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Database: UniProt
Entry: A0A2R9BDH1_PANPA
LinkDB: A0A2R9BDH1_PANPA
Original site: A0A2R9BDH1_PANPA 
ID   A0A2R9BDH1_PANPA        Unreviewed;       499 AA.
AC   A0A2R9BDH1;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=WASF3 {ECO:0000313|Ensembl:ENSPPAP00000025134.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000025134.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000025134.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000025134.1}
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; AJFE02062770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008969871.1; XM_008971623.1.
DR   AlphaFoldDB; A0A2R9BDH1; -.
DR   Ensembl; ENSPPAT00000047960.1; ENSPPAP00000025134.1; ENSPPAG00000035699.1.
DR   GeneTree; ENSGT00950000182962; -.
DR   Proteomes; UP000240080; Chromosome 13.
DR   Bgee; ENSPPAG00000035699; Expressed in cerebellum and 5 other cell types or tissues.
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   CDD; cd22073; WH2_WAVE-3; 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:SF7; WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER 3; 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:UP000240080}.
FT   DOMAIN          437..454
FT                   /note="WH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51082"
FT   REGION          171..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..312
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..352
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..409
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  55023 MW;  CB4CAB2678F9B1CE CRC64;
     MPLVKRNIEP RHLCRGALPE GITSELECVT NSTLAAIIRQ LSSLSKHAED IFGELFNEAN
     NFYIRANSLQ DRIDRLAVKV TQLDSTVEEV SLQDINMKKA FKSSTVQDQQ VVSKNSIPNP
     VADIYNQSDK PPPLNILTPY RDDKKDGLKF YTDPSYFFDL WKEKMLQDTE DKRKEKRRQK
     REKHKLNPNR NQQVNVRKVR TRKEEWERRK MGIEFMSDAK KLEQAGSAKE DRVPSGSHAS
     DVTDYSYPAT PNHSLHPQPV TPSYAAGDVP PHGPASQAAE HEYRPPSASA RHMALNRPQQ
     PPPPPPPQAP EGSQASAPMA PADYGMLPAQ IIEYYNPSGP PPPPPPPVIP SAQTAFVSPL
     QMPMQPPFPA SASSTHSAPP HPPSTGLLVT APPPPGPPPP PPGPPGPGSS LSSSPMHGPP
     VAEAKRQEPA QPPISDARSD LLAAIRMGIQ LKKVQEQREQ EAKREPVGND VATILSRRIA
     VEYSDSDDDS EFDENDWSD
//
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