ID CALD1_HUMAN Reviewed; 793 AA. AC Q05682; A8K0X1; Q13978; Q13979; Q14741; Q14742; Q9UD91; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 3. DT 11-NOV-2015, entry version 151. DE RecName: Full=Caldesmon; DE Short=CDM; GN Name=CALD1; Synonyms=CAD, CDM; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RC TISSUE=Lung fibroblast; RX PubMed=1885618; RA Novy R.E., Lin J.L.-C., Lin J.J.-C.; RT "Characterization of cDNA clones encoding a human fibroblast caldesmon RT isoform and analysis of caldesmon expression in normal and transformed RT cells."; RL J. Biol. Chem. 266:16917-16924(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), AND VARIANT ARG-397. RC TISSUE=Aorta; RX PubMed=1555769; DOI=10.1016/0378-1119(92)90376-Z; RA Humphrey M.B., Herrera-Sosa H., Gonzalez G., Lee R., Bryan J.; RT "Cloning of cDNAs encoding human caldesmons."; RL Gene 112:197-204(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5). RX PubMed=1465449; DOI=10.1073/pnas.89.24.12122; RA Hayashi K., Yano H., Hashida T., Takeuchi R., Takeda O., Asada K., RA Takahashi E., Kato I., Sobue K.; RT "Genomic structure of the human caldesmon gene."; RL Proc. Natl. Acad. Sci. U.S.A. 89:12122-12126(1992). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). RC TISSUE=Amygdala; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 497-793, AND FUNCTION. RC TISSUE=Fetal liver; RX PubMed=8227296; DOI=10.1007/BF00121289; RA Huber P.A.J., Redwood C.S., Avent N.D., Tanner M.J.A., Marston S.B.; RT "Identification of functioning regulatory sites and a new myosin RT binding site in the C-terminal 288 amino acids of caldesmon expressed RT from a human clone."; RL J. Muscle Res. Cell Motil. 14:385-391(1993). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-730, PHOSPHORYLATION RP [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 (ISOFORMS 3 AND 5), RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-730, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa RT cells and high confident phosphopeptide identification by cross- RT validation of MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724; THR-730; THR-753 RP AND SER-789, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 RP (ISOFORMS 3 AND 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724; THR-730 AND RP THR-753, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS RP 2; 4 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; TYR-21 RP AND SER-196 (ISOFORMS 3 AND 5), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643 AND SER-789, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND RP 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 (ISOFORMS 3 AND RP 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND THR-753, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND RP 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 (ISOFORMS 3 AND RP 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). 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 Involved in Schwann cell migration during peripheral nerve CC regeneration (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. CC Cytoplasm, myofibril {ECO:0000250}. Note=On thin filaments in CC smooth muscle and on stress fibers in fibroblasts (nonmuscle). CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; 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 Note=Contains a phosphoserine at position 202. CC {ECO:0000244|PubMed:17081983, ECO:0000244|PubMed:20068231, CC ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:24275569}; CC Name=3; Synonyms=HELA L-CAD I; CC