CNN3_BOVIN
ID CNN3_BOVIN Reviewed; 329 AA.
AC Q32L92;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Calponin-3;
DE AltName: Full=Calponin, acidic isoform;
GN Name=CNN3;
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].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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; BC109697; AAI09698.1; -; mRNA.
DR RefSeq; NP_001033268.1; NM_001038179.1.
DR AlphaFoldDB; Q32L92; -.
DR SMR; Q32L92; -.
DR STRING; 9913.ENSBTAP00000027115; -.
DR PaxDb; Q32L92; -.
DR PeptideAtlas; Q32L92; -.
DR PRIDE; Q32L92; -.
DR Ensembl; ENSBTAT00000027115; ENSBTAP00000027115; ENSBTAG00000020345.
DR GeneID; 538975; -.
DR KEGG; bta:538975; -.
DR CTD; 1266; -.
DR VEuPathDB; HostDB:ENSBTAG00000020345; -.
DR eggNOG; KOG2046; Eukaryota.
DR GeneTree; ENSGT00940000154539; -.
DR HOGENOM; CLU_055232_0_1_1; -.
DR InParanoid; Q32L92; -.
DR OMA; TMTHFNK; -.
DR OrthoDB; 861989at2759; -.
DR TreeFam; TF313921; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000020345; Expressed in neurohypophysis and 104 other tissues.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISS:AgBase.
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 Acetylation; Actin-binding; Calmodulin-binding; Methylation;
KW Reference proteome; Repeat.
FT CHAIN 1..329
FT /note="Calponin-3"
FT /id="PRO_0000244392"
FT DOMAIN 26..130
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 280..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DAW9"
FT MOD_RES 158
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15417"
SQ SEQUENCE 329 AA; 36358 MW; FF81146DBC34F013 CRC64;
MTHFNKGPSY GLSAEVKNKI ASKYDHQAEE DLRNWIEEVT GMSIGANFQL GLKDGIILCE
LINKLQPGSV KKVNESSLNW PQLENIGNFI KAIQAYGMKP HDIFEANDLF ENGNMTQVQT
TLVALAGLAK TKGFHTTIDI GVKYAEKQTR RFDEGKLKAG QSVIGLQMGT NKCASQAGMT
AYGTRRHLYD PKMQTDKPFD QTTISLQMGT NKGASQAGML APGTRRDIYD QKLTLQPVDN
STISLQMGTN KVASQKGMSV YGLGRQVYDP KYCAAPTEPV IHNGSQGTGT NGSEISDSDY
QAEYPDEYHG EYQDDYPRDY QYGDQGIDY