COTL1_MOUSE
ID COTL1_MOUSE Reviewed; 142 AA.
AC Q9CQI6;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Coactosin-like protein;
GN Name=Cotl1; Synonyms=Clp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas, Small intestine, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
RP PROTEIN SEQUENCE OF 19-30, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP FUNCTION, AND INTERACTION WITH 5-LIPOXYGENASE.
RX PubMed=11785969; DOI=10.1006/bbrc.2001.6236;
RA Doucet J., Provost P., Samuelsson B., Radmark O.;
RT "Molecular cloning and functional characterization of mouse coactosin-like
RT protein.";
RL Biochem. Biophys. Res. Commun. 290:783-789(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP STRUCTURE BY NMR.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of coactosin-like protein (cofilin family) from Mus
RT musculus.";
RL Submitted (MAY-2004) to the PDB data bank.
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, ECO:0000269|PubMed:11785969}.
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; AK010052; BAB26668.1; -; mRNA.
DR EMBL; AK007994; BAB25396.1; -; mRNA.
DR EMBL; AK008085; BAB25450.1; -; mRNA.
DR EMBL; BC011068; AAH11068.1; -; mRNA.
DR EMBL; BC010249; AAH10249.1; -; mRNA.
DR CCDS; CCDS22712.1; -.
DR RefSeq; NP_082347.1; NM_028071.3.
DR PDB; 1UDM; NMR; -; A=1-142.
DR PDB; 1WM4; NMR; -; A=1-142.
DR PDBsum; 1UDM; -.
DR PDBsum; 1WM4; -.
DR AlphaFoldDB; Q9CQI6; -.
DR BMRB; Q9CQI6; -.
DR SMR; Q9CQI6; -.
DR BioGRID; 215111; 7.
DR IntAct; Q9CQI6; 1.
DR STRING; 10090.ENSMUSP00000034285; -.
DR iPTMnet; Q9CQI6; -.
DR PhosphoSitePlus; Q9CQI6; -.
DR SwissPalm; Q9CQI6; -.
DR UCD-2DPAGE; Q9CQI6; -.
DR CPTAC; non-CPTAC-3778; -.
DR EPD; Q9CQI6; -.
DR jPOST; Q9CQI6; -.
DR MaxQB; Q9CQI6; -.
DR PaxDb; Q9CQI6; -.
DR PRIDE; Q9CQI6; -.
DR ProteomicsDB; 277997; -.
DR TopDownProteomics; Q9CQI6; -.
DR Antibodypedia; 30596; 351 antibodies from 30 providers.
DR DNASU; 72042; -.
DR Ensembl; ENSMUST00000034285; ENSMUSP00000034285; ENSMUSG00000031827.
DR Ensembl; ENSMUST00000168698; ENSMUSP00000126329; ENSMUSG00000031827.
DR GeneID; 72042; -.
DR KEGG; mmu:72042; -.
DR UCSC; uc012glt.1; mouse.
DR CTD; 23406; -.
DR MGI; MGI:1919292; Cotl1.
DR VEuPathDB; HostDB:ENSMUSG00000031827; -.
DR eggNOG; KOG3655; Eukaryota.
DR GeneTree; ENSGT00390000012498; -.
DR HOGENOM; CLU_129657_1_0_1; -.
DR InParanoid; Q9CQI6; -.
DR OMA; KSETTWL; -.
DR OrthoDB; 1424839at2759; -.
DR PhylomeDB; Q9CQI6; -.
DR TreeFam; TF324318; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 72042; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Cotl1; mouse.
DR EvolutionaryTrace; Q9CQI6; -.
DR PRO; PR:Q9CQI6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9CQI6; protein.
DR Bgee; ENSMUSG00000031827; Expressed in granulocyte and 257 other tissues.
DR ExpressionAtlas; Q9CQI6; baseline and differential.
DR Genevisible; Q9CQI6; MM.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
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 3D-structure; Acetylation; Actin-binding; Chaperone; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Nucleus; Phosphoprotein;
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_0000214955"
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 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B0BNA5"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:1UDM"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:1WM4"
FT STRAND 25..43
FT /evidence="ECO:0007829|PDB:1UDM"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:1UDM"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1UDM"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:1WM4"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1UDM"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1UDM"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:1UDM"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1UDM"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:1UDM"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1UDM"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:1UDM"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:1UDM"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:1WM4"
SQ SEQUENCE 142 AA; 15944 MW; 88CB1BF12447ABC8 CRC64;
MATKIDKEAC RAAYNLVRDD GSAVIWVTFR YDGATIVPGD QGADYQHFIQ QCTDDVRLFA
FVRFTTGDAM SKRSKFALIT WIGEDVSGLQ RAKTGTDKTL VKEVVQNFAK EFVISDRKEL
EEDFIRSELK KAGGANYDAQ SE
