ID K7F412_PELSI Unreviewed; 496 AA.
AC K7F412;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Wiskott-Aldrich syndrome protein family member {ECO:0000256|RuleBase:RU367034};
DE Short=WASP family protein member {ECO:0000256|RuleBase:RU367034};
GN Name=WASF2 {ECO:0000313|Ensembl:ENSPSIP00000002772.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000002772.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000002772.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Downstream effector molecule involved in the transmission of
CC signals from tyrosine kinase receptors and small GTPases to the actin
CC cytoskeleton. Promotes formation of actin filaments. Part of the WAVE
CC complex that regulates lamellipodia formation. The WAVE complex
CC regulates actin filament reorganization via its interaction with the
CC Arp2/3 complex. {ECO:0000256|RuleBase:RU367034}.
CC -!- SUBUNIT: Binds actin and the Arp2/3 complex.
CC {ECO:0000256|RuleBase:RU367034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367034}.
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family.
CC {ECO:0000256|ARBA:ARBA00006993, ECO:0000256|RuleBase:RU367034}.
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DR EMBL; AGCU01035819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01035820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01035821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01035822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01035823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7F412; -.
DR STRING; 13735.ENSPSIP00000002772; -.
DR Ensembl; ENSPSIT00000002783.1; ENSPSIP00000002772.1; ENSPSIG00000002694.1.
DR eggNOG; KOG1830; Eukaryota.
DR GeneTree; ENSGT00950000182962; -.
DR HOGENOM; CLU_036022_2_0_1; -.
DR OMA; PDMAYND; -.
DR TreeFam; TF315031; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0031209; C:SCAR complex; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051018; F:protein kinase A binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0030048; P:actin filament-based movement; IEA:Ensembl.
DR GO; GO:0001667; P:ameboidal-type cell migration; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0072673; P:lamellipodium morphogenesis; IEA:Ensembl.
DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0016601; P:Rac protein signal transduction; IEA:Ensembl.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 6.10.280.150; -; 2.
DR InterPro; IPR028288; SCAR/WAVE_fam.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR12902; WASP-1; 1.
DR PANTHER; PTHR12902:SF1; WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00246; WH2; 1.
DR PROSITE; PS51082; WH2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|RuleBase:RU367034};
KW Cytoplasm {ECO:0000256|RuleBase:RU367034};
KW Cytoskeleton {ECO:0000256|RuleBase:RU367034};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267}.
FT DOMAIN 434..451
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 173..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..276
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..423
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 54886 MW; 72F6785D3E953868 CRC64;
MPLVTRNIEP RHLCRQTLPT VKSELECMTN ITLANVIRQL GSLSKFAEDI FGELFTQANT
FAFRVSSLVE RVDRLQVKVT QLDPKEEEVS LQGINTRKAF KSSTTQDQKL FDRDSLPVPV
LETYNICNTP PPLNILSPYR DDGKEALKFY TDPSYFFDLW KEKMLQDTKD IMKEKRKHRK
EKKDNPNRGN VNPRKIKTRK EEWEKLKMGQ EFVESKDKQG NSSIYPSNMV YQNGSIGSDE
SMEMNYYPPP PQSDSVSPPS PSYPDDNLPP PPLEFSHPSV NSTSLSLPGP QPSSLILPSH
PEGCCCWGAR LPLPSGQGPR LAVVWPQPSL VSRQSPVPSS THNKPTNHLT PYSPSVNSYP
VDNQRGSGSG GPKRSSLVSP SHPPPAPPPP PPPPPPPGPP PLSSGGMAGA PAPLPPPDSS
ASKPKSSLPP VSDARSDLLS AIRQGFQLRK VEEQREQEKR DVGGNDVATI LSRRIAVEYS
DSEDDSSEFD EDDWSD
//
