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Cysteine and glycine-rich protein 3 (Cardiac LIM protein) (Cysteine-rich protein 3) (CRP3) (LIM domain protein, cardiac) (Muscle LIM protein)

 CSRP3_HUMAN             Reviewed;         194 AA.
P50461; Q9P131; S4S7M7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 166.
RecName: Full=Cysteine and glycine-rich protein 3;
AltName: Full=Cardiac LIM protein;
AltName: Full=Cysteine-rich protein 3;
Short=CRP3;
AltName: Full=LIM domain protein, cardiac;
AltName: Full=Muscle LIM protein;
Name=CSRP3; Synonyms=CLP, MLP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
PubMed=7490106; DOI=10.1006/geno.1995.1200;
Fung Y.W., Wang R.X., Heng H.H.Q., Liew C.C.;
"Mapping of a human LIM protein (CLP) to human chromosome 11p15.1 by
fluorescence in situ hybridization.";
Genomics 28:602-603(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Muscle;
Medvedev A., Jetten A.M.;
"Cloning of the gene encoding the human muscle LIM protein, a
regulator of myogenesis.";
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Yasunaga S., Harada H., Kimura A.;
"Cloning and characterization of the human muscle LIM protein gene.";
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart, and Skeletal muscle;
Chen K.H., Zhang J.F., Ma D.L., Tang J.;
"A novel member of LIM gene family involved in cardiovascular
diseases.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2),
SUBCELLULAR LOCATION (ISOFORM 2), TISSUE SPECIFICITY, INTERACTION WITH
MYOD1; MYOG; TCAP AND ALPHA-ACTININ, AND SELF-ASSOCIATION.
PubMed=24860983; DOI=10.1111/febs.12859;
Vafiadaki E., Arvanitis D.A., Papalouka V., Terzis G.,
Roumeliotis T.I., Spengos K., Garbis S.D., Manta P., Kranias E.G.,
Sanoudou D.;
"Muscle lim protein isoform negatively regulates striated muscle actin
dynamics and differentiation.";
FEBS J. 281:3261-3279(2014).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skeletal muscle, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH TCAP.
PubMed=15582318; DOI=10.1016/j.jacc.2004.08.058;
Hayashi T., Arimura T., Itoh-Satoh M., Ueda K., Hohda S., Inagaki N.,
Takahashi M., Hori H., Yasunami M., Nishi H., Koga Y., Nakamura H.,
Matsuzaki M., Choi B.Y., Bae S.W., You C.W., Han K.H., Park J.E.,
Knoell R., Hoshijima M., Chien K.R., Kimura A.;
"Tcap gene mutations in hypertrophic cardiomyopathy and dilated
cardiomyopathy.";
J. Am. Coll. Cardiol. 44:2192-2201(2004).
[8]
INTERACTION WITH NRAP AND ACTN2, AND CHARACTERIZATION OF VARIANT CMH12
GLY-58.
PubMed=15205937; DOI=10.1007/s00441-004-0873-y;
Gehmlich K., Geier C., Osterziel K.J., Van der Ven P.F., Fuerst D.O.;
"Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP
and alpha-actinin and their implication for hypertrophic
cardiomyopathy.";
Cell Tissue Res. 317:129-136(2004).
[9]
FUNCTION, AND INTERACTION WITH CFL2.
PubMed=19752190; DOI=10.1128/MCB.00654-09;
Papalouka V., Arvanitis D.A., Vafiadaki E., Mavroidis M.,
Papadodima S.A., Spiliopoulou C.A., Kremastinos D.T., Kranias E.G.,
Sanoudou D.;
"Muscle LIM protein interacts with cofilin 2 and regulates F-actin
dynamics in cardiac and skeletal muscle.";
Mol. Cell. Biol. 29:6046-6058(2009).
[10]
FUNCTION, SUBCELLULAR LOCATION, SELF-ASSOCIATION, AND LIM ZINC-BINDING
DOMAINS.
PubMed=24934443; DOI=10.1128/MCB.00651-14;
Hoffmann C., Moreau F., Moes M., Luthold C., Dieterle M., Goretti E.,
Neumann K., Steinmetz A., Thomas C.;
"Human muscle LIM protein dimerizes along the actin cytoskeleton and
cross-links actin filaments.";
Mol. Cell. Biol. 34:3053-3065(2014).
[11]
FUNCTION, PHOSPHORYLATION, CHARACTERIZATION OF VARIANTS CMH12 PRO-44;
54-ARG-GLY-55 AND GLY-58, CHARACTERIZATION OF VARIANT ARG-72, AND
MUTAGENESIS OF LYS-69.
PubMed=27353086; DOI=10.1038/ncomms12120;
Lange S., Gehmlich K., Lun A.S., Blondelle J., Hooper C., Dalton N.D.,
Alvarez E.A., Zhang X., Bang M.L., Abassi Y.A., Dos Remedios C.G.,
Peterson K.L., Chen J., Ehler E.;
"MLP and CARP are linked to chronic PKCalpha signalling in dilated
cardiomyopathy.";
Nat. Commun. 7:12120-12120(2016).
[12]
STRUCTURE BY NMR OF 7-66 AND 119-176.
PubMed=19230835; DOI=10.1016/j.febslet.2009.02.021;
Schallus T., Feher K., Ulrich A.S., Stier G., Muhle-Goll C.;
"Structure and dynamics of the human muscle LIM protein.";
FEBS Lett. 583:1017-1022(2009).
[13]
VARIANT CMD1M ARG-4, INTERACTION WITH TCAP, AND CHARACTERIZATION OF
VARIANT CMD1M ARG-4.
PubMed=12507422; DOI=10.1016/S0092-8674(02)01226-6;
Knoell R., Hoshijima M., Hoffman H.M., Person V., Lorenzen-Schmidt I.,
Bang M.-L., Hayashi T., Shiga N., Yasukawa H., Schaper W., McKenna W.,
Yokoyama M., Schork N.J., Omens J.H., McCulloch A.D., Kimura A.,
Gregorio C.C., Poller W., Schaper J., Schultheiss H.P., Chien K.R.;
"The cardiac mechanical stretch sensor machinery involves a Z disc
complex that is defective in a subset of human dilated
cardiomyopathy.";
Cell 111:943-955(2002).
[14]
VARIANTS CMH12 PRO-44; 54-ARG-GLY-55 AND GLY-58.
PubMed=12642359; DOI=10.1161/01.CIR.0000056522.82563.5F;
Geier C., Perrot A., Ozcelik C., Binner P., Counsell D., Hoffmann K.,
Pilz B., Martiniak Y., Gehmlich K., van der Ven P.F.M., Furst D.O.,
Vornwald A., von Hodenberg E., Nurnberg P., