CNN3_MOUSE
ID CNN3_MOUSE Reviewed; 330 AA.
AC Q9DAW9; Q3TW23;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Calponin-3;
DE AltName: Full=Calponin, acidic isoform;
GN Name=Cnn3;
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=Amnion, Liver, Placenta, and Spinal ganglion;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Thin filament-associated protein that is implicated in the
CC regulation and modulation of smooth muscle contraction. It is capable
CC of binding to actin, calmodulin and tropomyosin. The interaction of
CC calponin with actin inhibits the actomyosin Mg-ATPase activity (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
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DR EMBL; AK005460; BAB24051.1; -; mRNA.
DR EMBL; AK051628; BAC34697.1; -; mRNA.
DR EMBL; AK159555; BAE35180.1; -; mRNA.
DR EMBL; AK159871; BAE35444.1; -; mRNA.
DR EMBL; AK166578; BAE38867.1; -; mRNA.
DR EMBL; AK167201; BAE39329.1; -; mRNA.
DR EMBL; AK167613; BAE39666.1; -; mRNA.
DR EMBL; AK169021; BAE40817.1; -; mRNA.
DR EMBL; AK169098; BAE40881.1; -; mRNA.
DR EMBL; AK169410; BAE41156.1; -; mRNA.
DR EMBL; BC055711; AAH55711.1; -; mRNA.
DR EMBL; BC085268; AAH85268.1; -; mRNA.
DR CCDS; CCDS17802.1; -.
DR RefSeq; NP_082320.1; NM_028044.2.
DR AlphaFoldDB; Q9DAW9; -.
DR SMR; Q9DAW9; -.
DR BioGRID; 215081; 35.
DR IntAct; Q9DAW9; 3.
DR MINT; Q9DAW9; -.
DR STRING; 10090.ENSMUSP00000029773; -.
DR iPTMnet; Q9DAW9; -.
DR PhosphoSitePlus; Q9DAW9; -.
DR EPD; Q9DAW9; -.
DR jPOST; Q9DAW9; -.
DR MaxQB; Q9DAW9; -.
DR PaxDb; Q9DAW9; -.
DR PeptideAtlas; Q9DAW9; -.
DR PRIDE; Q9DAW9; -.
DR ProteomicsDB; 285512; -.
DR Antibodypedia; 4078; 232 antibodies from 35 providers.
DR DNASU; 71994; -.
DR Ensembl; ENSMUST00000029773; ENSMUSP00000029773; ENSMUSG00000053931.
DR GeneID; 71994; -.
DR KEGG; mmu:71994; -.
DR UCSC; uc008rdy.1; mouse.
DR CTD; 1266; -.
DR MGI; MGI:1919244; Cnn3.
DR VEuPathDB; HostDB:ENSMUSG00000053931; -.
DR eggNOG; KOG2046; Eukaryota.
DR GeneTree; ENSGT00940000154539; -.
DR HOGENOM; CLU_055232_0_1_1; -.
DR InParanoid; Q9DAW9; -.
DR OMA; TMTHFNK; -.
DR OrthoDB; 861989at2759; -.
DR PhylomeDB; Q9DAW9; -.
DR TreeFam; TF313921; -.
DR BioGRID-ORCS; 71994; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Cnn3; mouse.
DR PRO; PR:Q9DAW9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9DAW9; protein.
DR Bgee; ENSMUSG00000053931; Expressed in pharyngeal arch 2 and 258 other tissues.
DR ExpressionAtlas; Q9DAW9; baseline and differential.
DR Genevisible; Q9DAW9; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; ISO:MGI.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001997; Calponin/LIMCH1.
DR InterPro; IPR000557; Calponin_repeat.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR003096; SM22_calponin.
DR Pfam; PF00402; Calponin; 3.
DR Pfam; PF00307; CH; 1.
DR PRINTS; PR00889; CALPONIN.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS01052; CALPONIN_1; 3.
DR PROSITE; PS51122; CALPONIN_2; 3.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Calmodulin-binding; Methylation;
KW Reference proteome; Repeat.
FT CHAIN 1..330
FT /note="Calponin-3"
FT /id="PRO_0000204777"
FT DOMAIN 26..130
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 164..189
FT /note="Calponin-like 1"
FT REPEAT 204..229
FT /note="Calponin-like 2"
FT REPEAT 243..268
FT /note="Calponin-like 3"
FT REGION 279..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 158
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15417"
SQ SEQUENCE 330 AA; 36429 MW; FF448A33F29B2C90 CRC64;
MTHFNKGPSY GLSAEVKNKI ASKYDQQAEE DLRNWIEEVT GLGIGTNFQL GLKDGIILCE
LINKLQPGSV KKVNESSLNW PQLENIGNFI KAIQAYGMKP HDIFEANDLF ENGNMTQVQT
TLVALAGLAK TKGFHTTIDI GVKYAEKQTR RFDEGKLKAG QSVIGLQMGT NKCASQAGMT
AYGTRRHLYD PKMQTDKPFD QTTISLQMGT NKGASQAGML APGTRRDIYD QKLTLQPVDN
STISLQMGTN KVASQKGMSV YGLGRQVYDP KYCAAPTEPV IHNGSQGTGT NGSEISDSDY
QAEYPDEYHG EYPDDYPREY QYGDDQGIDY
