ID A0A2Y9LKJ5_DELLE Unreviewed; 559 AA.
AC A0A2Y9LKJ5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, 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 Name=WASF1 {ECO:0000313|RefSeq:XP_022409986.1,
GN ECO:0000313|RefSeq:XP_022409993.1, ECO:0000313|RefSeq:XP_022410000.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022410000.1};
RN [1] {ECO:0000313|RefSeq:XP_022409986.1, ECO:0000313|RefSeq:XP_022409993.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022409986.1,
RC ECO:0000313|RefSeq:XP_022409993.1};
RG RefSeq;
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: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367034}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family.
CC {ECO:0000256|ARBA:ARBA00006993, ECO:0000256|RuleBase:RU367034}.
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DR RefSeq; XP_022409986.1; XM_022554278.1.
DR RefSeq; XP_022409993.1; XM_022554285.1.
DR RefSeq; XP_022410000.1; XM_022554292.1.
DR STRING; 9749.A0A2Y9LKJ5; -.
DR Ensembl; ENSDLET00000027973; ENSDLEP00000025421; ENSDLEG00000018477.
DR KEGG; dle:111164540; -.
DR OrthoDB; 616448at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0031209; C:SCAR complex; 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:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProtKB-UniRule.
DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IEA:Ensembl.
DR GO; GO:0097484; P:dendrite extension; IEA:Ensembl.
DR GO; GO:0072673; P:lamellipodium morphogenesis; IEA:Ensembl.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IEA:Ensembl.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IEA:Ensembl.
DR GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0016601; P:Rac protein signal transduction; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR CDD; cd22071; WH2_WAVE-1; 1.
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:SF8; WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER 1; 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 Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cytoplasm {ECO:0000256|RuleBase:RU367034};
KW Cytoskeleton {ECO:0000256|RuleBase:RU367034};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 497..514
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 170..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..440
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 61594 MW; 2B6EA9B335F456C4 CRC64;
MPLVKRNIDP RHLCHTALPR GIKNELECVT NISLANIIRQ LSSLSKYAED IFGELFNEAH
SFSFRVNSLQ ERVDRLSVSV TQLDPKEEEL SLQDITMRKA FRSSTVQDQQ LFDRRTLPVP
LQETYDVCEQ PPPLNILTPY RDDGKEGLKF YTNPSYFFDL WKEKMLQDTE DKRKEKRKQK
QKNLDRPHEP EKVPRAPHDR RREWQKLAQG PELAEDDANL LHKHIEVANG PASHFETRPQ
TYVDHMDGSY SLSALPFSQM SELLTRAEER VLVRPHEPPP PPPVHGAGDA KPIPTCISSA
TGLIENRPQS PATGRTPVFV SATPPPPPPP LPSALSTSSL RASMTSTPPP PVPPPPPPPT
TALQAPAVPP PPAPLQIAPG VLHPAPPPIA PPLVQPSPPV ARAAPVCETV PVHPLPQGEV
QGLPPPPPPP PLPPPGIRPS SPVSVAALAH PPSGLHPTPS TAPGPHVPLM PPSPPSQIIP
ASEPKRHPST LPVISDARSV LLEAIRKGIQ LRKVEEQREQ EAKHERIEND VATILSRRIA
VEYSDSEDDS EFDEVDWLE
//
