ID A0A0N4WBK0_HAEPC Unreviewed; 453 AA.
AC A0A0N4WBK0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Wiskott-Aldrich syndrome protein family member {ECO:0000256|RuleBase:RU367034};
DE Short=WASP family protein member {ECO:0000256|RuleBase:RU367034};
GN ORFNames=HPLM_LOCUS7820 {ECO:0000313|EMBL:VDO33081.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0000782801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0000782801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO33081.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO33081.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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. {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; UZAF01016734; VDO33081.1; -; Genomic_DNA.
DR STRING; 6290.A0A0N4WBK0; -.
DR WBParaSite; HPLM_0000782801-mRNA-1; HPLM_0000782801-mRNA-1; HPLM_0000782801.
DR OMA; NQAQEHV; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; Unassembled WGS sequence.
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-UniRule.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProtKB-UniRule.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|RuleBase:RU367034};
KW Cytoskeleton {ECO:0000256|RuleBase:RU367034};
KW Reference proteome {ECO:0000313|Proteomes:UP000268014}.
FT DOMAIN 388..405
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 176..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..87
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 257..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..360
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 50159 MW; 1377A6D59B3D8D01 CRC64;
MPLIKRAVSP VHVSRVKIPP EVTNGELQYV ANSTLANLIR QLSSISKHAE HIFGEIYLEA
MKLDHKSNTL EKRIANLTEK VSKLDSTNEQ ASLGELQMRK PFKSSMLIDQ HTLDRSTLPV
ALAEVYSRCD PPPNLDALNP FRDPGAPSAL SLYTNPSFFF DLWRQEMLKD CADNTARRRI
KSPPPDGLNM VRSPKKRRQR LPMQQQEVPR QQAARYMSSL RNTRTAAPSF PDEYQTPQSL
GLQLHKTNQI QHIQPIQTST PSQISGMSHR VAPTPDNRQR VNLSPPKELK RELPPPDLAL
LSIDDEDEEL PPPPPTLMHT SVVNHLPSPP PSAIQLVPSD TQAVVPPPPA PPPPPQNLIT
APAPSAATFG ASAKPTTETE EEEKKPDTRS NLLAEIQSGI KLKKVRLAEE AAADKAAAEA
NDVAAILKRR MEHVMGNEDE ESQSSGDDGE WED
//
