CNN3_RAT
ID CNN3_RAT Reviewed; 330 AA.
AC P37397;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Calponin-3;
DE AltName: Full=Calponin, acidic isoform;
DE AltName: Full=Calponin, non-muscle isoform;
GN Name=Cnn3;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Vascular smooth muscle;
RX PubMed=8144658; DOI=10.1016/s0021-9258(17)34113-3;
RA Applegate D.E., Feng W., Green R.S., Taubman M.B.;
RT "Cloning and expression of a novel acidic calponin isoform from rat aortic
RT vascular smooth muscle.";
RL J. Biol. Chem. 269:10683-10690(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 54-64, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) 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 -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
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DR EMBL; U06755; AAA18590.1; -; mRNA.
DR EMBL; BC062020; AAH62020.1; -; mRNA.
DR PIR; A53742; A53742.
DR RefSeq; NP_062232.1; NM_019359.1.
DR AlphaFoldDB; P37397; -.
DR SMR; P37397; -.
DR BioGRID; 248537; 3.
DR IntAct; P37397; 1.
DR STRING; 10116.ENSRNOP00000015579; -.
DR iPTMnet; P37397; -.
DR PhosphoSitePlus; P37397; -.
DR jPOST; P37397; -.
DR PaxDb; P37397; -.
DR PRIDE; P37397; -.
DR Ensembl; ENSRNOT00000119824; ENSRNOP00000092181; ENSRNOG00000011559.
DR GeneID; 54321; -.
DR KEGG; rno:54321; -.
DR UCSC; RGD:71044; rat.
DR CTD; 1266; -.
DR RGD; 71044; Cnn3.
DR eggNOG; KOG2046; Eukaryota.
DR GeneTree; ENSGT00940000154539; -.
DR HOGENOM; CLU_055232_0_1_1; -.
DR InParanoid; P37397; -.
DR OMA; TMTHFNK; -.
DR OrthoDB; 861989at2759; -.
DR PhylomeDB; P37397; -.
DR TreeFam; TF313921; -.
DR PRO; PR:P37397; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011559; Expressed in stomach and 20 other tissues.
DR Genevisible; P37397; RN.
DR GO; GO:0005884; C:actin filament; TAS:RGD.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0005874; C:microtubule; TAS:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:RGD.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IDA:RGD.
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; Direct protein sequencing;
KW Methylation; Reference proteome; Repeat.
FT CHAIN 1..330
FT /note="Calponin-3"
FT /id="PRO_0000204778"
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:0000250|UniProtKB:Q9DAW9"
FT MOD_RES 158
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15417"
SQ SEQUENCE 330 AA; 36435 MW; 428226594E10BA05 CRC64;
MTHFNKGPSY GLSAEVKNKI ASKYDQQAEE DLRNWIEEVT GMGIGTNFQL GLKDGIILCE
LINKLQPGSV KKVNESSLNW PQLENIGNFI KAIQAYGMKP HDIFEANDLF ENGNMTQVQT
TLVALAGLAK TKGFHTTIDI GVKYAEKQTR RFDEGKLKAG QSVIGLQMGT NKCASQAGMT
AYGTRRHLYD PKMQTDKPFD QTTISLQMGT NKGASQAGMS APGTRRDIYD QKLTLQPVDN
STISLQMGTN KVASQKGMSV YGLGRQVYDP KYCAAPTEPV IHNGSQGTGT NGSEISDSDY
QAEYPDEYHG EYPDEYPREY QYGDDQGIDY
