ID A0A3Q0RWT0_AMPCI Unreviewed; 297 AA.
AC A0A3Q0RWT0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Calponin {ECO:0000256|RuleBase:RU361224};
GN Name=CNN1 {ECO:0000313|Ensembl:ENSACIP00000014168.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000014168.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000014168.1}
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 AlphaFoldDB; A0A3Q0RWT0; -.
DR Ensembl; ENSACIT00000014549.1; ENSACIP00000014168.1; ENSACIG00000010970.1.
DR GeneTree; ENSGT00940000159680; -.
DR OMA; GEPTHNH; -.
DR Proteomes; UP000261340; Unplaced.
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 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:SF18; TRANSGELIN; 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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 27..130
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
SQ SEQUENCE 297 AA; 33348 MW; EC3D0F77EEBFDBF5 CRC64;
MTTHFRSGPA FGLSAEVKSK LAGKYDPQKE EELRLWIEDV IGKRIGDNFM ESLKDGVMLC
ELINVLQPGS VKKINHSSQN WHQLENIGNF VRAITEYGLK PHDIFEANDL FENVNHTQVQ
CTLIALAGMA KSKGFHSKYD IGVKYAEKQQ RRFAPEKLRE GRNVIGLQMG TNQFASQKGM
TSYGTRRHLY DAKIAMDNPD QSTISLQMGT NKGASQSGMT APGTRRHIFD KNLKLEDCDT
TTISLQMGTN KGASQQGMTT YGLPRQVYDN KYCANPTEAY YNNGSEVEFD GYNQYSD
//
