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COF1

Gene
COF1
Protein
Cofilin
Organism
Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084)
Length
153 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
16.969 kDa
Sequence
MSQSGATVSQDCITAFNDLKLNKKYKFIVYKLSDDYKEIVIDKASESRDWEDFRETLVNATAKSRTGAVGKGPRYAVYDFEYNLASGDGIRNKITFIAWSPDDAGIQPKMIYASSKEALKRSLTGIATELQANDTDDIEYDSILKTVSKGLAA

Gene
COF1
Protein
Cofilin
Organism
Yarrowia lipolytica (strain CLIB 122 / E 150)
Length
153 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
17.029 kDa
Sequence
MFQPCCSKSTMSRSGVAVNDSALQAFNELKLGKKVTFIIYKINDAKTEIVVEEEGTTDSYDTFLGKLPENDCRYAVYDFEYEISSGEGKRSKLVFFTWSPDTAPVRSKMIYASSKDSLRRALTGISTEIQGTDFSEVAYESVLERVSRGAGSH

Gene
COF1
Protein
Cofilin
Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
Length
143 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
15.902 kDa
Sequence
MSRSGVAVADESLTAFNDLKLGKKYKFVLFGLNADKTSIIVKETSNERDYDVFLEKLPEDDCLYAVYDFEYEISGAEGKRSKIVFFTWSPDTAPIRSKMVYASSKDALRRALNGVSSDIQGTDFSEVAYESVLEKVSRGAGSH

Gene
COF1
Protein
Cofilin
Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Length
143 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
15.902 kDa
Sequence
MSRSGVAVADESIQAFNDLKLGMKYKFVLFSLNDAKTEIVVKETSSDPSYDAFLEKLPENDCLYAVYDFEYQISESEGKRSKIVFFTWSPDTASVRPKMVYASSKDALKRALNGVAIEIQGTDFSEVSYEAVLEKVSRGAGSH

Gene
COF1
Protein
Cofilin
Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968)
Length
143 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
15.86 kDa
Sequence
MSRSGVAVADESLTAFNDLKLGKKYKFIIFALNDQKTEIVVEETSNNSDYDAFLEKLPENECKYAIYDFEYEIGGGEGKRSKIVFFTWSPDTAPIKSKMIYASSKDALRRALNGVSSDVQGTDFSEVAYESVLDRVSKGAGSH

Gene
COF1
Protein
Cofilin
Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
Length
143 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
16.044 kDa
Sequence
MSRSGVAVADESLNAFNDLKLGKKYKFILYALNDSKTEIIVKETSAEQDYDKFLEQLPENDCLYAVYDFEYELGNNEGKRSKIVFFTWSPDTAPVRSKMVYASSKDALRRALNGVSSDIQGTDFSEVAYESVLEKVSRAAGSH

Gene
COF1
Protein
Cofilin
Organism
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
Length
143 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
15.971 kDa
Sequence
MSRSGVAVSDEALKAFNDLKLGKKFKSIIYKLNDAKTEIVVDSTSTEDAYDAFVEDLPENDCRYAVYDFEYEVGQGDGKRNKIVFYQWSPDTASVRAKMVYASSKDALRRALNGIGTEIQGTDFSEVAYESVLEKISRTTGLH

Gene
COF1
Protein
Cofilin
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
143 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton. In effect, yeast cofilin increases the rate of actin polymerization by making new ends available for actin subunit addition. Such a protein complex is important for the polarized growth of yeast cells.
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
15.901 kDa
Sequence
MSRSGVAVADESLTAFNDLKLGKKYKFILFGLNDAKTEIVVKETSTDPSYDAFLEKLPENDCLYAIYDFEYEINGNEGKRSKIVFFTWSPDTAPVRSKMVYASSKDALRRALNGVSTDVQGTDFSEVSYDSVLERVSRGAGSH

Gene
cof1
Protein
Cofilin
Organism
Zygosaccharomyces rouxii
Length
143 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
15.882 kDa
Sequence
MSRSGVSVADESLQAFNDLKLGKKYKFVLYGISEDKTTIVVKETSTSQSYDEFLGKLPENDCLYAIYDFEYEIGGNEGKRSKIVFFTWSPDTAPVRSKMVYASSKDALRRALTGVSSDIQGTDFSEVSFETVLERVSKSAGSH

Gene
COF1
Protein
Cofilin
Organism
Ustilago maydis (strain 521 / FGSC 9021)
Length
139 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
15.744 kDa
Sequence
MSSGVKVSQECLDKFQELKLGKKIKYIIYSLNDKNTEIVVQNTSTSTSYDDFLAELPPTECRYAIYDFEYEKGDAGKRNKICFFSWSPDDAKIKPKMVFASSKDALRKALVGISTEIQGTDFSEVSYDTVLDKVSRSTF

Gene
COF1
Protein
Cofilin
Organism
Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
Length
138 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
15.738 kDa
Sequence
MSSGVQPTQECLEKFQELKTGKKLTYVIYGLSEDKRSIVVLKASEDKDFDSFVAELPEKDCRWAVYDFEFTLPGGEGVRNKLCFIVWSPDDASVKNKMIFASSKEAIRRRLDGIHTEIQATDFSEITKDALFEKATRK

Gene
COF1
Protein
Cofilin
Organism
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565)
Length
138 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
15.738 kDa
Sequence
MSSGVQPTQECLEKFQELKTGKKLTYVIYGLSEDKRSIVVLKASEDKDFDSFVAELPEKDCRWAVYDFEFTLPGGEGVRNKLCFIVWSPDDASVKNKMIFASSKEAIRRRLDGIHTEIQATDFSEITKDALFEKATRK

Gene
cof1
Protein
Cofilin
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Length
137 amino acids
Function
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton.
Similarity
Belongs to the actin-binding proteins ADF family.
Mass
15.62 kDa
Sequence
MSFSGVKVSPECLEAFQELKLGKSLRYVVFKMNDTKTEIVVEKKSTDKDFDTFLGDLPEKDCRYAIYDFEFNLGEGVRNKIIFISWSPDVAPIKSKMVYSSSKDTLRRAFTGIGTDIQATDFSEVAYETVLEKVTRK