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COF2_DICDI
ID   COF2_DICDI              Reviewed;         143 AA.
AC   Q966T6; Q556H4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cofilin-2;
GN   Name=cofC-1; Synonyms=dcof3; ORFNames=DDB_G0272568;
GN   and
GN   Name=cofC-2; Synonyms=dcof3; ORFNames=DDB_G0274059;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=AX2;
RX   PubMed=11683919; DOI=10.1046/j.1365-2443.2001.00470.x;
RA   Aizawa H., Kishi Y., Iida K., Sameshima M., Yahara I.;
RT   "Cofilin-2, a novel type of cofilin, is expressed specifically at
RT   aggregation stage of Dictyostelium discoideum development.";
RL   Genes Cells 6:913-921(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Controls reversibly actin polymerization and depolymerization
CC       in a pH-sensitive manner. It has the ability to bind G- and F-actin in
CC       a 1:1 ratio of cofilin to actin. It is the major component of
CC       intranuclear and cytoplasmic actin rods. Cofilin-2 may play a distinct
CC       role from that of cofilin-1 in destabilization of the actin
CC       cytoskeleton during Dictyostelium development.
CC       {ECO:0000269|PubMed:11683919}.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Cytoplasm,
CC       cytoskeleton {ECO:0000250}. Note=Localizes at substrate adhesion sites.
CC       {ECO:0000269|PubMed:11683919}.
CC   -!- DEVELOPMENTAL STAGE: Not expressed in vegetative cells, but is
CC       transiently induced during the aggregation stage of development.
CC       {ECO:0000269|PubMed:11683919}.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC       AX4. These strains contain a duplication of a segment of 750 kb of
CC       chromosome 2 compared to the corresponding sequence in strain AX2.
CC       {ECO:0000305}.
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DR   EMBL; AB055926; BAB62414.1; -; Genomic_DNA.
DR   EMBL; AAFI02000011; EAL70463.1; -; Genomic_DNA.
DR   EMBL; AAFI02000009; EAL70921.1; -; Genomic_DNA.
DR   RefSeq; XP_644388.1; XM_639296.1.
DR   RefSeq; XP_645025.1; XM_639933.1.
DR   AlphaFoldDB; Q966T6; -.
DR   SMR; Q966T6; -.
DR   STRING; 44689.DDB0185192; -.
DR   PaxDb; Q966T6; -.
DR   EnsemblProtists; EAL70463; EAL70463; DDB_G0274059.
DR   EnsemblProtists; EAL70921; EAL70921; DDB_G0272568.
DR   GeneID; 8618702; -.
DR   GeneID; 8619274; -.
DR   KEGG; ddi:DDB_G0272568; -.
DR   KEGG; ddi:DDB_G0274059; -.
DR   dictyBase; DDB_G0272568; cofC-1.
DR   dictyBase; DDB_G0274059; cofC-2.
DR   eggNOG; KOG1735; Eukaryota.
DR   HOGENOM; CLU_1809787_0_0_1; -.
DR   InParanoid; Q966T6; -.
DR   PhylomeDB; Q966T6; -.
DR   PRO; PR:Q966T6; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:dictyBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0030042; P:actin filament depolymerization; IDA:dictyBase.
DR   GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR   CDD; cd11286; ADF_cofilin_like; 1.
DR   Gene3D; 3.40.20.10; -; 1.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR017904; ADF/Cofilin.
DR   PANTHER; PTHR11913; PTHR11913; 1.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   SMART; SM00102; ADF; 1.
DR   PROSITE; PS51263; ADF_H; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome.
FT   CHAIN           1..143
FT                   /note="Cofilin-2"
FT                   /id="PRO_0000311819"
FT   DOMAIN          10..139
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
SQ   SEQUENCE   143 AA;  16362 MW;  A78731198E6F40B2 CRC64;
     MSAPLSPSPT VVKLSPECQQ YYQDVRIKNK YQGVVYKINK ESNQMIIDKT FPNDCNFNEL
     TQCFKENECC IIVFKYVISN SQSKLFFIYW GSETAPQTDK VLYSNAKLTL AITLKGIDIK
     IAGTKKSELT EEIFKERAIP KQA
 
 
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