ID   COTL1_BOVIN             Reviewed;         142 AA.
AC   Q2HJ57;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Coactosin-like protein;
GN   Name=COTL1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to F-actin in a calcium-independent manner. Has no
CC       direct effect on actin depolymerization. Acts as a chaperone for ALOX5
CC       (5LO), influencing both its stability and activity in leukotrienes
CC       synthesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with 5-lipoxygenase (ALOX5/5LO) in a calcium-
CC       independent manner. Binds to F-actin with a stoichiometry of 1:2 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14019}.
CC       Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14019}. Nucleus
CC       {ECO:0000250|UniProtKB:Q14019}.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. Coactosin
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC113301; AAI13302.1; -; mRNA.
DR   RefSeq; NP_001040058.1; NM_001046593.1.
DR   RefSeq; XP_005218454.1; XM_005218397.1.
DR   AlphaFoldDB; Q2HJ57; -.
DR   BMRB; Q2HJ57; -.
DR   SMR; Q2HJ57; -.
DR   STRING; 9913.ENSBTAP00000021704; -.
DR   PaxDb; Q2HJ57; -.
DR   PRIDE; Q2HJ57; -.
DR   Ensembl; ENSBTAT00000021704; ENSBTAP00000021704; ENSBTAG00000016315.
DR   GeneID; 617165; -.
DR   KEGG; bta:617165; -.
DR   CTD; 23406; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016315; -.
DR   VGNC; VGNC:27626; COTL1.
DR   eggNOG; KOG3655; Eukaryota.
DR   GeneTree; ENSGT00390000012498; -.
DR   HOGENOM; CLU_129657_1_0_1; -.
DR   InParanoid; Q2HJ57; -.
DR   OMA; KSETTWL; -.
DR   OrthoDB; 1424839at2759; -.
DR   TreeFam; TF324318; -.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000016315; Expressed in leukocyte and 105 other tissues.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0050832; P:defense response to fungus; IEA:Ensembl.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR   Gene3D; 3.40.20.10; -; 1.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR030502; CLP.
DR   PANTHER; PTHR10829:SF29; PTHR10829:SF29; 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   Acetylation; Actin-binding; Chaperone; Cytoplasm; Cytoskeleton; Nucleus;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q14019"
FT   CHAIN           2..142
FT                   /note="Coactosin-like protein"
FT                   /id="PRO_0000244595"
FT   DOMAIN          2..130
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   REGION          66..75
FT                   /note="Flexible and important for F-actin binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14019"
FT   MOD_RES         102
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14019"
FT   MOD_RES         126
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14019"
SQ   SEQUENCE   142 AA;  16010 MW;  31CBB907D906E35F CRC64;
     MATKIDKEAC RTAYNLVRDD SSAVIWVTFK YDGSTIVPGE QGAEYQDFIQ QCTDDVRLFA
     FVRFTTGDAM SKRSKFALIT WIGENVSGLQ RAKTGTDKTL VKEVVQNFAK EFVISDRKEL
     EEDFIKNELK KAGGANYDAQ TE