ID   CNN1_MUSPF              Reviewed;         297 AA.
AC   Q9GK38;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Calponin-1;
DE   AltName: Full=Basic calponin;
DE   AltName: Full=Calponin H1, smooth muscle;
GN   Name=CNN1;
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC   Mustela.
OX   NCBI_TaxID=9669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Je H., Gangopadhyay S.S., Ashworth T.D., Morgan K.G.;
RT   "Downregulation of calponin inhibits contractility of differentiated smooth
RT   muscle.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
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   -!- 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   -!- INTERACTION:
CC       Q9GK38; Q6U1J6; NbExp=4; IntAct=EBI-7323120, EBI-7323108;
CC   -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
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DR   EMBL; AF323674; AAG40880.1; -; mRNA.
DR   RefSeq; NP_001297140.1; NM_001310211.1.
DR   RefSeq; XP_012909581.1; XM_013054127.1.
DR   AlphaFoldDB; Q9GK38; -.
DR   SMR; Q9GK38; -.
DR   IntAct; Q9GK38; 2.
DR   MINT; Q9GK38; -.
DR   STRING; 9668.ENSMPUP00000004882; -.
DR   GeneID; 101688825; -.
DR   KEGG; mpuf:101688825; -.
DR   CTD; 1264; -.
DR   eggNOG; KOG2046; Eukaryota.
DR   InParanoid; Q9GK38; -.
DR   Proteomes; UP000000715; Unassembled WGS sequence.
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; 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_0000232495"
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         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"
SQ   SEQUENCE   297 AA;  33231 MW;  D049B517E22C103C CRC64;
     MSSAHFNRGP AYGLSAEVKN KLAQKYDHQR EQELREWIEG VTGRRIGSNF MDGLKDGIIL
     CEFINKLQPG SVKKVNESTQ NWHQLENIGN FIKAITKYGV KPHDIFEAND LFENTNHTQV
     QSTLLALASM AKTKGNKVNV GVKYAEKQER KFEPEKLREG RNIIGLQMGT NKFASQQGMT
     AYGTRRHLYD PKLGTDQPLD QATISLQMGT NKGASQAGMT APGTKRQIFE PGLGMEHCDT
     LNVSLQMGSN KGASQRGMTV YGLPRQVYDP KYCLTPEYPE LGEPTHNHHA HNYYNSA