ID G9KXK6_MUSPF Unreviewed; 497 AA.
AC G9KXK6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Wiskott-Aldrich syndrome protein family member {ECO:0000256|RuleBase:RU367034};
DE Short=WASP family protein member {ECO:0000256|RuleBase:RU367034};
DE Flags: Fragment;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES09635.1};
RN [1] {ECO:0000313|EMBL:AES09635.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lungs {ECO:0000313|EMBL:AES09635.1};
RX PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA Farooqui A., Kelvin D.J.;
RT "Sequencing, annotation, and characterization of the influenza ferret
RT infectome.";
RL J. Virol. 87:1957-1966(2013).
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; JP021037; AES09635.1; -; mRNA.
DR AlphaFoldDB; G9KXK6; -.
DR HOGENOM; CLU_036022_2_0_1; -.
DR OMA; PDMAYND; -.
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:SF6; WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER 2; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00246; WH2; 1.
DR PROSITE; PS51082; WH2; 1.
PE 2: Evidence at transcript level;
KW Actin-binding {ECO:0000256|RuleBase:RU367034};
KW Cytoplasm {ECO:0000256|RuleBase:RU367034};
KW Cytoskeleton {ECO:0000256|RuleBase:RU367034}.
FT DOMAIN 436..453
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 173..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..275
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..413
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AES09635.1"
FT NON_TER 497
FT /evidence="ECO:0000313|EMBL:AES09635.1"
SQ SEQUENCE 497 AA; 53962 MW; 04F45210B9597073 CRC64;
MPLVTRNIEP RHLCRQTLPS VRSELECVTN ITLANVIRQL GSLSKYAEDI VGELFTQANT
FASRVSSLAE RVDRLQVKVT QLDPKEEEVS LQGINTRKAF RSSTIQDQKL FDRNSLPVPV
LETYNTCDTP PPLNNLTPYR DDGKEALKFY TDPSYFFDLW KEKMLQDTKD IMKEKRKHRK
EKKDNPNRGN VNPRKIKTRK EEWEKMKMGQ EFVESKEKLG PSGYPPTLVY QNGSIGSVEN
VDANSYPPPP LSDSTSPPSP SFSEDSLPPP PAEFSCPADS NQRGPGLAGP KRSSVVSPSH
PPPAPPLGSP PGSKPGFAPP PAPPPPPPMM GVPPPPPPGG FGLPGTPPPP SPSSFPPHPD
FAAPPPPPPP PTADYPTLPP PPLPQPGGGA PPPPPPPPPP GPPPFPSSGA ENPSVAPPPL
SDATKPKSSL PPVSDARSDL LSAIRQGFQL RRVEEQQEQE KRDVVGNDVA TILSRRIAVE
YSDSEDDSSE FDEDDWS
//
