CALD1_CHICK
ID CALD1_CHICK Reviewed; 771 AA.
AC P12957; Q03698; Q90756; Q90761; Q92018; Q99230;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Caldesmon;
DE Short=CDM;
GN Name=CALD1; Synonyms=CAD;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE (ISOFORM GIZZARD
RP H-CAD).
RC TISSUE=Gizzard, and Oviduct;
RX PubMed=2760048; DOI=10.1016/s0021-9258(18)80081-3;
RA Bryan J., Imai M., Lee R., Moore P., Cook R.G., Lin W.-G.;
RT "Cloning and expression of a smooth muscle caldesmon.";
RL J. Biol. Chem. 264:13873-13879(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE (ISOFORM GIZZARD
RP H-CAD).
RC TISSUE=Gizzard;
RX PubMed=2803315; DOI=10.1016/0006-291x(89)91748-8;
RA Hayashi K., Kanda K., Kimizuka F., Kato I., Sobue K.;
RT "Primary structure and functional expression of h-caldesmon complementary
RT DNA.";
RL Biochem. Biophys. Res. Commun. 164:503-511(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE (ISOFORM BRAIN
RP L-CAD).
RC TISSUE=Brain;
RX PubMed=1824698; DOI=10.1016/s0021-9258(18)52442-x;
RA Hayashi K., Fujio Y., Kato I., Sobue K.;
RT "Structural and functional relationships between h- and l-caldesmons.";
RL J. Biol. Chem. 266:355-361(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (GIZZARD H-CAD; BRAIN L-CAD AND GIZZARD
RP L-CAD).
RX PubMed=8250919; DOI=10.1006/bbrc.1993.2453;
RA Haruna M., Hayashi K., Yano H., Takeuchi O., Sobue K.;
RT "Common structural and expressional properties of vertebrate caldesmon
RT genes.";
RL Biochem. Biophys. Res. Commun. 197:145-153(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIZZARD L-CAD).
RC TISSUE=Gizzard;
RX PubMed=1939602; DOI=10.1007/bf01738592;
RA Bryan J., Lee R.;
RT "Sequence of an avian non-muscle caldesmon.";
RL J. Muscle Res. Cell Motil. 12:372-375(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15 (ISOFORM BRAIN L-CAD).
RC TISSUE=Brain;
RX PubMed=8002994; DOI=10.1006/bbrc.1994.1746;
RA Yano H., Hayashi K., Haruna M., Sobue K.;
RT "Identification of two distinct promoters in the chicken caldesmon gene.";
RL Biochem. Biophys. Res. Commun. 201:618-626(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 451-756, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Gizzard;
RX PubMed=2730665; DOI=10.1016/0006-291x(89)91556-8;
RA Hayashi K., Yamada S., Kanda K., Kimizuka F., Kato I., Sobue K.;
RT "35 kDa fragment of h-caldesmon conserves two consensus sequences of the
RT tropomyosin-binding domain in troponin T.";
RL Biochem. Biophys. Res. Commun. 161:38-45(1989).
RN [8]
RP PROTEIN SEQUENCE OF 498-525.
RX PubMed=3401222; DOI=10.1016/0006-291x(88)90177-5;
RA Mornet D., Audemard E., Derancourt J.;
RT "Identification of a 15 kilodalton actin binding region on gizzard
RT caldesmon probed by chemical cross-linking.";
RL Biochem. Biophys. Res. Commun. 154:564-571(1988).
RN [9]
RP PHOSPHORYLATION AT SER-597; SER-682; THR-688; THR-711 AND SER-717.
RX PubMed=1939059; DOI=10.1016/s0021-9258(18)54878-x;
RA Mak A.S., Carpenter M., Smillie L.B., Wang J.H.;
RT "Phosphorylation of caldesmon by p34cdc2 kinase. Identification of
RT phosphorylation sites.";
RL J. Biol. Chem. 266:19971-19975(1991).
RN [10]
RP PHOSPHORYLATION AT TYR-27 AND TYR-640.
RX PubMed=10559276; DOI=10.1074/jbc.274.47.33807;
RA Wang Z., Danielsen A.J., Maihle N.J., McManus M.J.;
RT "Tyrosine phosphorylation of caldesmon is required for binding to the
RT Shc.Grb2 complex.";
RL J. Biol. Chem. 274:33807-33813(1999).
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.
