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Database: UniProt
Entry: D3Z7R6_MOUSE
LinkDB: D3Z7R6_MOUSE
Original site: D3Z7R6_MOUSE 
ID   D3Z7R6_MOUSE            Unreviewed;       266 AA.
AC   D3Z7R6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Calponin {ECO:0000256|RuleBase:RU361224};
GN   Name=Cnn2 {ECO:0000313|Ensembl:ENSMUSP00000101013.2,
GN   ECO:0000313|MGI:MGI:105093};
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 {ECO:0000313|Ensembl:ENSMUSP00000101013.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000101013.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000101013.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [3] {ECO:0007829|PubMed:23806337}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000101013.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000101013.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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.
CC       {ECO:0000256|ARBA:ARBA00025109, ECO:0000256|RuleBase:RU361224}.
CC   -!- SIMILARITY: Belongs to the calponin family.
CC       {ECO:0000256|ARBA:ARBA00009631, ECO:0000256|RuleBase:RU361224}.
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DR   AlphaFoldDB; D3Z7R6; -.
DR   SMR; D3Z7R6; -.
DR   jPOST; D3Z7R6; -.
DR   MaxQB; D3Z7R6; -.
DR   PeptideAtlas; D3Z7R6; -.
DR   ProteomicsDB; 364017; -.
DR   Antibodypedia; 22499; 484 antibodies from 38 providers.
DR   Ensembl; ENSMUST00000105374.2; ENSMUSP00000101013.2; ENSMUSG00000004665.11.
DR   AGR; MGI:105093; -.
DR   MGI; MGI:105093; Cnn2.
DR   VEuPathDB; HostDB:ENSMUSG00000004665; -.
DR   GeneTree; ENSGT00940000154355; -.
DR   ChiTaRS; Cnn2; mouse.
DR   Proteomes; UP000000589; Chromosome 10.
DR   Bgee; ENSMUSG00000004665; Expressed in external carotid artery and 251 other cell types or tissues.
DR   ExpressionAtlas; D3Z7R6; baseline and differential.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR   CDD; cd21283; CH_CNN2; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   InterPro; IPR001997; Calponin/LIMCH1.
DR   InterPro; IPR000557; Calponin_repeat.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR003096; SM22_calponin.
DR   PANTHER; PTHR47385; CALPONIN; 1.
DR   PANTHER; PTHR47385:SF7; CALPONIN-2; 1.
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; Calponin-homology domain, CH-domain; 1.
DR   PROSITE; PS01052; CALPONIN_1; 1.
DR   PROSITE; PS51122; CALPONIN_2; 3.
DR   PROSITE; PS50021; CH; 1.
PE   1: Evidence at protein level;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW   ECO:0000256|RuleBase:RU361224};
KW   Calmodulin-binding {ECO:0000256|RuleBase:RU361224};
KW   Proteomics identification {ECO:0007829|EPD:D3Z7R6,
KW   ECO:0007829|MaxQB:D3Z7R6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          28..132
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
SQ   SEQUENCE   266 AA;  28959 MW;  9F56605C4D92486D CRC64;
     MSSTQFNKGP SYGLSAEVKN RLLSKYDPQK EAELRSWIEG LTGLSIGPDF QKGLKDGVIL
     CTLMNKLQPG SVPKINRSMQ NWHQLENLSN FIKAMVSYGM NPVDLFEAND LFESGNMTQV
     QVSLLALAGK MGTNKCASQS GMTAYGTRRH LYDPKNHILP PMDHCTISLQ MGTNKCASQV
     GMTAPGTRRH IYDTKLGTDK CDNSSMSLQM GYTQGANQSG QVFGLGRQIY DPKYCPQGSA
     ADGAPAGDGQ GEAPEYLAYC QEEAGY
//
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