ID   CNN1_MELGA              Reviewed;         176 AA.
AC   P37803;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   07-OCT-2020, entry version 85.
DE   RecName: Full=Calponin-1;
DE   AltName: Full=Calponin, smooth muscle;
DE   Flags: Fragment;
GN   Name=CNN1;
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Gizzard;
RX   PubMed=2253766; DOI=10.1016/0014-5793(90)81350-w;
RA   Vancompernolle K., Gimona M., Herzog M., van Damme J., Vandekerckhove J.,
RA   Small V.;
RT   "Isolation and sequence of a tropomyosin-binding fragment of turkey gizzard
RT   calponin.";
RL   FEBS Lett. 274:146-150(1990).
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   -!- 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   PIR; S12914; S12914.
DR   BMRB; P37803; -.
DR   InParanoid; P37803; -.
DR   Proteomes; UP000001645; 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   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; 1.
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; PS51122; CALPONIN_2; 1.
DR   PROSITE; PS50021; CH; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Calmodulin-binding; Direct protein sequencing;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           <1..>176
FT                   /note="Calponin-1"
FT                   /id="PRO_0000204772"
FT   DOMAIN          22..125
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REPEAT          158..>176
FT                   /note="Calponin-like"
FT   MOD_RES         164
FT                   /note="Phosphothreonine; by ROCK2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         169
FT                   /note="Phosphoserine; by ROCK2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         174
FT                   /note="Phosphothreonine; by ROCK2"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         176
SQ   SEQUENCE   176 AA;  19828 MW;  A9166FF481C1E2D3 CRC64;
     NRGPAYGLSA EVKNKLAQKY DPQTERQLRV WIEGATGRRI GDNFXDGLKD GVILMELINK
     LQPGSVQKVN DPVQNWHKLE NIGNFLRAIK HYGVKPHDIF EANDLFENTN HTQVQSTLIA
     LASQAKTKGN NVGLGVKYAE KQQRRFQPEK LREGRNIIGL QMGTNKFASQ QGMTAY