CALD1_RAT
ID CALD1_RAT Reviewed; 531 AA.
AC Q62736;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Non-muscle caldesmon;
DE Short=CDM;
DE AltName: Full=L-caldesmon;
GN Name=Cald1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS, AND PHOSPHORYLATION AT SER-249;
RP SER-462; THR-468; SER-491; SER-497 AND SER-527.
RC TISSUE=Liver;
RX PubMed=7876150; DOI=10.1074/jbc.270.8.4023;
RA Yamashiro S., Yamakita Y., Yoshida K.-S., Takiguchi K., Matsumura F.;
RT "Characterization of the COOH terminus of non-muscle caldesmon mutants
RT lacking mitosis-specific phosphorylation sites.";
RL J. Biol. Chem. 270:4023-4030(1995).
RN [2]
RP PHOSPHORYLATION BY CDK1.
RX PubMed=1986309; DOI=10.1038/349169a0;
RA Yamashiro S., Yamakita Y., Hosoya H., Matsumura F.;
RT "Phosphorylation of non-muscle caldesmon by p34cdc2 kinase during
RT mitosis.";
RL Nature 349:169-172(1991).
RN [3]
RP FUNCTION IN SCHWANN CELL MIGRATION, AND PHOSPHORYLATION BY CDK1.
RX PubMed=17200138; DOI=10.1242/jcs.03322;
RA Han I.S., Seo T.B., Kim K.-H., Yoon J.-H., Yoon S.-J., Namgung U.;
RT "Cdc2-mediated Schwann cell migration during peripheral nerve
RT regeneration.";
RL J. Cell Sci. 120:246-255(2007).
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. Involved in Schwann cell migration during peripheral
CC nerve regeneration. {ECO:0000269|PubMed:17200138}.
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 -!- TISSUE SPECIFICITY: High-molecular-weight caldesmon (h-caldesmon) is
CC predominantly expressed in smooth muscles, whereas low-molecular-weight
CC caldesmon (l-caldesmon) is widely distributed in non-muscle tissues and
CC cells. Not expressed in skeletal muscle or heart.
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 CDK1 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. CDK1-mediated phosphorylation promotes Schwann cell
CC migration during peripheral nerve regeneration.
CC {ECO:0000269|PubMed:17200138, ECO:0000269|PubMed:1986309,
CC ECO:0000269|PubMed:7876150}.
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; U18419; AAA68521.1; -; mRNA.
DR PIR; A55887; A55887.
DR RefSeq; NP_037278.1; NM_013146.2.
DR AlphaFoldDB; Q62736; -.
DR SMR; Q62736; -.
DR BioGRID; 247716; 1.
DR STRING; 10116.ENSRNOP00000043767; -.
DR iPTMnet; Q62736; -.
DR PhosphoSitePlus; Q62736; -.
DR jPOST; Q62736; -.
DR PaxDb; Q62736; -.
DR PRIDE; Q62736; -.
DR GeneID; 25687; -.
DR KEGG; rno:25687; -.
DR UCSC; RGD:2256; rat.
DR CTD; 800; -.
DR RGD; 2256; Cald1.
DR eggNOG; ENOG502QSYB; Eukaryota.
DR InParanoid; Q62736; -.
DR OrthoDB; 1038798at2759; -.
DR PhylomeDB; Q62736; -.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR PRO; PR:Q62736; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030478; C:actin cap; ISO:RGD.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005884; C:actin filament; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO: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; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:RGD.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
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 PANTHER; PTHR18949; PTHR18949; 2.
DR PANTHER; PTHR18949:SF0; PTHR18949:SF0; 2.
DR Pfam; PF02029; Caldesmon; 1.
DR PRINTS; PR01076; CALDESMON.
PE 1: Evidence at protein level;
KW Actin-binding; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Muscle protein; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..531
FT /note="Non-muscle caldesmon"
FT /id="PRO_0000089290"
FT REGION 20..200
FT /note="Myosin and calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 21..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..360
FT /note="Tropomyosin-binding"
FT /evidence="ECO:0000255"
FT REGION 392..424
FT /note="Strong actin-binding"
FT /evidence="ECO:0000250"
FT REGION 402..412
FT /note="Tropomyosin-binding"
FT /evidence="ECO:0000255"
FT REGION 454..460
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 458..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..531
FT /note="Weak actin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 22..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05682"
FT MOD_RES 249
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:7876150"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05682"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05682"
FT MOD_RES 462
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:7876150"
FT MOD_RES 468
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:7876150"
FT MOD_RES 491
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:7876150"
FT MOD_RES 497
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:7876150"
FT MOD_RES 527
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:7876150"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q05682"
FT MUTAGEN 249
FT /note="S->A: Decreases strongly phosphorylation-dependent
FT actin binding."
FT /evidence="ECO:0000269|PubMed:7876150"
FT MUTAGEN 462
FT /note="S->A: Decreases phosphorylation-dependent actin
FT binding."
FT /evidence="ECO:0000269|PubMed:7876150"
FT MUTAGEN 468
FT /note="T->A: Decreases phosphorylation-dependent actin
FT binding."
FT /evidence="ECO:0000269|PubMed:7876150"
FT MUTAGEN 491
FT /note="S->A: Decreases phosphorylation-dependent actin
FT binding."
FT /evidence="ECO:0000269|PubMed:7876150"
FT MUTAGEN 497
FT /note="S->A: Decreases phosphorylation-dependent actin
FT binding."
FT /evidence="ECO:0000269|PubMed:7876150"
FT MUTAGEN 527
FT /note="S->A: Does not decrease phosphorylation-dependent
FT actin binding."
FT /evidence="ECO:0000269|PubMed:7876150"
SQ SEQUENCE 531 AA; 60584 MW; CBBEC50271A23829 CRC64;
MLSRSGSQGR RCLATLSQIA YQRNDDDEEE AARERRRRAR QERLRQKQEE ESLGQVTDQV
EAHVQNSAPD 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
