CNN1_PIG
ID CNN1_PIG Reviewed; 297 AA.
AC Q08092;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Calponin-1;
DE AltName: Full=Basic calponin;
DE AltName: Full=Calponin H1, smooth muscle;
GN Name=CNN1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Smooth muscle;
RX PubMed=8370452; DOI=10.1016/0014-5793(93)80909-e;
RA Strasser P., Gimona M., Moessler H., Herzog M., Small J.V.;
RT "Mammalian calponin. Identification and expression of genetic variants.";
RL FEBS Lett. 330:13-18(1993).
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; Z19538; CAA79598.1; -; mRNA.
DR PIR; S36146; S31484.
DR RefSeq; NP_999043.1; NM_213878.1.
DR AlphaFoldDB; Q08092; -.
DR SMR; Q08092; -.
DR STRING; 9823.ENSSSCP00000014468; -.
DR iPTMnet; Q08092; -.
DR PaxDb; Q08092; -.
DR PeptideAtlas; Q08092; -.
DR PRIDE; Q08092; -.
DR Ensembl; ENSSSCT00005072861; ENSSSCP00005045603; ENSSSCG00005045130.
DR GeneID; 396911; -.
DR KEGG; ssc:396911; -.
DR CTD; 1264; -.
DR eggNOG; KOG2046; Eukaryota.
DR HOGENOM; CLU_055232_0_0_1; -.
DR InParanoid; Q08092; -.
DR OrthoDB; 861989at2759; -.
DR TreeFam; TF313921; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q08092; SS.
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 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_0000204769"
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; 33226 MW; C8ED9C170D12E027 CRC64;
MSSAHFNRGP AYGLSAEVKN KLAQKYDHQQ EQELREWIEG VTGRRIGNNF MDGLKDGIIL
CEFINKLQPG SVKKVNESTQ NWHQLENIGN FIKAITKYGV KPHDIFEAND LFENTNHTQV
QSTLLALASM AKTKGNKVNV GVKYAEKQER KFEPEKLREG RNIIGLQMGT NKFASQQGMT
AYGTRRHLYD PKLGTDQPLD QATISLQMGT NKGASQAGMT APGTKRQIFE PGLGMEHCDT
LNVSLQMGSN KGASQRGMTV YGLPRQVYDP KYCLTPEYPE LGEPAHNHHP HNYYNSA