CNN1_RAT
ID CNN1_RAT Reviewed; 297 AA.
AC Q08290;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Calponin-1;
DE AltName: Full=Basic calponin;
DE AltName: Full=Calponin H1, smooth muscle;
GN Name=Cnn1;
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=Wistar; TISSUE=Aortic smooth muscle;
RX PubMed=8508530; DOI=10.1161/01.res.73.1.193;
RA Shanahan C.M., Weissberg P.L., Metcalfe J.C.;
RT "Isolation of gene markers of differentiated and proliferating vascular
RT smooth muscle cells.";
RL Circ. Res. 73:193-204(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Aortic smooth muscle;
RX PubMed=8359698; DOI=10.1016/0378-1119(93)90435-6;
RA Nishida W., Kitami Y., Hiwada K.;
RT "cDNA cloning and mRNA expression of calponin and SM22 in rat aorta smooth
RT muscle cells.";
RL Gene 130:297-302(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pulmonary artery;
RA Takahashi K.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SUBUNIT: Part of cGMP kinase signaling complex at least composed of
CC ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and
CC ITPR1. {ECO:0000250}.
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; X71071; CAA50397.1; -; mRNA.
DR EMBL; D14437; BAA03320.1; -; mRNA.
DR EMBL; BC061809; AAH61809.1; -; mRNA.
DR PIR; S37640; JN0773.
DR RefSeq; NP_113935.1; NM_031747.1.
DR AlphaFoldDB; Q08290; -.
DR SMR; Q08290; -.
DR BioGRID; 249316; 3.
DR IntAct; Q08290; 1.
DR MINT; Q08290; -.
DR STRING; 10116.ENSRNOP00000029782; -.
DR iPTMnet; Q08290; -.
DR PhosphoSitePlus; Q08290; -.
DR PaxDb; Q08290; -.
DR PRIDE; Q08290; -.
DR Ensembl; ENSRNOT00000106276; ENSRNOP00000080119; ENSRNOG00000027736.
DR GeneID; 65204; -.
DR KEGG; rno:65204; -.
DR UCSC; RGD:621883; rat.
DR CTD; 1264; -.
DR RGD; 621883; Cnn1.
DR eggNOG; KOG2046; Eukaryota.
DR GeneTree; ENSGT00940000159680; -.
DR HOGENOM; CLU_055232_0_0_1; -.
DR InParanoid; Q08290; -.
DR OMA; GEPTHNH; -.
DR OrthoDB; 861989at2759; -.
DR PhylomeDB; Q08290; -.
DR PRO; PR:Q08290; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000027736; Expressed in colon and 19 other tissues.
DR Genevisible; Q08290; RN.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO: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 Actin-binding; Calmodulin-binding; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..297
FT /note="Calponin-1"
FT /id="PRO_0000204770"
FT DOMAIN 28..131
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 MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 170
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000250"
FT MOD_RES 175
FT /note="Phosphoserine; by ROCK2"
FT /evidence="ECO:0000250"
FT MOD_RES 180
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000250"
FT MOD_RES 184
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000250"
FT MOD_RES 259
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000250"
FT CONFLICT 97
FT /note="K -> E (in Ref. 2; BAA03320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 33344 MW; 80483631899BE025 CRC64;
MSSAHFNRGP AYGLSAEVKN KLAQKYDHQR EQELREWIEG VTGRRIGSNF MDGLKDGIIL
CEFINKLQPG SVKKVNESTQ NWHQLENIGN FIKAITKYGV KPHDIFEAND LFENTNHTQV
QSTLLALASM AKTKGNKVNV GVKYAEKQER RFEPEKLREG RNIIGLQMGT NKFASQQGMT
AYGTRRHLYD PKLGTDQPLD QATISLQMGT NKGASQAGMT APGTKRQIFE PGLGMEHCDT
LNVSLQMGSN KGASQRGMTV YGLPRQVYDP KYCLTPEYPE LDEPTHNHHP HNYYNSA