IsoId=Q05682-3; Sequence=VSP_004154, VSP_004155; CC Note=Contains a phosphoserine at position 196. Contains a CC phosphoserine at position 12. Contains a phosphotyrosine at CC position 21. {ECO:0000244|PubMed:17081983, CC ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231, CC ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:24275569}; CC Name=4; Synonyms=WI-38 L-CAD II, 1-CAD; CC IsoId=Q05682-4; Sequence=VSP_004156; CC Note=Contains a phosphoserine at position 202. CC {ECO:0000244|PubMed:17081983, ECO:0000244|PubMed:20068231, CC ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:24275569}; CC Name=5; Synonyms=HELA L-CAD II; CC IsoId=Q05682-5; Sequence=VSP_004154, VSP_004156; CC Note=Contains a phosphoserine at position 196. Contains a CC phosphoserine at position 12. Contains a phosphotyrosine at CC position 21. {ECO:0000244|PubMed:17081983, CC ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231, CC ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:24275569}; CC Name=6; CC IsoId=Q05682-6; Sequence=VSP_004155, VSP_043292; CC Note=No experimental confirmation available. Contains a CC phosphoserine at position 202. {ECO:0000244|PubMed:17081983, CC ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692, CC ECO:0000244|PubMed:24275569}; 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. CDK1-mediated phosphorylation promotes Schwann CC cell migration during peripheral nerve regeneration (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the caldesmon family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; AK289686; BAF82375.1; -; mRNA. DR EMBL; AC019014; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC083870; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC040354; AAH40354.1; -; mRNA. DR CCDS; CCDS47716.1; -. [Q05682-3] DR CCDS; CCDS47717.1; -. [Q05682-5] DR CCDS; CCDS5834.1; -. [Q05682-4] DR CCDS; CCDS5835.1; -. [Q05682-1] DR CCDS; CCDS5836.2; -. [Q05682-6] DR PIR; JH0628; JH0628. DR RefSeq; NP_004333.1; NM_004342.6. [Q05682-4] DR RefSeq; NP_149129.2; NM_033138.3. [Q05682-1] DR RefSeq; NP_149130.1; NM_033139.3. [Q05682-3] DR RefSeq; NP_149131.1; NM_033140.3. [Q05682-5] DR RefSeq; NP_149347.2; NM_033157.3. [Q05682-6] DR RefSeq; XP_011514887.1; XM_011516585.1. [Q05682-2] DR UniGene; Hs.490203; -. DR ProteinModelPortal; Q05682; -. DR BioGrid; 107251; 28. DR IntAct; Q05682; 7. DR STRING; 9606.ENSP00000354826; -. DR PhosphoSite; Q05682; -. DR BioMuta; CALD1; -. DR DMDM; 338817891; -. DR OGP; Q05682; -. DR MaxQB; Q05682; -. DR PaxDb; Q05682; -. DR PRIDE; Q05682; -. DR DNASU; 800; -. DR Ensembl; ENST00000361675; ENSP00000354826; ENSG00000122786. [Q05682-1] DR Ensembl; ENST00000361901; ENSP00000354513; ENSG00000122786. [Q05682-4] DR Ensembl; ENST00000393118; ENSP00000376826; ENSG00000122786. [Q05682-3] DR Ensembl; ENST00000417172; ENSP00000398826; ENSG00000122786. [Q05682-4] DR Ensembl; ENST00000422748; ENSP00000395710; ENSG00000122786. [Q05682-6] DR Ensembl; ENST00000424922; ENSP00000393621; ENSG00000122786. [Q05682-5] DR GeneID; 800; -. DR KEGG; hsa:800; -. DR UCSC; uc003vrz.3; human. [Q05682-1] DR UCSC; uc003vsb.3; human. [Q05682-4] DR UCSC; uc003vsc.3; human. [Q05682-3] DR UCSC; uc003vsd.3; human. [Q05682-5] DR UCSC; uc010lmm.3; human. [Q05682-6] DR CTD; 800; -. DR GeneCards; CALD1; -. DR HGNC; HGNC:1441; CALD1. DR HPA; CAB000006; -. DR HPA; HPA008066; -. DR HPA; HPA017330; -. DR MIM; 114213; gene. DR neXtProt; NX_Q05682; -. DR PharmGKB; PA26034; -. DR eggNOG; ENOG410IH1F; Eukaryota. DR eggNOG; ENOG410ZMZI; LUCA. DR GeneTree; ENSGT00730000111125; -. DR HOGENOM; HOG000013012; -. DR