ID I3LZE3_ICTTR Unreviewed; 504 AA.
AC I3LZE3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=WASP like actin nucleation promoting factor {ECO:0000313|Ensembl:ENSSTOP00000001688.2};
GN Name=WASL {ECO:0000313|Ensembl:ENSSTOP00000001688.2};
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:ENSSTOP00000001688.2, 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:ENSSTOP00000001688.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AGTP01074188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005333991.1; XM_005333934.2.
DR AlphaFoldDB; I3LZE3; -.
DR STRING; 43179.ENSSTOP00000001688; -.
DR Ensembl; ENSSTOT00000001894.3; ENSSTOP00000001688.2; ENSSTOG00000001892.3.
DR GeneID; 101971056; -.
DR CTD; 8976; -.
DR eggNOG; KOG3671; Eukaryota.
DR GeneTree; ENSGT00730000110895; -.
DR HOGENOM; CLU_015385_3_1_1; -.
DR InParanoid; I3LZE3; -.
DR OMA; LGRKCQT; -.
DR OrthoDB; 3837860at2759; -.
DR TreeFam; TF316736; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0030478; C:actin cap; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0030041; P:actin filament polymerization; IEA:Ensembl.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:2000402; P:negative regulation of lymphocyte migration; IEA:Ensembl.
DR GO; GO:1903526; P:negative regulation of membrane tubulation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0031503; P:protein-containing complex localization; IEA:Ensembl.
DR GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0051653; P:spindle localization; IEA:Ensembl.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01205; EVH1_WASP-like; 1.
DR CDD; cd22075; WH2_hN-WASP_r2_like; 1.
DR CDD; cd22074; WH2_N-WASP_r1; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR011026; WAS_C.
DR InterPro; IPR033927; WASPfam_EVH1.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR11202:SF36; NEURAL WISKOTT-ALDRICH SYNDROME PROTEIN; 1.
DR PANTHER; PTHR11202; SPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00568; WH1; 1.
DR Pfam; PF02205; WH2; 2.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00461; WH1; 1.
DR SMART; SM00246; WH2; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47912; Wiscott-Aldrich syndrome protein, WASP, C-terminal domain; 2.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50229; WH1; 1.
DR PROSITE; PS51082; WH2; 2.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT DOMAIN 33..140
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT DOMAIN 202..215
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 404..421
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT DOMAIN 432..449
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 137..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..394
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..504
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 54600 MW; 45EFF8C08411ADF1 CRC64;
MSSGQQPPPP RKVTNVGSLL LTPQENESLF TFLGKKCVTM SSAVVQLYAA DRNCMWSKKC
SGVACLVKDN PQRSYFLRIF DIKDGKLLWE QELYNNFVYN SPRGYFHTFA GDTCQVALNF
ANEEEAKKFR KAVTDLLGRR QRKSEKRRDP PNGPNLPMAT VDIKNPEITT NRFYSTQVNN
ISHTKEKKKG KAKKKRLTKA DIGTPSNFQH IGHVGWDPNT GFDLNNLDPE LKNLFDLCGI
SEAQLKDRET SKVIYDFIEK TGGVEAVKNE LRRQAPPPPP PSRGGPPPPP PPPHSSGPPP
PPARGRGAPP PPPSRAPTAA PPPPPPSRPG VVVPPPPPNR VYPPPPPALP SSAPSGPPPP
PPPLSVVGSV TAPPPPPPPP PPGPPPPPGL PSDGDHQVPT PAGNKAALLD QIREGAQLKK
VEQNSRPVSC SGRDALLDQI RQGIQLKSVS DGQESAPPTP APTSGIVGAL MEVMQKRSKA
IHSSDEDEDE DDEEDFEDDD EWED
//