ID A0A084WPY6_ANOSI Unreviewed; 531 AA.
AC A0A084WPY6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Wiskott-Aldrich syndrome protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ZHAS_00020398 {ECO:0000313|EMBL:KFB52280.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB52280.1};
RN [1] {ECO:0000313|EMBL:KFB52280.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC020398-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the CDC42SE/SPEC family.
CC {ECO:0000256|ARBA:ARBA00005720}.
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DR EMBL; ATLV01025138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE525369; KFB52280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084WPY6; -.
DR STRING; 74873.A0A084WPY6; -.
DR EnsemblMetazoa; ASIC020398-RA; ASIC020398-PA; ASIC020398.
DR VEuPathDB; VectorBase:ASIC020398; -.
DR VEuPathDB; VectorBase:ASIS020456; -.
DR OMA; IMFEQEL; -.
DR Proteomes; UP000030765; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01205; EVH1_WASP-like; 1.
DR CDD; cd21762; WH2; 1.
DR Gene3D; 6.10.280.150; -; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR039056; SPEC.
DR InterPro; IPR011026; WAS_C.
DR InterPro; IPR033927; WASPfam_EVH1.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR13502; CDC42 SMALL EFFECTOR PROTEIN HOMOLOG; 1.
DR PANTHER; PTHR13502:SF6; CDC42 SMALL EFFECTOR PROTEIN HOMOLOG; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00568; WH1; 1.
DR Pfam; PF02205; WH2; 2.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00461; WH1; 1.
DR SMART; SM00246; WH2; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47912; Wiscott-Aldrich syndrome protein, WASP, C-terminal domain; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50229; WH1; 1.
DR PROSITE; PS51082; WH2; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765}.
FT DOMAIN 39..148
FT /note="WH1"
FT /evidence="ECO:0000259|PROSITE:PS50229"
FT DOMAIN 199..212
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 424..441
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT DOMAIN 455..472
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 57345 MW; 8DE9DAC4BE295309 CRC64;
MKQPGGIDTA GDRNSTASKA NRPSLLLTNE ENDQLFRLLG RRCQTLSTAV VQLYTTQSPA
HASWVKRCTG ALCFIKDNLR KSYYFRLYCL KANLMVWEQE LYDKIEVTQP KPYLITFEGQ
DGIVALNFAT EDEAAGFMST TLTTVHNRNR RRDAVPAFQQ PYPAHQQQQQ QPHSQQLGSQ
SHQKPRKVKG MGKLSKADIG TPSNFKHVTH VGWDPHSGFD LSGEEDTLKP FLAKAGVRDQ
HLKDRDTCAF IYDFIQTNNV LGQVKWESSG KKQKPPAPPP VPVRSQTQPT QAESSEGFPS
LSPQHAHLPI LPHEQHQNQA GGNTAPPLQP DNGQRNPPPP PPHRTLPPLP PTTPPKVAGS
GGPPAVTRPP PPLQSAPGPP PPPPPPPAMT GGPMPPPPPP AMMPPVKGLA PAIPGGAAGG
AQDDRSALLD SIRKGTTLKK VDQSALSTGS SSGDTRGDLM YEIQKGFQLR PVADRELGNA
PGDRNSAGGG DVGTDALADA LRRALAERGR VIQPSDEEDS DSESNNTDWE D
//
