WASF2_BOVIN
ID WASF2_BOVIN Reviewed; 493 AA.
AC A2VDK6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Actin-binding protein WASF2 {ECO:0000305};
DE AltName: Full=Wiskott-Aldrich syndrome protein family member 2;
DE Short=WASP family protein member 2;
GN Name=WASF2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:Q9Y6W5}.
CC -!- SUBUNIT: Binds actin and the Arp2/3 complex. Interacts with BAIAP2.
CC Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1,
CC NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and WASF2/WAVE2.
CC Directly interacts with BRK1. Interacts with human cytomegalovirus
CC protein UL135. Interacts with FNBP1L (via the SH3 domain).
CC {ECO:0000250|UniProtKB:Q9Y6W5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC projection, lamellipodium {ECO:0000250}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q9Y6W5}. Note=At the interface between the
CC lamellipodial actin meshwork and the membrane. {ECO:0000250}.
CC -!- DOMAIN: Binds and activates the Arp2/3 complex via the C-terminal
CC domain. Interacts with actin via the WH2 domain (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y6W5}.
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family. {ECO:0000305}.
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DR EMBL; BC133284; AAI33285.1; -; mRNA.
DR RefSeq; NP_001074980.1; NM_001081511.1.
DR RefSeq; XP_005203144.1; XM_005203087.3.
DR RefSeq; XP_010800830.1; XM_010802528.2.
DR AlphaFoldDB; A2VDK6; -.
DR SMR; A2VDK6; -.
DR STRING; 9913.ENSBTAP00000024447; -.
DR PaxDb; A2VDK6; -.
DR PRIDE; A2VDK6; -.
DR Ensembl; ENSBTAT00000024447; ENSBTAP00000024447; ENSBTAG00000018374.
DR Ensembl; ENSBTAT00000081815; ENSBTAP00000067550; ENSBTAG00000018374.
DR GeneID; 504482; -.
DR KEGG; bta:504482; -.
DR CTD; 10163; -.
DR VEuPathDB; HostDB:ENSBTAG00000018374; -.
DR VGNC; VGNC:36866; WASF2.
DR eggNOG; KOG1830; Eukaryota.
DR GeneTree; ENSGT00950000182962; -.
DR HOGENOM; CLU_036022_2_0_1; -.
DR InParanoid; A2VDK6; -.
DR OrthoDB; 1183697at2759; -.
DR TreeFam; TF315031; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000018374; Expressed in monocyte and 106 other tissues.
DR ExpressionAtlas; A2VDK6; baseline and differential.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0031209; C:SCAR complex; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR InterPro; IPR028288; SCAR/WAVE_fam.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR12902; PTHR12902; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00246; WH2; 1.
DR PROSITE; PS51082; WH2; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..493
FT /note="Actin-binding protein WASF2"
FT /id="PRO_0000284948"
FT DOMAIN 431..448
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 173..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6W5"
SQ SEQUENCE 493 AA; 54031 MW; 67DFD8519C2788FE CRC64;
MPLVTRNIEP RHLCRQTLPS VRSELECMTN ITLANVIRQL GSLSKYAEDI FGELFTQANT
FASRVSSLAE RVDRLQVKVT QLDPKEEEVS LQGINTRKAF RSSTVQDQKL FDRNSLPIPV
LETYNTCDTP PPLNNLTPYR DDGKEALKFY TDPSYFFDLW KEKMLQDTKD IMKEKRKHRK
EKKDNPNRGN VNPRKIKTRK EEWEKMKMGQ EFVESKEKPS RYPPTLVYQN GSIGSVENVD
AGNYPPPPQS DSISPPSPSF SEDNLPPPPA EFSYPADNNQ RAGLKRSSVV SPSHPPPAPP
LGSAPGPKPG FAPPPAPPPP PPMINTPPPP PPGGFGSPAT PPPPSPPSFP PHPDFAAPPP
PPPPPAVDYS TLPPPPLSQS AGGAPPPPPP PPPPGPPPPP FSGADGQLAA PPPPLSDTTK
PKSSLPPVSD ARSDLLSAIR QGFQLRRVEE QREQEKRDVV GNDVATILSR RIAVEYSDSE
DDSSEFDEDE WSD
