ID A0A287CZ14_ICTTR Unreviewed; 557 AA.
AC A0A287CZ14;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=ENAH actin regulator {ECO:0000313|Ensembl:ENSSTOP00000026511.1};
GN Name=ENAH {ECO:0000313|Ensembl:ENSSTOP00000026511.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000026511.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000026511.1}
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 EMBL; AGTP01044457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01044462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_013214674.1; XM_013359220.1.
DR AlphaFoldDB; A0A287CZ14; -.
DR Ensembl; ENSSTOT00000038656.1; ENSSTOP00000026511.1; ENSSTOG00000028215.2.
DR GeneTree; ENSGT00940000157376; -.
DR OrthoDB; 2884005at2759; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; 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 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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 1..111
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT REGION 117..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 61998 MW; 99D9F61ADAC741A4 CRC64;
MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI
NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQEAGPTL
PRQNSQLPAQ VQNGPSQEEL EIQRRQLQEQ QRQKEMERER LERERMERER LERERLERER
LEQEQLERER QERDRQERLE RERLERLERE RQERERQEQL EREQLEWERE RRVSNAAAPA
SVETPLNSVL GDSSASEPGL QAASQPAETP AQQGVVLGPP APPPPPPLPP CPAQASALPP
PPGPPPPPPL PSSGPPPPPP PPPLPNQVPP PPPPPPAPPL PASGFFSGSV SEDNRPLTGL
AAAIAGAKLR KVSRMEDASF PSGGSTISVN SSKTDTSRGN GPLPLGGSGL MEEMSALLAR
RRRIAEKGST IEAEQKEDRN EDSEPVTSKA SSTSTPEPTR KPWERTNTMN GSKSPVISRR
DSPRKNQIVF DNRSYDSLHR PKSTPSSQPS ANGVQTEGLD YDRLKQDILD EMRKELTKLK
EELIDAIRQE LSKSNTA
//
