ID   CNN1_BOVIN              Reviewed;         297 AA.
AC   Q2HJ38; A7E3U3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Calponin-1;
DE   AltName: Full=Basic calponin;
DE   AltName: Full=Calponin H1, smooth muscle;
GN   Name=CNN1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) 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   -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
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DR   EMBL; BT030714; ABS45030.1; -; mRNA.
DR   EMBL; BC113327; AAI13328.1; -; mRNA.
DR   RefSeq; NP_001039844.1; NM_001046379.1.
DR   AlphaFoldDB; Q2HJ38; -.
DR   SMR; Q2HJ38; -.
DR   CORUM; Q2HJ38; -.
DR   STRING; 9913.ENSBTAP00000014883; -.
DR   PaxDb; Q2HJ38; -.
DR   PeptideAtlas; Q2HJ38; -.
DR   PRIDE; Q2HJ38; -.
DR   Ensembl; ENSBTAT00000014883; ENSBTAP00000014883; ENSBTAG00000011207.
DR   GeneID; 534583; -.
DR   KEGG; bta:534583; -.
DR   CTD; 1264; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011207; -.
DR   VGNC; VGNC:27508; CNN1.
DR   eggNOG; KOG2046; Eukaryota.
DR   GeneTree; ENSGT00940000159680; -.
DR   HOGENOM; CLU_055232_0_0_1; -.
DR   InParanoid; Q2HJ38; -.
DR   OMA; GEPTHNH; -.
DR   OrthoDB; 861989at2759; -.
DR   TreeFam; TF313921; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000011207; Expressed in vas deferens and 105 other tissues.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
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; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Actin-binding; Calmodulin-binding; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..297
FT                   /note="Calponin-1"
FT                   /id="PRO_0000244391"
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;  33283 MW;  3DDF1F3199961026 CRC64;
     MSSAHFNRGP AYGLSAEVKN KLAQKYDHQR EQELREWIEG VTGRRIGNNF MDGLKDGIIL
     CEFINKLQPG SVKKVNESTQ NWHQLENIGN FIKAITKYGV KPHDIFEAND LFENTNHTQV
     QSTLLALASM AKTKGNKVNV GVKYAEKQER RFEPEKLREG RNIIGLQMGT NKFASQQGMT
     AYGTRRHLYD PKLGTDQPLD QATISLQMGT NKGASQAGMT APGTKRQIFE PGLGMEHCDT
     LNVSLQMGSN KGASQRGMTV YGLPRQVYDP KYCLTPEYPE LGEPAHNHHP HNYYNSA