(data stored in ACNUC6444 zone)

HOGENOM: RAT4_PE477

ID   RAT4_PE477                           STANDARD;      PRT;   531 AA.
AC   RAT4_PE477; Q62736;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Non-muscle caldesmon; Short=CDM;AltName: Full=L-caldesmon;
DE   (RAT4.PE477).
GN   Name=Cald1;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT4.PE477.
CC       Rattus norvegicus chromosome 4 RGSC3.4  sequence 1..187126005
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:CALD1_RAT
CC   -!- FUNCTION: Actin- and myosin-binding protein implicated in the
CC       regulation of actomyosin interactions in smooth muscle and
CC       nonmuscle cells (could act as a bridge between myosin and actin
CC       filaments). Stimulates actin binding of tropomyosin which
CC       increases the stabilization of actin filament structure. In muscle
CC       tissues, inhibits the actomyosin ATPase by binding to F-actin.
CC       This inhibition is attenuated by calcium-calmodulin and is
CC       potentiated by tropomyosin. Interacts with actin, myosin, two
CC       molecules of tropomyosin and with calmodulin. Also play an
CC       essential role during cellular mitosis and receptor capping.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cytoplasm, myofibril (By similarity). Note=On thin filaments in
CC       smooth muscle and on stress fibers in fibroblasts (nonmuscle) (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: High-molecular-weight caldesmon (h-caldesmon)
CC       is predominantly expressed in smooth muscles, whereas low-
CC       molecular-weight caldesmon (l-caldesmon) is widely distributed in
CC       non-muscle tissues and cells. Not expressed in skeletal muscle or
CC       heart (By similarity).
CC   -!- DOMAIN: The N-terminal part seems to be a myosin/calmodulin-
CC       binding domain, and the C-terminal a tropomyosin/actin/calmodulin-
CC       binding domain. These two domains are separated by a central
CC       helical region in the smooth-muscle form.
CC   -!- PTM: In non-muscle cells, phosphorylation by CDK1 during mitosis
CC       causes caldesmon to dissociate from microfilaments.
CC       Phosphorylation reduces caldesmon binding to actin, myosin, and
CC       calmodulin as well as its inhibition of actomyosin ATPase
CC       activity. Phosphorylation also occurs in both quiescent and
CC       dividing smooth muscle cells with similar effects on the
CC       interaction with actin and calmodulin and on microfilaments
CC       reorganization.
CC   -!- SIMILARITY: Belongs to the caldesmon family.
CC   -!- GENE_FAMILY: HOG000013012 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000010233;ENSRNOT00000041264;ENSRNOP00000043767.
DR   EMBL; U18419; - ;
DR   UniProtKB/Swiss-Prot; Q62736; -.
DR   EMBL; U18419; AAA68521.1; -; mRNA.
DR   IPI; IPI00208118; -.
DR   PIR; A55887; A55887.
DR   RefSeq; NP_037278.1; NM_013146.2.
DR   UniGene; Rn.204926; -.
DR   ProteinModelPortal; Q62736; -.
DR   STRING; Q62736; -.
DR   PhosphoSite; Q62736; -.
DR   PRIDE; Q62736; -.
DR   GeneID; 25687; -.
DR   KEGG; rno:25687; -.
DR   UCSC; NM_013146; rat.
DR   CTD; 800; -.
DR   RGD; 2256; Cald1.
DR   eggNOG; maNOG06563; -.
DR   GeneTree; ENSGT00600000084370; -.
DR   InParanoid; Q62736; -.
DR   OrthoDB; EOG4GQQ67; -.
DR   NextBio; 607677; -.
DR   ArrayExpress; Q62736; -.
DR   Genevestigator; Q62736; -.
DR   GermOnline; ENSRNOG00000010233; Rattus norvegicus.
DR   GO; GO:0005884; C:actin filament; IDA:RGD.
DR   GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR   GO; GO:0003779; F:actin binding; IDA:RGD.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0017022; F:myosin binding; IEA:InterPro.
DR   GO; GO:0051017; P:actin filament bundle assembly; IDA:RGD.
DR   GO; GO:0007565; P:female pregnancy; TAS:RGD.
DR   GO; GO:0006936; P:muscle contraction; IEA:InterPro.
DR   GO; GO:0032092; P:positive regulation of protein binding; IDA:RGD.
DR   InterPro; IPR006017; Caldesmon.
DR   InterPro; IPR006018; Caldesmon_LSP.
DR   Pfam; PF02029; Caldesmon; 2.
DR   PRINTS; PR01076; CALDESMON.
DR   HOGENOMDNA; RAT4.PE477; -.
KW   ENSRNOG00000010233820036002503210000011;
KW   Cald1; CALD1_RAT; U18419;
KW   Actin-binding; Calmodulin-binding; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Muscle protein; Phosphoprotein; Reference proteome.
SQ   SEQUENCE   531 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLSRSGSQGR RCLATLSQIA YQRNDDDEEE AARERRRRAR QERLRQKQEE ESLGQVTDQV
     EAHVQNSVPD EESKPATANA QVEGDEEAAL LERLARREER RQKRLQEALE RQKEFDPTIT
     DGSLSVPSRR MQNNSAENET AEGEEKGESR SGRYEMEETE VVITSYQKNS YQDAEDKKKE
     EKEEEEEEEK LKGGNLGENQ IKDEKIKKDK EPKEEVKNFL DRKKGFTEVK AQNGEFMTHK
     LKQTENAFSP SRSGGRASGD KEAEGAPQVE AGKRLEELRR RRGETESEEF EKLKQKQQEA
     ALELEELKKK REERRKVLEE EEQRRKQEEA DRKAREEEEK RRLKEEIERR RAEAAEKRQK
     MPEDGLSEDK KPFKCFTPKG SSLKIEERAE FLNKSVQKSG VKSTHQAAVV SKIDSRLEQY
     TNAIEGTKAS KPMKPAASDL PVPAEGVRNI KSMWEKGSVF SSPSASGTPN KETAGLKVGV
     SSRINEWLTK SPDGNKSPAP KPSDLRPGDV SGKRNLWEKQ SVDKVTSPTK V
//

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