CNN2_MOUSE
ID CNN2_MOUSE Reviewed; 305 AA.
AC Q08093;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Calponin-2;
DE AltName: Full=Calponin H2, smooth muscle;
DE AltName: Full=Neutral calponin;
GN Name=Cnn2;
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 [MRNA].
RC TISSUE=Smooth muscle;
RX PubMed=8370452; DOI=10.1016/0014-5793(93)80909-e;
RA Strasser P., Gimona M., Moessler H., Herzog M., Small J.V.;
RT "Mammalian calponin. Identification and expression of genetic variants.";
RL FEBS Lett. 330:13-18(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N;
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=Heart, Kidney, Liver, Lung, 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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-8, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], 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.
CC -!- TISSUE SPECIFICITY: Smooth muscle, and tissues containing significant
CC amounts of smooth muscle.
CC -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
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DR EMBL; Z19543; CAA79603.1; -; mRNA.
DR EMBL; BC009144; AAH09144.1; -; mRNA.
DR EMBL; BC018482; AAH18482.1; -; mRNA.
DR CCDS; CCDS24003.1; -.
DR PIR; S36147; S31485.
DR RefSeq; NP_031751.1; NM_007725.2.
DR AlphaFoldDB; Q08093; -.
DR SMR; Q08093; -.
DR BioGRID; 198791; 5.
DR IntAct; Q08093; 1.
DR MINT; Q08093; -.
DR STRING; 10090.ENSMUSP00000004784; -.
DR iPTMnet; Q08093; -.
DR PhosphoSitePlus; Q08093; -.
DR EPD; Q08093; -.
DR jPOST; Q08093; -.
DR PaxDb; Q08093; -.
DR PeptideAtlas; Q08093; -.
DR PRIDE; Q08093; -.
DR ProteomicsDB; 283453; -.
DR Antibodypedia; 22499; 419 antibodies from 38 providers.
DR DNASU; 12798; -.
DR Ensembl; ENSMUST00000004784; ENSMUSP00000004784; ENSMUSG00000004665.
DR GeneID; 12798; -.
DR KEGG; mmu:12798; -.
DR UCSC; uc007gaz.1; mouse.
DR CTD; 1265; -.
DR MGI; MGI:105093; Cnn2.
DR VEuPathDB; HostDB:ENSMUSG00000004665; -.
DR eggNOG; KOG2046; Eukaryota.
DR GeneTree; ENSGT00940000154355; -.
DR HOGENOM; CLU_055232_0_2_1; -.
DR InParanoid; Q08093; -.
DR OMA; GKQIGPD; -.
DR OrthoDB; 861989at2759; -.
DR PhylomeDB; Q08093; -.
DR TreeFam; TF313921; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 12798; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cnn2; mouse.
DR PRO; PR:Q08093; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q08093; protein.
DR Bgee; ENSMUSG00000004665; Expressed in external carotid artery and 247 other tissues.
DR ExpressionAtlas; Q08093; baseline and differential.
DR Genevisible; Q08093; MM.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; 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:0031032; P:actomyosin structure organization; IEA:InterPro.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:1905517; P:macrophage migration; IMP:MGI.
DR GO; GO:1905522; P:negative regulation of macrophage migration; IMP:MGI.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:MGI.
DR GO; GO:0006909; P:phagocytosis; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0032970; P:regulation of actin filament-based process; ISO:MGI.
DR GO; GO:0070663; P:regulation of leukocyte proliferation; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IMP: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; IPR029974; CNN2.
DR InterPro; IPR003096; SM22_calponin.
DR PANTHER; PTHR46756:SF2; PTHR46756:SF2; 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; 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; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..305
FT /note="Calponin-2"
FT /id="PRO_0000204774"
FT DOMAIN 28..132
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 166..191
FT /note="Calponin-like 1"
FT REPEAT 206..231
FT /note="Calponin-like 2"
FT REPEAT 245..269
FT /note="Calponin-like 3"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 25
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99439"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99439"
SQ SEQUENCE 305 AA; 33156 MW; 91DCDB47BEED53F8 CRC64;
MSSTQFNKGP SYGLSAEVKN RLLSKYDPQK EAELRSWIEG LTGLSIGPDF QKGLKDGVIL
CTLMNKLQPG SVPKINRSMQ NWHQLENLSN FIKAMVSYGM NPVDLFEAND LFESGNMTQV
QVSLLALAGK AKTKGLQSGV DIGVKYSEKQ ERNFDDATMK AGQCVIGLQM GTNKCASQSG
MTAYGTRRHL YDPKNHILPP MDHCTISLQM GTNKCASQVG MTAPGTRRHI YDTKLGTDKC
DNSSMSLQMG YTQGANQSGQ VFGLGRQIYD PKYCPQGSAA DGAPAGDGQG EAPEYLAYCQ
EEAGY
