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Database: UniProt
Entry: A0A087XID2_POEFO
LinkDB: A0A087XID2_POEFO
Original site: A0A087XID2_POEFO 
ID   A0A087XID2_POEFO        Unreviewed;       551 AA.
AC   A0A087XID2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Wiskott-Aldrich syndrome protein family member {ECO:0000256|RuleBase:RU367034};
DE            Short=WASP family protein member {ECO:0000256|RuleBase:RU367034};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000005535.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000005535.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; AYCK01008993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01008994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007561789.1; XM_007561727.2.
DR   RefSeq; XP_016531709.1; XM_016676223.1.
DR   AlphaFoldDB; A0A087XID2; -.
DR   STRING; 48698.ENSPFOP00000005535; -.
DR   Ensembl; ENSPFOT00000005544.2; ENSPFOP00000005535.2; ENSPFOG00000005603.2.
DR   GeneID; 103144648; -.
DR   KEGG; pfor:103144648; -.
DR   eggNOG; KOG1830; Eukaryota.
DR   GeneTree; ENSGT00950000182962; -.
DR   OMA; NQAQEHV; -.
DR   OrthoDB; 616448at2759; -.
DR   Proteomes; UP000028760; 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   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:SF1; WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER; 1.
DR   Pfam; PF02205; WH2; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
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:UP000028760}.
FT   DOMAIN          489..506
FT                   /note="WH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51082"
FT   REGION          169..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..385
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..454
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  59977 MW;  7690883811123FE7 CRC64;
     MPLVKRNIEP RHLCRGALPD GVTSELECVT NSTLAAIIKQ LGSLSRHAED IFGELFNEAN
     SFYLRMSSLQ ERVDQLAVKV TQLDSTVEEV SLQDINMRKA FKSSTIQDQQ VVSRTSVPNP
     VVEMYHRCDK PPPLNILSPY RDDKKDALKF YTDPSYFFNL WKEKMLQATE DKRKEKRRQK
     SCPAHPDRPH SRQAPPRSPL SISEQQRQVE DPSREVKKVR KARNRRQEWN VLAYDKEFRP
     DARLTPSPYH GMSSEGSLSP DSRSMASDSY PASPNHPTTQ APSAAHPADH HARDHLAAAQ
     TQSLDRGLRP ANQPPGAAGA GPPGRHAASL GRTPSGHGVQ AGGDPTVNGP RQQSIKEYRA
     GGQPSTIPEY YIPPAPPPPP PTIPSAQTAF DSATAPPSAA ASAIPPTSSA LSCHYSPSPP
     PPPANYIPSP AHPPSGAPPA APPPPPPGVP VGHQAHPSPP HAAVGQTAVD SAPSTRKSTM
     LGMIPMSDAR SDLLAAIRRG IQLRKVQEQR EQEAKREPVG NDVATILSRR IAVEYSESDD
     DSELDENEWS D
//
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