WDR1B_XENLA
ID WDR1B_XENLA Reviewed; 607 AA.
AC Q6PAX7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=WD repeat-containing protein 1-B;
DE AltName: Full=Actin-interacting protein 1-B;
DE Short=xAIP1-B;
GN Name=wdr1-b; Synonyms=aip1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH60007.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH60007.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Induces disassembly of actin filaments in conjunction with
CC ADF/cofilin family proteins. Doesn't sever actin filaments alone, but
CC caps the barbed ends of filaments severed by cofilin, which blocks
CC annealing and depolymerization and allows more extensive severing by
CC cofilin (By similarity). {ECO:0000250|UniProtKB:Q9W7F2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9W7F2}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus
CC {ECO:0000250|UniProtKB:Q9W7F2}.
CC -!- SIMILARITY: Belongs to the WD repeat AIP1 family. {ECO:0000255}.
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DR EMBL; BC060007; AAH60007.1; -; mRNA.
DR RefSeq; NP_001083198.1; NM_001089729.1.
DR AlphaFoldDB; Q6PAX7; -.
DR SMR; Q6PAX7; -.
DR DNASU; 398797; -.
DR GeneID; 398797; -.
DR KEGG; xla:398797; -.
DR CTD; 398797; -.
DR Xenbase; XB-GENE-865912; wdr1.S.
DR OrthoDB; 325552at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 398797; Expressed in brain and 19 other tissues.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0030043; P:actin filament fragmentation; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011045; N2O_reductase_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50974; SSF50974; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Nucleus;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..607
FT /note="WD repeat-containing protein 1-B"
FT /id="PRO_0000289068"
FT REPEAT 4..45
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 48..87
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 93..135
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 138..176
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 180..218
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 224..263
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 270..306
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 311..351
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REPEAT 358..408
FT /note="WD 9"
FT /evidence="ECO:0000255"
FT REPEAT 432..474
FT /note="WD 10"
FT /evidence="ECO:0000255"
FT REPEAT 480..518
FT /note="WD 11"
FT /evidence="ECO:0000255"
FT REPEAT 523..561
FT /note="WD 12"
FT /evidence="ECO:0000255"
FT REPEAT 566..604
FT /note="WD 13"
FT /evidence="ECO:0000255"
SQ SEQUENCE 607 AA; 66169 MW; 1E82176B3D9E595D CRC64;
MPYEIKKVFA SLPQVERGVA KIIAGDPKGN NFLYTNGKSV IIRNIDNPAI ADIYTEHAHQ
VVVARYAPSG FYIASGDTSG KLRIWDTTQK EHLLKYEYQP FAGKIKDIAW TEDSKRIAVV
GEGREKFGSV FLWDTGSSVG EIIGNIKVIN SVDIKQTRPY RLVTGSDDNC CAFFEGPPFK
FKFTMSDHSR FVNCVRFSPD GSRLASAGAD GQIFLYDGKT GEKVCSLGGS KAHDGGIYAV
SWSPDGTQLL SASGDKTAKI WDVAANSAVT TFNLGSDVLD QQLGCLWQKD YLLSVSLSGY
INYLDKNNPA KPFRIIKGHN KSIQCMTVDK SDGRSTIYTG SHDGHINYWD AETGENNTFT
GKGHTNQVSS MDLDGSSQLI TCSMDDTLRY TNLISKDYSS SESVKMDVQP KCVAVGSGGY
VVTVCIGQIV LLKDKKKVFA IDSLDYEPEA VAIHKGSGTV SVGGADGKVH LYSIQGNSLK
DEGKTLPAKG AVTDLAYSPD GAFLAVTDAN KVVTVFSVAD GYSEHNSYYG HHAKALSVAW
SPDNEHFASS GMDMMVYVWT LSDPDTRIKM PDAHRLHHVS SLAWLDENTL ATVSHDACVK
QWTVTFK