ID   CALD1_MELGA             Reviewed;         274 AA.
AC   P13505;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Caldesmon, smooth muscle;
DE            Short=CDM;
DE   Flags: Fragment;
GN   Name=CALD1; Synonyms=CAD;
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.
RX   PubMed=1924267;
RA   Collins J.H., Leszyk J., Mornet D., Audemard E.;
RT   "Turkey gizzard caldesmon: complete sequence of a C-terminal thrombic
RT   fragment that binds actin, tropomyosin and calmodulin.";
RL   Protein Seq. Data Anal. 4:29-32(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-239.
RC   TISSUE=Gizzard;
RX   PubMed=2730648; DOI=10.1016/s0006-291x(89)80155-x;
RA   Leszyk J., Mornet D., Audemard E., Collins J.H.;
RT   "Caldesmon structure and function: sequence analysis of a 35 kilodalton
RT   actin- and calmodulin-binding fragment from the C-terminus of the turkey
RT   gizzard protein.";
RL   Biochem. Biophys. Res. Commun. 160:1371-1378(1989).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-96.
RC   TISSUE=Gizzard;
RX   PubMed=2653315; DOI=10.1016/0006-291x(89)91642-2;
RA   Leszyk J., Mornet D., Audemard E., Collins J.H.;
RT   "Amino acid sequence of a 15 kilodalton actin-binding fragment of turkey
RT   gizzard caldesmon: similarity with dystrophin, tropomyosin and the
RT   tropomyosin-binding region of troponin T.";
RL   Biochem. Biophys. Res. Commun. 160:210-216(1989).
CC   -!- FUNCTION: Control of actomyosin interactions in smooth muscle and
CC       nonmuscle cells (could act as a bridge between myosin and actin
CC       filaments). Inhibits the actin-activated ATPase of myosin this
CC       inhibition is attenuated by calcium-calmodulin and is potentiated by
CC       tropomyosin. Interacts with actin, myosin, 2 molecules of tropomyosin
CC       and with calmodulin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, myofibril.
CC       Cytoplasm, cytoskeleton, stress fiber. Note=On thin filaments in smooth
CC       muscle and on stress fibers in fibroblasts (nonmuscle).
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DR   PIR; S16925; S16925.
DR   AlphaFoldDB; P13505; -.
DR   BMRB; P13505; -.
DR   SMR; P13505; -.
DR   InParanoid; P13505; -.
DR   Proteomes; UP000001645; Unplaced.
DR   GO; GO:0005884; C:actin filament; IDA:CAFA.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IPI:CAFA.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0017022; F:myosin binding; IPI:CAFA.
DR   GO; GO:0006936; P:muscle contraction; IEA:InterPro.
DR   GO; GO:1904530; P:negative regulation of actin filament binding; IDA:CAFA.
DR   InterPro; IPR006017; Caldesmon.
DR   InterPro; IPR006018; Caldesmon_LSP.
DR   PANTHER; PTHR18949; PTHR18949; 1.
DR   PANTHER; PTHR18949:SF0; PTHR18949:SF0; 1.
DR   Pfam; PF02029; Caldesmon; 1.
DR   PRINTS; PR01076; CALDESMON.
PE   1: Evidence at protein level;
KW   Actin-binding; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Muscle protein; Reference proteome.
FT   CHAIN           <1..>274
FT                   /note="Caldesmon, smooth muscle"
FT                   /id="PRO_0000089289"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         274
SQ   SEQUENCE   274 AA;  30408 MW;  62DDAFFA71E79C9E CRC64;
     SNLKGAANAE AGSEKLKEKQ QEAAVELDEL KKRREERRKI LEEEEQKKKQ EEAERKIREE
     EEKKRMKEEI ERRRAEAAEK RQKMPEDGVS EEKKPFKCFS PKGSSLKIEE RAEFLNKSAQ
     KSGMKPAHTT AVVSKIDSRL EQYTSAVVGN KAAKPAKPAA SDLPVPAEGV RNIKSMWEKG
     NVFSSPGGTG TPNKETAGLK VGVSSRINEW LTKTPEGNKS PAPKPSDLRP GDVSGKRNLW
     EKQSVEKPAA SSSKVTATGK KSETDGLRQF EKEP