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Database: UniProt
Entry: A0A452FMK7_CAPHI
LinkDB: A0A452FMK7_CAPHI
Original site: A0A452FMK7_CAPHI 
ID   A0A452FMK7_CAPHI        Unreviewed;       329 AA.
AC   A0A452FMK7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Calponin {ECO:0000256|RuleBase:RU361224};
GN   Name=CNN3 {ECO:0000313|Ensembl:ENSCHIP00000025433.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000025433.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000025433.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000025433.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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       {ECO:0000256|ARBA:ARBA00025109, ECO:0000256|RuleBase:RU361224}.
CC   -!- SIMILARITY: Belongs to the calponin family.
CC       {ECO:0000256|ARBA:ARBA00009631, ECO:0000256|RuleBase:RU361224}.
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DR   EMBL; LWLT01000004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_017901282.1; XM_018045793.1.
DR   AlphaFoldDB; A0A452FMK7; -.
DR   SMR; A0A452FMK7; -.
DR   STRING; 9925.ENSCHIP00000025433; -.
DR   Ensembl; ENSCHIT00000033295.1; ENSCHIP00000025433.1; ENSCHIG00000022213.1.
DR   GeneID; 102184300; -.
DR   KEGG; chx:102184300; -.
DR   CTD; 1266; -.
DR   GeneTree; ENSGT00940000154539; -.
DR   OMA; EYQRDYH; -.
DR   OrthoDB; 11630at2759; -.
DR   Proteomes; UP000291000; Chromosome 3.
DR   Bgee; ENSCHIG00000022213; Expressed in metanephros cortex and 18 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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   GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR   CDD; cd21284; CH_CNN3; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   InterPro; IPR001997; Calponin/LIMCH1.
DR   InterPro; IPR000557; Calponin_repeat.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR003096; SM22_calponin.
DR   PANTHER; PTHR47385; CALPONIN; 1.
DR   PANTHER; PTHR47385:SF14; MUSCLE-SPECIFIC PROTEIN 20; 1.
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; Calponin-homology domain, CH-domain; 1.
DR   PROSITE; PS01052; CALPONIN_1; 2.
DR   PROSITE; PS51122; CALPONIN_2; 3.
DR   PROSITE; PS50021; CH; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW   ECO:0000256|RuleBase:RU361224};
KW   Calmodulin-binding {ECO:0000256|RuleBase:RU361224};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          26..130
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
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"
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
//
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