK VSRNEDSPVP SGGTNSASPK TDTSRGNGPL PLGGSGLMEE MSALLARRRR
IAEKGSSETE TKEEKSEEPE PLAPKPPSTS TPELTRKPWE RTNTMNGSKS PIISRPKSAS
SGQPNTNGVQ SEGLDYDRLK QDILEEMRKE LTKLKEELID AIRQELNKSN TV
//
