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TWF2_DANRE
ID   TWF2_DANRE              Reviewed;         347 AA.
AC   Q6GMH3;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Twinfilin-2;
DE   AltName: Full=Twinfilin-1-like protein;
GN   Name=twf2; Synonyms=ptk9l, twf1l; ORFNames=zgc:91817;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Actin-binding protein involved in motile and morphological
CC       processes. Inhibits actin polymerization, likely by sequestering G-
CC       actin (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with G-actin; ADP-actin form and capping protein
CC       (CP). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC       perinuclear region {ECO:0000250}. Note=Perinuclear and G-actin-rich
CC       cortical actin structure sublocalization. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. Twinfilin
CC       subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular embrace - Issue 73
CC       of August 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/073";
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DR   EMBL; BC074077; AAH74077.1; -; mRNA.
DR   RefSeq; NP_001009897.1; NM_001009897.2.
DR   AlphaFoldDB; Q6GMH3; -.
DR   SMR; Q6GMH3; -.
DR   STRING; 7955.ENSDARP00000024168; -.
DR   PaxDb; Q6GMH3; -.
DR   Ensembl; ENSDART00000065006; ENSDARP00000065005; ENSDARG00000094792.
DR   GeneID; 100310784; -.
DR   KEGG; dre:100310784; -.
DR   CTD; 11344; -.
DR   ZFIN; ZDB-GENE-030131-7638; twf2a.
DR   GeneTree; ENSGT00530000063868; -.
DR   HOGENOM; CLU_031995_1_0_1; -.
DR   InParanoid; Q6GMH3; -.
DR   PhylomeDB; Q6GMH3; -.
DR   TreeFam; TF352598; -.
DR   PRO; PR:Q6GMH3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 6.
DR   Bgee; ENSDARG00000094792; Expressed in muscle tissue and 14 other tissues.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR   GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR   GO; GO:0010591; P:regulation of lamellipodium assembly; IBA:GO_Central.
DR   GO; GO:0042989; P:sequestering of actin monomers; IBA:GO_Central.
DR   Gene3D; 3.40.20.10; -; 2.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR028458; Twinfilin.
DR   PANTHER; PTHR13759; PTHR13759; 1.
DR   Pfam; PF00241; Cofilin_ADF; 2.
DR   SMART; SM00102; ADF; 2.
DR   PROSITE; PS51263; ADF_H; 2.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome; Repeat.
FT   CHAIN           1..347
FT                   /note="Twinfilin-2"
FT                   /id="PRO_0000233140"
FT   DOMAIN          3..137
FT                   /note="ADF-H 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   DOMAIN          175..311
FT                   /note="ADF-H 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   REGION          314..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   347 AA;  39859 MW;  948D3BCD3A0D7B21 CRC64;
     MFLVLVVTEE LREFLARARN GTGRLIQVLI RDEQLVLGAY REPRHSWDKD YDPVLLPLLD
     PLEPCYILYR LDSKNAQGYE WLFISWSPDQ SPVRQKMLYA ATRATVKKEF GGGHVKDEMF
     GTVEEDICLQ GYLRHITSCS APAPLTVAEQ ELQRIKITEV KAEISVDPKH QTLQGLAFPL
     QAEAKRALKQ LAERRINYIQ LKLDTEKETI DLVHTSPTDI RDLPCRIPLD TPRYHFFLYK
     HSHEGDYLES VVFIYSMPGY SCSIKERMLY SSCKSRLLDE VERDFHLEVA KKLEIDSGEE
     LTEEYLYDEV HPKQHAHKQA FAKPRGPAGK RGNKRLIKGG GENGGNS
 
 
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