ID   CALD1_BOVIN             Reviewed;          83 AA.
AC   Q27976;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Non-muscle caldesmon;
DE            Short=CDM;
DE   AltName: Full=L-caldesmon;
DE   Flags: Fragment;
GN   Name=CALD1;
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 [MRNA].
RC   TISSUE=Retina;
RX   PubMed=8016144; DOI=10.1073/pnas.91.13.6231;
RA   Aiello L.P., Robinson G.S., Lin Y.-W., Nishio Y., King G.L.;
RT   "Identification of multiple genes in bovine retinal pericytes altered by
RT   exposure to elevated levels of glucose by using mRNA differential
RT   display.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:6231-6235(1994).
CC   -!- FUNCTION: Actin- and myosin-binding protein implicated in the
CC       regulation of actomyosin interactions in smooth muscle and nonmuscle
CC       cells (could act as a bridge between myosin and actin filaments).
CC       Stimulates actin binding of tropomyosin which increases the
CC       stabilization of actin filament structure. In muscle tissues, inhibits
CC       the actomyosin ATPase by binding to F-actin. This inhibition is
CC       attenuated by calcium-calmodulin and is potentiated by tropomyosin.
CC       Interacts with actin, myosin, two molecules of tropomyosin and with
CC       calmodulin. Also plays an essential role during cellular mitosis and
CC       receptor capping.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P13505}. Cytoplasm, myofibril
CC       {ECO:0000250|UniProtKB:P13505}. Cytoplasm, cytoskeleton, stress fiber
CC       {ECO:0000250|UniProtKB:P13505}. Note=On thin filaments in smooth muscle
CC       and on stress fibers in fibroblasts (nonmuscle).
CC       {ECO:0000250|UniProtKB:P13505}.
CC   -!- DOMAIN: The N-terminal part seems to be a myosin/calmodulin-binding
CC       domain, and the C-terminal a tropomyosin/actin/calmodulin-binding
CC       domain. These two domains are separated by a central helical region in
CC       the smooth-muscle form.
CC   -!- PTM: In non-muscle cells, phosphorylation by CDC2 during mitosis causes
CC       caldesmon to dissociate from microfilaments. Phosphorylation reduces
CC       caldesmon binding to actin, myosin, and calmodulin as well as its
CC       inhibition of actomyosin ATPase activity. Phosphorylation also occurs
CC       in both quiescent and dividing smooth muscle cells with similar effects
CC       on the interaction with actin and calmodulin and on microfilaments
CC       reorganization (By similarity). {ECO:0000250}.
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DR   EMBL; U09956; AAA21602.1; -; mRNA.
DR   PIR; I46058; I46058.
DR   AlphaFoldDB; Q27976; -.
DR   STRING; 9913.ENSBTAP00000018566; -.
DR   PaxDb; Q27976; -.
DR   PRIDE; Q27976; -.
DR   eggNOG; ENOG502QSYB; Eukaryota.
DR   OrthoDB; 1038798at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0017022; F:myosin binding; IBA:GO_Central.
DR   GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
PE   2: Evidence at transcript level;
KW   Actin-binding; Calmodulin-binding; Cytoplasm; Cytoskeleton; Muscle protein;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           <1..>83
FT                   /note="Non-muscle caldesmon"
FT                   /id="PRO_0000089286"
FT   REGION          <1..63
FT                   /note="Myosin and calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         83
SQ   SEQUENCE   83 AA;  9920 MW;  86D0AF7BAABC6A68 CRC64;
     QTSEKEGRSE SRQERQELEE TEIVTKSHQK NDWMEAEEKK KEEKEKEEEE EEKPKPGSIE
     ENQLKDEKTK KDKESKNILS LCL