CNN1_CHICK
ID CNN1_CHICK Reviewed; 292 AA.
AC P26932; P26933; Q9PSG0;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Calponin-1;
DE AltName: Full=Calponin, smooth muscle;
GN Name=CNN1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gizzard smooth muscle;
RX PubMed=2071603; DOI=10.1016/s0021-9258(18)98836-8;
RA Takahashi K., Nadal-Ginard B.;
RT "Molecular cloning and sequence analysis of smooth muscle calponin.";
RL J. Biol. Chem. 266:13284-13288(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gizzard smooth muscle;
RX PubMed=8130072; DOI=10.1016/0898-6568(93)90029-l;
RA Winder S.J., Walsh M.P.;
RT "Calponin: thin filament-linked regulation of smooth muscle contraction.";
RL Cell. Signal. 5:677-686(1993).
RN [3]
RP PROTEIN SEQUENCE OF 7-21; 52-66 AND 183-194.
RX PubMed=1639822; DOI=10.1016/s0021-9258(19)49625-7;
RA Mezgueldi M., Fattoum A., Derancourt J., Kassab R.;
RT "Mapping of the functional domains in the amino-terminal region of
RT calponin.";
RL J. Biol. Chem. 267:15943-15951(1992).
RN [4]
RP PROTEIN SEQUENCE OF 157-192 AND 252-271, AND PHOSPHORYLATION AT THR-170;
RP SER-175; THR-180; THR-184 AND THR-259.
RX PubMed=10873572; DOI=10.1006/bbrc.2000.2901;
RA Kaneko T., Amano M., Maeda A., Goto H., Takahashi K., Ito M., Kaibuchi K.;
RT "Identification of calponin as a novel substrate of Rho-kinase.";
RL Biochem. Biophys. Res. Commun. 273:110-116(2000).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS.
RX PubMed=8276752; DOI=10.1093/oxfordjournals.jbchem.a124197;
RA Gong B.J., Mabuchi K., Takahashi K., Nadal-Ginard B., Tao T.;
RT "Characterization of wild type and mutant chicken gizzard alpha calponin
RT expressed in E. coli.";
RL J. Biochem. 114:453-456(1993).
RN [6]
RP PHOSPHORYLATION AT SER-175.
RX PubMed=8280082; DOI=10.1042/bj2960827;
RA Winder S.J., Allen B.G., Fraser E.D., Kang H.M., Kargacin G.J., Walsh M.P.;
RT "Calponin phosphorylation in vitro and in intact muscle.";
RL Biochem. J. 296:827-836(1993).
RN [7]
RP PHOSPHORYLATION AT THR-184.
RX PubMed=8454594; DOI=10.1016/s0021-9258(18)53238-5;
RA Nakamura F., Mino T., Yamamoto J., Naka M., Tanaka T.;
RT "Identification of the regulatory site in smooth muscle calponin that is
RT phosphorylated by protein kinase C.";
RL J. Biol. Chem. 268:6194-6201(1993).
RN [8]
RP STRUCTURE BY NMR OF 27-134.
RX PubMed=11839310; DOI=10.1016/s0969-2126(02)00703-7;
RA Bramham J., Hodgkinson J.L., Smith B.O., Uhrin D., Barlow P.N.,
RA Winder S.J.;
RT "Solution structure of the calponin CH domain and fitting to the 3D-helical
RT reconstruction of F-actin:calponin.";
RL Structure 10:249-258(2002).
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 -!- INTERACTION:
CC P26932; P68135: ACTA1; Xeno; NbExp=5; IntAct=EBI-8602797, EBI-367540;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=P26932-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P26932-2; Sequence=VSP_000756;
CC -!- TISSUE SPECIFICITY: Smooth muscle, and tissues containing significant
CC amounts of smooth muscle.
CC -!- PTM: Phosphorylation by PKC or CaM kinase II reduces the binding of
CC calponin to F-actin and tropomyosin. {ECO:0000269|PubMed:10873572,
CC ECO:0000269|PubMed:8280082, ECO:0000269|PubMed:8454594}.
CC -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
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DR EMBL; M63559; AAA48651.1; -; mRNA.
DR EMBL; M63560; AAA48652.1; -; mRNA.
DR PIR; A39871; A39871.
DR RefSeq; NP_990847.1; NM_205516.1.
DR PDB; 1H67; NMR; -; A=28-134.
DR PDBsum; 1H67; -.
DR AlphaFoldDB; P26932; -.
DR BMRB; P26932; -.
DR SMR; P26932; -.
DR IntAct; P26932; 1.
DR MINT; P26932; -.
DR iPTMnet; P26932; -.
DR Ensembl; ENSGALT00000100379; ENSGALP00000068053; ENSGALG00000041266. [P26932-1]
DR GeneID; 396522; -.
DR KEGG; gga:396522; -.
DR CTD; 1264; -.
DR VEuPathDB; HostDB:geneid_424485; -.
DR GeneTree; ENSGT00940000159680; -.
DR InParanoid; P26932; -.
DR OrthoDB; 861989at2759; -.
DR PhylomeDB; P26932; -.
DR EvolutionaryTrace; P26932; -.
DR PRO; PR:P26932; -.
DR Proteomes; UP000000539; Chromosome 30.
DR Bgee; ENSGALG00000041266; Expressed in colon and 11 other tissues.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IBA:GO_Central.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
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 3D-structure; Actin-binding; Alternative splicing; Calmodulin-binding;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..292
FT /note="Calponin-1"
FT /id="PRO_0000204771"
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 REGION 185..193
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000305"
FT MOD_RES 170
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000269|PubMed:10873572"
FT MOD_RES 175
FT /note="Phosphoserine; by PKC, CaMK2 and ROCK2"
FT /evidence="ECO:0000269|PubMed:10873572,
FT ECO:0000269|PubMed:8280082"
FT MOD_RES 180
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000269|PubMed:10873572"
FT MOD_RES 184
FT /note="Phosphothreonine; by PKC and CaMK2"
FT /evidence="ECO:0000269|PubMed:10873572,
FT ECO:0000269|PubMed:8454594"
FT MOD_RES 184
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000269|PubMed:10873572,
FT ECO:0000269|PubMed:8454594"
FT MOD_RES 259
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000269|PubMed:10873572"
FT VAR_SEQ 217..256
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_000756"
FT CONFLICT 66
FT /note="K -> T (in Ref. 1; AAA48651/AAA48652)"
FT /evidence="ECO:0000305"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:1H67"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:1H67"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:1H67"
FT HELIX 82..98
FT /evidence="ECO:0007829|PDB:1H67"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1H67"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:1H67"
FT HELIX 118..133
FT /evidence="ECO:0007829|PDB:1H67"
SQ SEQUENCE 292 AA; 32361 MW; A80E55FE5966DAC6 CRC64;
MSNANFNRGP AYGLSAEVKN KLAQKYDPQT ERQLRVWIEG ATGRRIGDNF MDGLKDGVIL
CELINKLQPG SVQKVNDPVQ NWHKLENIGN FLRAIKHYGV KPHDIFEAND LFENTNHTQV
QSTLIALASQ AKTKGNNVGL GVKYAEKQQR RFQPEKLREG RNIIGLQMGT NKFASQQGMT
AYGTRRHLYD PKLGTDQPLD QATISLQMGT NKGASQAGMT APGTKRQIFE PSLGMERCDT
NIIGLQMGSN KGASQQGMTV YGLPRQVYDP KYCDAPGLLG EDGLNHSFYN SQ
