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WDR1_XENTR
ID   WDR1_XENTR              Reviewed;         607 AA.
AC   Q6DIF4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=WD repeat-containing protein 1;
DE   AltName: Full=Actin-interacting protein 1;
DE            Short=AIP1;
GN   Name=wdr1 {ECO:0000312|EMBL:AAH75588.1};
GN   Synonyms=aip1 {ECO:0000250|UniProtKB:Q9W7F2};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAH75588.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula {ECO:0000312|EMBL:AAH75588.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) 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; BC075588; AAH75588.1; -; mRNA.
DR   RefSeq; NP_001006781.1; NM_001006780.1.
DR   AlphaFoldDB; Q6DIF4; -.
DR   SMR; Q6DIF4; -.
DR   STRING; 8364.ENSXETP00000064033; -.
DR   DNASU; 448473; -.
DR   GeneID; 448473; -.
DR   KEGG; xtr:448473; -.
DR   CTD; 9948; -.
DR   Xenbase; XB-GENE-489897; wdr1.
DR   eggNOG; KOG0318; Eukaryota.
DR   InParanoid; Q6DIF4; -.
DR   OrthoDB; 325552at2759; -.
DR   Reactome; R-XTR-114608; Platelet degranulation.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
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:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR   GO; GO:0030043; P:actin filament fragmentation; ISS:UniProtKB.
DR   GO; GO:0040011; P:locomotion; IBA:GO_Central.
DR   GO; GO:0030836; P:positive regulation of actin filament depolymerization; IBA:GO_Central.
DR   GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 2.
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; PF00400; WD40; 5.
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"
FT                   /id="PRO_0000289069"
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;  66311 MW;  62EB98B658E90395 CRC64;
     MPYELKKVFA SLPQVERGVA KIITGDPKGN NFLYTNGKSV IIRNIENPAI ADIYTEHAHP
     VVVARYAPSG FYIASGDTSG KLRIWDTTQK EHLLKYEYQP FAGKIKDIAW TEDSKRIAVV
     GEGREKFGSV FLWDTGSSVG EISGNIKVIN SVDIKQTRPY RLVTGSDDNC CAFFEGPPFK
     FKFTMADHSR FVNCVRFSPD GSRLASAGAD GQIFLYDGKT GEKVGNLGGS KAHDGGIYAV
     SWSADSTQLL SASGDKTAKI WDVAANSAVT TFHLGTEVLD QQLGCLWQKD YLLSVSLSGY
     INYLDKNNPS RPLRVIKGHN KSIQCMTVHN SDGRSTIYTG SHDGHINYWD AETGENDTFT
     GKGHTNQVSR MDLDSSNQLI TCSMDDTVRY TSLTSKDYSS SESVKMDVQP KCVAVGSGGY
     VVTLCIGQIV LLKDKKKVFA IDSLDYEPEA VAIHKGSGTV AVGGVDGNVH LYSIQGNSLK
     DEGKSLPVKG AVTDLAYSHD GAFLAVTDAN KVVTVFNVAD GYSEQNVYYG HHAKAVSVAW
     SPDNEHFASS GMDMMVYVWT LSDPDARIKI PDAHRLHHVS SLAWLDEHTL ATVSHDACVK
     QWTVTFK
 
 
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