(data stored in ACNUC6444 zone)

HOGENOM: CHICK1_PE1108

ID   CHICK1_PE1108                        STANDARD;      PRT;   771 AA.
AC   CHICK1_PE1108; P12957; Q03698; Q90756; Q90761; Q92018; Q99230;
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=Caldesmon; Short=CDM; (CHICK1.PE1108).
GN   Name=CALD1; Synonyms=CAD;
OS   GALLUS GALLUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Sauropsida; Sauria; Archosauria;
OC   Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae;
OC   Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHICK1.PE1108.
CC       Gallus gallus chromosome 1 WASHUC2  sequence 1..200994015 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:CALD1_CHICK
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Gizzard h-cad;
CC         IsoId=P12957-1; Sequence=Displayed;
CC       Name=Brain l-cad;
CC         IsoId=P12957-2; Sequence=VSP_004152, VSP_004153;
CC       Name=Gizzard l-cad;
CC         IsoId=P12957-3; Sequence=VSP_004153;
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.
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 muscle forms.
CC   -!- PTM: Phosphorylated in non-muscle cells. Phosphorylation by CDK1
CC       during mitosis 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 (By similarity).
CC   -!- SIMILARITY: Belongs to the caldesmon family.
CC   -!- GENE_FAMILY: HOG000013012 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Gallus_gallus;ENSGALG00000013071;ENSGALT00000021345;ENSGALP00000021314.
DR   EMBL; D17552; - ;
DR   EMBL; D17648; - ;
DR   EMBL; J04968; - ;
DR   EMBL; M26684; - ;
DR   EMBL; M28417; - ;
DR   EMBL; M59762; - ;
DR   EMBL; M60620; - ;
DR   UniProtKB/Swiss-Prot; P12957; Q03698; Q90756; Q90761; Q92018; Q99230; -.
DR   EMBL; J04968; AAA49067.1; -; mRNA.
DR   EMBL; D17648; BAA04539.1; -; Genomic_DNA.
DR   EMBL; M28417; AAA48810.1; -; mRNA.
DR   EMBL; M60620; AAA48936.1; -; mRNA.
DR   EMBL; D17648; BAA04538.1; -; Genomic_DNA.
DR   EMBL; D17648; BAA04540.1; -; Genomic_DNA.
DR   EMBL; M59762; AAA48649.1; -; mRNA.
DR   EMBL; D17552; BAA04490.1; -; Genomic_DNA.
DR   EMBL; M26684; AAA48811.1; -; mRNA.
DR   IPI; IPI00572834; -.
DR   IPI; IPI00577689; -.
DR   IPI; IPI00583069; -.
DR   PIR; A33430; A33430.
DR   PIR; A39038; A39038.
DR   RefSeq; NP_989489.1; NM_204158.1.
DR   UniGene; Gga.4988; -.
DR   ProteinModelPortal; P12957; -.
DR   DisProt; DP00120; -.
DR   STRING; P12957; -.
DR   GeneID; 373965; -.
DR   KEGG; gga:373965; -.
DR   CTD; 800; -.
DR   eggNOG; veNOG15435; -.
DR   GeneTree; ENSGT00600000084370; -.
DR   InParanoid; P12957; -.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0017022; F:myosin binding; IEA:InterPro.
DR   GO; GO:0006936; P:muscle contraction; IEA:InterPro.
DR   InterPro; IPR006017; Caldesmon.
DR   InterPro; IPR006018; Caldesmon_LSP.
DR   Pfam; PF02029; Caldesmon; 1.
DR   PRINTS; PR01076; CALDESMON.
DR   HOGENOMDNA; CHICK1.PE1108; -.
KW   ENSGALG00000013071fold_1320000031; ENSGALP00000021314fold_1320000031;
KW   D17552; D17648; J04968; M26684; M28417; M59762; M60620;
KW   Actin-binding; Alternative splicing; Calmodulin-binding;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Muscle protein; Phosphoprotein; Reference proteome; Repeat.
SQ   SEQUENCE   771 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDDFERRREL RRQKREEMRL EAERLSYQRN DDDEEEAARE RRRRARQERL RQKEEGDVSG
     EVTEKSEVNA QNSVAEEETK RSTDDEAALL ERLARREERR QKRLQEALER QKEFDPTITD
     GSLSVPSRRE VNNVEENETT GKEEKVETRQ GRCEIEETET VTKSYQRNNW RQDGEEEGKK
     EEKDSEEEKP KEVPTEENQV DVAVEKSTDK EEVVETKTLA VNAENDTNAM LEGEQSITDA
     ADKEKEEAEK EREKLEAEEK ERLKAEEEKK AAEEKQKAEE EKKAAEERER AKAEEEKRAA
     EERERAKAEE ERKAAEERER AKAEEERKAA EERAKAEEER KAAEERAKAE EERKAAEERA
     KAEKERKAAE ERERAKAEEE KRAAEEKARL EAEKLKEKKK MEEKKAQEEK AQANLLRKQE
     EDKEAKVEAK KESLPEKLQP TSKKDQVKDN KDKEKAPKEE MKSVWDRKRG VPEQKAQNGE
     RELTTPKLKS TENAFGRSNL KGAANAEAGS EKLKEKQQEA AVELDELKKR REERRKILEE
     EEQKKKQEEA ERKIREEEEK KRMKEEIERR RAEAAEKRQK VPEDGVSEEK KPFKCFSPKG
     SSLKIEERAE FLNKSAQKSG MKPAHTTAVV SKIDSRLEQY TSAVVGNKAA KPAKPAASDL
     PVPAEGVRNI KSMWEKGNVF SSPGGTGTPN KETAGLKVGV SSRINEWLTK TPEGNKSPAP
     KPSDLRPGDV SGKRNLWEKQ SVEKPAASSS KVTATGKKSE TNGLRQFEKE P
//

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