TWF1_RAT
ID TWF1_RAT Reviewed; 350 AA.
AC Q5RJR2;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Twinfilin-1;
GN Name=Twf1; Synonyms=Ptk9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND SER-277, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Actin-binding protein involved in motile and morphological
CC processes. Inhibits actin polymerization, likely by sequestering G-
CC actin. By capping the barbed ends of filaments, it also regulates
CC motility. Seems to play an important role in clathrin-mediated
CC endocytosis and distribution of endocytic organelles (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with G-actin; ADP-actin form and capping protein
CC (CP). May also be able to interact with TWF2 and phosphoinositides,
CC PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated. Interacts
CC with ACTG1. {ECO:0000250|UniProtKB:Q12792,
CC ECO:0000250|UniProtKB:Q91YR1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Diffuse cytoplasmic localization with perinuclear and G-actin-rich
CC cortical actin structures sublocalization. Also found at membrane
CC ruffles and cell-cell contacts (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine and threonine residues. {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; BC086536; AAH86536.1; -; mRNA.
DR RefSeq; NP_001008521.1; NM_001008521.1.
DR AlphaFoldDB; Q5RJR2; -.
DR SMR; Q5RJR2; -.
DR BioGRID; 260975; 1.
DR IntAct; Q5RJR2; 4.
DR STRING; 10116.ENSRNOP00000030138; -.
DR iPTMnet; Q5RJR2; -.
DR PhosphoSitePlus; Q5RJR2; -.
DR jPOST; Q5RJR2; -.
DR PaxDb; Q5RJR2; -.
DR PRIDE; Q5RJR2; -.
DR GeneID; 315265; -.
DR KEGG; rno:315265; -.
DR CTD; 5756; -.
DR RGD; 1311872; Twf1.
DR VEuPathDB; HostDB:ENSRNOG00000022507; -.
DR eggNOG; KOG1747; Eukaryota.
DR HOGENOM; CLU_031995_1_0_1; -.
DR InParanoid; Q5RJR2; -.
DR OMA; VKKDWER; -.
DR OrthoDB; 1578109at2759; -.
DR PhylomeDB; Q5RJR2; -.
DR TreeFam; TF352598; -.
DR Reactome; R-RNO-9013418; RHOBTB2 GTPase cycle.
DR PRO; PR:Q5RJR2; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000022507; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q5RJR2; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030175; C:filopodium; ISO:RGD.
DR GO; GO:0030016; C:myofibril; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; ISO:RGD.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0043538; P:regulation of actin phosphorylation; ISO:RGD.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IBA:GO_Central.
DR GO; GO:0042989; P:sequestering of actin monomers; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q12792"
FT CHAIN 2..350
FT /note="Twinfilin-1"
FT /id="PRO_0000232406"
FT DOMAIN 2..139
FT /note="ADF-H 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 175..313
FT /note="ADF-H 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT REGION 316..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q12792"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 309
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q12792"
FT MOD_RES 349
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12792"
SQ SEQUENCE 350 AA; 40090 MW; 99706DAA174B8913 CRC64;
MSHQTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVVG SCSPPSDSWE QDYDPFVLPL
LEDKQPCYVL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML YAATRATLKK EFGGGHIKDE
VFGTVKEDVS LHGYRKYLLS QSSPAPLTAA EEELRQIKIS EVQTDVSVDT KHQTLQGVAF
PISRDAFQAL EKLSKRQLNY VQLEIDIKNE TIILANTENT ELKDLPKRIP KDSARYHFFL
YKHSHEGDYL ESIVFIYSMP GYTCSIRERM LYSSCKSPLL DIVERQLQMD VIRKIEIDNG
DELTADFLYD EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAEAEATTD
