(data stored in ACNUC6444 zone)

HOGENOM: HS7_PE3875

ID   HS7_PE3875                           STANDARD;      PRT;   793 AA.
AC   HS7_PE3875; Q05682; Q13978; Q13979; Q14741; Q14742; Q9UD91;
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; (HS7.PE3875).
GN   Name=CALD1; Synonyms=CAD, CDM;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS7.PE3875.
CC       Homo sapiens chromosome 7 GRCh37  sequence 1..159128663 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:CALD1_HUMAN
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=5;
CC       Name=1; Synonyms=H-CAD;
CC         IsoId=Q05682-1; Sequence=Displayed;
CC       Name=2; Synonyms=WI-38 L-CAD I;
CC         IsoId=Q05682-2; Sequence=VSP_004155;
CC       Name=3; Synonyms=HELA L-CAD I;
CC         IsoId=Q05682-3; Sequence=VSP_004154, VSP_004155;
CC       Name=4; Synonyms=WI-38 L-CAD II, 1-CAD;
CC         IsoId=Q05682-4; Sequence=VSP_004156;
CC       Name=5; Synonyms=HELA L-CAD II;
CC         IsoId=Q05682-5; Sequence=VSP_004154, VSP_004156;
CC   -!- TISSUE SPECIFICITY: High-molecular-weight caldesmon (isoform 1) is
CC       predominantly expressed in smooth muscles, whereas low-molecular-
CC       weight caldesmon (isoforms 2, 3, 4 and 5) are widely distributed
CC       in non-muscle tissues and cells. Not expressed in skeletal muscle
CC       or 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 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 (By similarity).
CC   -!- SIMILARITY: Belongs to the caldesmon family.
CC   -!- GENE_FAMILY: HOG000013012 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000122786;ENST00000361675;ENSP00000354826.
DR   EMBL; AC019014; - ;
DR   EMBL; AC083870; - ;
DR   EMBL; AK304729; - ;
DR   EMBL; BC040354; - ;
DR   EMBL; BX538339; - ;
DR   EMBL; D90452; - ;
DR   EMBL; D90453; - ;
DR   EMBL; M64110; - ;
DR   EMBL; M83216; - ;
DR   UniProtKB/Swiss-Prot; Q05682; Q13978; Q13979; Q14741; Q14742; Q9UD91; -.
DR   EMBL; M64110; AAA35636.1; -; mRNA.
DR   EMBL; M83216; AAA58420.1; -; mRNA.
DR   EMBL; M83216; AAA58419.1; -; mRNA.
DR   EMBL; D90452; BAA14418.1; -; mRNA.
DR   EMBL; D90453; BAA14419.1; -; mRNA.
DR   EMBL; AC019014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC083870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC040354; AAH40354.1; -; mRNA.
DR   IPI; IPI00014516; -.
DR   IPI; IPI00218694; -.
DR   IPI; IPI00218695; -.
DR   IPI; IPI00333771; -.
DR   IPI; IPI01013595; -.
DR   PIR; JH0628; JH0628.
DR   RefSeq; NP_004333.1; NM_004342.6.
DR   RefSeq; NP_149129.2; NM_033138.3.
DR   RefSeq; NP_149130.1; NM_033139.3.
DR   RefSeq; NP_149131.1; NM_033140.3.
DR   UniGene; Hs.490203; -.
DR   IntAct; Q05682; 6.
DR   STRING; Q05682; -.
DR   PhosphoSite; Q05682; -.
DR   OGP; Q05682; -.
DR   PRIDE; Q05682; -.
DR   Ensembl; ENST00000361675; ENSP00000354826; ENSG00000122786.
DR   GeneID; 800; -.
DR   KEGG; hsa:800; -.
DR   UCSC; uc003vrz.1; human.
DR   CTD; 800; -.
DR   GeneCards; GC07P128770; -.
DR   H-InvDB; HIX0007104; -.
DR   HGNC; HGNC:1441; CALD1.
DR   HPA; CAB000006; -.
DR   HPA; HPA008066; -.
DR   HPA; HPA017330; -.
DR   MIM; 114213; gene.
DR   neXtProt; NX_Q05682; -.
DR   eggNOG; prNOG10813; -.
DR   InParanoid; Q05682; -.
DR   Reactome; REACT_17044; Muscle contraction.
DR   NextBio; 3252; -.
DR   ArrayExpress; Q05682; -.
DR   Bgee; Q05682; -.
DR   CleanEx; HS_CAD; -.
DR   CleanEx; HS_CALD1; -.
DR   Genevestigator; Q05682; -.
DR   GermOnline; ENSG00000122786; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR   GO; GO:0005516; F:calmodulin binding; TAS:ProtInc.
DR   GO; GO:0017022; F:myosin binding; IEA:InterPro.
DR   GO; GO:0005523; F:tropomyosin binding; TAS:ProtInc.
DR   GO; GO:0006928; P:cellular component movement; TAS:UniProtKB.
DR   GO; GO:0006936; P:muscle contraction; EXP:Reactome.
DR   InterPro; IPR006017; Caldesmon.
DR   InterPro; IPR006018; Caldesmon_LSP.
DR   Pfam; PF02029; Caldesmon; 1.
DR   PRINTS; PR01076; CALDESMON.
DR   HOGENOMDNA; HS7.PE3875; -.
KW   ENSG000001227861755old_1320000031; ENSP000003548267901old_1320000031;
KW   B4E3I0_HUMAN; C9JE79_HUMAN; Q7Z2Y9_HUMAN; AC019014; AC083870; AK304729;
KW   BX538339; D90452; D90453; M64110; M83216;
KW   Actin-binding; Alternative splicing; Calmodulin-binding;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Muscle protein;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat.
SQ   SEQUENCE   793 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDDFERRREL RRQKREEMRL EAERIAYQRN DDDEEEAARE RRRRARQERL RQKQEEESLG
     QVTDQVEVNA QNSVPDEEAK TTTTNTQVEG DDEAAFLERL ARREERRQKR LQEALERQKE
     FDPTITDASL SLPSRRMQND TAENETTEKE EKSESRQERY EIEETETVTK SYQKNDWRDA
     EENKKEDKEK EEEEEEKPKR GSIGENQVEV MVEEKTTESQ EETVVMSLKN GQISSEEPKQ
     EEEREQGSDE ISHHEKMEEE DKERAEAERA RLEAEERERI KAEQDKKIAD ERARIEAEEK
     AAAQERERRE AEERERMREE EKRAAEERQR IKEEEKRAAE ERQRIKEEEK RAAEERQRIK
     EEEKRAAEER QRARAEEEEK AKVEEQKRNK QLEEKKHAMQ ETKIKGEKVE QKIEGKWVNE
     KKAQEDKLQT AVLKKQGEEK GTKVQAKREK LQEDKPTFKK EEIKDEKIKK DKEPKEEVKS
     FMDRKKGFTE VKSQNGEFMT HKLKHTENTF SRPGGRASVD TKEAEGAPQV EAGKRLEELR
     RRRGETESEE FEKLKQKQQE AALELEELKK KREERRKVLE EEEQRRKQEE ADRKLREEEE
     KRRLKEEIER RRAEAAEKRQ KMPEDGLSDD KKPFKCFTPK GSSLKIEERA EFLNKSVQKS
     SGVKSTHQAA IVSKIDSRLE QYTSAIEGTK SAKPTKPAAS DLPVPAEGVR NIKSMWEKGN
     VFSSPTAAGT PNKETAGLKV GVSSRINEWL TKTPDGNKSP APKPSDLRPG DVSSKRNLWE
     KQSVDKVTSP TKV
//

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