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 -!- 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) 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 muscle forms.
CC -!- PTM: Phosphorylated in non-muscle cells. Phosphorylation by CDK1 during
CC 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 activity.
CC Phosphorylation also occurs in both quiescent and dividing smooth
CC muscle cells with similar effects on the interaction with actin and
CC calmodulin and on microfilaments reorganization (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the caldesmon family. {ECO:0000305}.
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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 PIR; A33430; A33430.
DR PIR; A39038; A39038.
DR RefSeq; NP_989489.1; NM_204158.1.
DR AlphaFoldDB; P12957; -.
DR BMRB; P12957; -.
DR SMR; P12957; -.
DR STRING; 9031.ENSGALP00000021314; -.
DR iPTMnet; P12957; -.
DR PaxDb; P12957; -.
DR PRIDE; P12957; -.
DR GeneID; 373965; -.
DR KEGG; gga:373965; -.
DR CTD; 800; -.
DR VEuPathDB; HostDB:geneid_373965; -.
DR eggNOG; ENOG502QSYB; Eukaryota.
DR InParanoid; P12957; -.
DR OrthoDB; 273358at2759; -.
DR PhylomeDB; P12957; -.
DR SABIO-RK; P12957; -.
DR PRO; PR:P12957; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:AgBase.
DR GO; GO:0005516; F:calmodulin binding; IPI:CAFA.
DR GO; GO:0017022; F:myosin binding; IBA:GO_Central.
DR GO; GO:0045159; F:myosin II binding; IDA:AgBase.
DR GO; GO:0044548; F:S100 protein binding; IPI:AgBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IEA:InterPro.
DR GO; GO:1903611; P:negative regulation of calcium-dependent ATPase activity; IMP:AgBase.
DR DisProt; DP00120; -.
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; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Muscle protein; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..771
FT /note="Caldesmon"
FT /id="PRO_0000089287"
FT REPEAT 251..265
FT /note="1"
FT REPEAT 266..278
FT /note="2"
FT REPEAT 279..291
FT /note="3"
FT REPEAT 294..306
FT /note="4"
FT REPEAT 309..321
FT /note="5"
FT REPEAT 324..336
FT /note="6"
FT REPEAT 337..349
FT /note="7"
FT REPEAT 350..362
FT /note="8"
FT REPEAT 363..375
FT /note="9"
FT REPEAT 378..390
FT /note="10"
FT REGION 23..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..199
FT /note="Myosin and calmodulin-binding"
FT REGION 104..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..390
FT /note="10 X 13 AA approximate tandem repeats"
FT REGION 523..580
FT /note="Tropomyosin-binding"
FT /evidence="ECO:0000255"
FT REGION 612..644
FT /note="Strong actin-binding"
FT REGION 622..632
FT /note="Tropomyosin-binding"
FT /evidence="ECO:0000255"
FT REGION 674..680
FT /note="Calmodulin-binding"
FT REGION 676..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..752
FT /note="Weak actin-binding"
FT COMPBIAS 23..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10559276"
FT MOD_RES 597
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000305|PubMed:1939059"
FT MOD_RES 640
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10559276"
FT MOD_RES 682
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000305|PubMed:1939059"
FT MOD_RES 688
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000305|PubMed:1939059"
FT MOD_RES 711
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000305|PubMed:1939059"
FT MOD_RES 717
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000305|PubMed:1939059"
FT VAR_SEQ 1..24
FT /note="MDDFERRRELRRQKREEMRLEAER -> MISRSYCRQNLSSLSK (in
FT isoform Brain l-cad)"
FT /evidence="ECO:0000305"
FT /id="VSP_004152"
FT VAR_SEQ 200..446
FT /note="Missing (in isoform Brain l-cad and isoform Gizzard
FT l-cad)"
FT /evidence="ECO:0000303|PubMed:1939602"
FT /id="VSP_004153"
FT CONFLICT 318..332
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="D -> V (in Ref. 3; AAA48936)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="N -> NA (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 771 AA; 88747 MW; 518912418DCFC14C CRC64;
MDDFERRREL RRQKREEMRL EAERLSYQRN DDDEEEAARE RRRRARQERL RQKEEGDVSG
EVTEKSEVNA QNSVAEEETK RSTDDEAALL ERLARREERR QKRLQEALER QKEFDPTITD
GSLSVPSRRE VNNVEENEIT 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