HOVERGEN; HBG050785; -. DR InParanoid; Q05682; -. DR KO; K12327; -. DR OMA; QKMPEDS; -. DR OrthoDB; EOG7FNC7W; -. DR PhylomeDB; Q05682; -. DR TreeFam; TF331771; -. DR Reactome; R-HSA-445355; Smooth Muscle Contraction. DR ChiTaRS; CALD1; human. DR GeneWiki; Caldesmon; -. DR GenomeRNAi; 800; -. DR NextBio; 3252; -. DR PRO; PR:Q05682; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; Q05682; -. DR CleanEx; HS_CAD; -. DR CleanEx; HS_CALD1; -. DR ExpressionAtlas; Q05682; baseline and differential. DR Genevisible; Q05682; HS. DR GO; GO:0030478; C:actin cap; IEA:Ensembl. DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA. DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0003779; F:actin binding; TAS:ProtInc. DR GO; GO:0005516; F:calmodulin binding; TAS:ProtInc. DR GO; GO:0005523; F:tropomyosin binding; TAS:ProtInc. DR GO; GO:0006928; P:movement of cell or subcellular component; TAS:UniProtKB. DR GO; GO:0006936; P:muscle contraction; TAS:Reactome. DR InterPro; IPR006017; Caldesmon. DR InterPro; IPR006018; Caldesmon_LSP. DR PANTHER; PTHR18949; PTHR18949; 2. DR PANTHER; PTHR18949:SF0; PTHR18949:SF0; 2. DR Pfam; PF02029; Caldesmon; 2. DR PRINTS; PR01076; CALDESMON. PE 1: Evidence at protein level; KW Actin-binding; Alternative splicing; Calmodulin-binding; KW Complete proteome; Cytoplasm; Cytoskeleton; Muscle protein; KW Phosphoprotein; Polymorphism; Reference proteome; Repeat. FT CHAIN 1 793 Caldesmon. FT /FTId=PRO_0000089288. FT REPEAT 319 332 1. FT REPEAT 333 346 2. FT REPEAT 347 360 3. FT REGION 26 207 Myosin and calmodulin-binding. FT {ECO:0000250}. FT REGION 319 375 3 X 14 AA tandem repeats of E-E-E-K-R-A- FT A-E-E-R-Q-R-I-K. FT REGION 564 621 Tropomyosin-binding. {ECO:0000255}. FT REGION 653 686 Strong actin-binding. {ECO:0000250}. FT REGION 664 674 Tropomyosin-binding. {ECO:0000255}. FT REGION 716 722 Calmodulin-binding. {ECO:0000250}. FT REGION 768 793 Weak actin-binding. {ECO:0000250}. FT COMPBIAS 39 46 Poly-Arg. FT COMPBIAS 81 86 Poly-Thr. FT COMPBIAS 189 196 Poly-Glu. FT COMPBIAS 376 379 Poly-Glu. FT COMPBIAS 540 543 Poly-Arg. FT COMPBIAS 580 583 Poly-Glu. FT COMPBIAS 597 600 Poly-Glu. FT MOD_RES 129 129 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 643 643 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 724 724 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 730 730 Phosphothreonine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:17924679, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 753 753 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 759 759 Phosphoserine. FT {ECO:0000250|UniProtKB:Q62736}. FT MOD_RES 789 789 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:21406692}. FT VAR_SEQ 1 24 MDDFERRRELRRQKREEMRLEAER -> MLGGSGSHGRRSL FT AALSQ (in isoform 3 and isoform 5). FT {ECO:0000303|PubMed:1465449}. FT /FTId=VSP_004154. FT VAR_SEQ 208 462 Missing (in isoform 4 and isoform 5). FT {ECO:0000303|PubMed:1465449, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:1555769, FT ECO:0000303|PubMed:1885618}. FT /FTId=VSP_004156. FT VAR_SEQ 208 436 Missing (in isoform 2, isoform 3 and FT isoform 6). {ECO:0000303|PubMed:1465449, FT ECO:0000303|PubMed:14702039}. FT /FTId=VSP_004155. FT VAR_SEQ 660 660 Missing (in isoform 6). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043292. FT VARIANT 397 397 H -> R (in dbSNP:rs6973420). FT {ECO:0000269|PubMed:1555769}. FT /FTId=VAR_065254. FT CONFLICT 530 530 V -> M (in Ref. 1; AAA35636). FT {ECO:0000305}. SQ SEQUENCE 793 AA; 93231 MW; 7468E2C3E40BF697 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 //