COTL1_RAT
ID COTL1_RAT Reviewed; 142 AA.
AC B0BNA5;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Coactosin-like protein {ECO:0000250|UniProtKB:Q14019};
GN Name=Cotl1 {ECO:0000312|EMBL:AAI58747.1, ECO:0000312|RGD:1305498};
GN Synonyms=Clp {ECO:0000250|UniProtKB:Q14019};
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] {ECO:0000305, ECO:0000312|EMBL:EDL92684.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:EDL92684.1};
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAI58747.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway/Mcwi {ECO:0000269|PubMed:15489334};
RC TISSUE=Spleen {ECO:0000312|EMBL:AAI58747.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:EDL92684.1}
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (MAR-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-141, 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: 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:0000255}.
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DR EMBL; CH473972; EDL92684.1; -; Genomic_DNA.
DR EMBL; CH473972; EDL92686.1; -; Genomic_DNA.
DR EMBL; BC158746; AAI58747.1; -; mRNA.
DR RefSeq; NP_001101922.1; NM_001108452.1.
DR AlphaFoldDB; B0BNA5; -.
DR BMRB; B0BNA5; -.
DR SMR; B0BNA5; -.
DR STRING; 10116.ENSRNOP00000021954; -.
DR iPTMnet; B0BNA5; -.
DR PhosphoSitePlus; B0BNA5; -.
DR SwissPalm; B0BNA5; -.
DR jPOST; B0BNA5; -.
DR PaxDb; B0BNA5; -.
DR PeptideAtlas; B0BNA5; -.
DR PRIDE; B0BNA5; -.
DR GeneID; 361422; -.
DR KEGG; rno:361422; -.
DR UCSC; RGD:1305498; rat.
DR CTD; 23406; -.
DR RGD; 1305498; Cotl1.
DR VEuPathDB; HostDB:ENSRNOG00000016257; -.
DR eggNOG; KOG3655; Eukaryota.
DR HOGENOM; CLU_129657_1_0_1; -.
DR InParanoid; B0BNA5; -.
DR OMA; KSETTWL; -.
DR OrthoDB; 1424839at2759; -.
DR PhylomeDB; B0BNA5; -.
DR TreeFam; TF324318; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:B0BNA5; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Proteomes; UP000234681; Chromosome 19.
DR Bgee; ENSRNOG00000016257; Expressed in spleen and 19 other tissues.
DR Genevisible; B0BNA5; RN.
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:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0050832; P:defense response to fungus; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Actin-binding; Chaperone; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; 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_0000365097"
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 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14019"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 142 AA; 15932 MW; 9257309C928ED5FD CRC64;
MATKIDKEAC RAAYNLVRDD GSSVIWVTFK YDGATIVPGD QGADYQHFIQ QCTDDVRLFA
FVRFTTGDAM SKRSKFALIT WIGEDVSGLQ RAKTGTDKTL VKEVVQNFAK EFVISDRKEL
EEDFIRSELK KAGGANYDAQ SE
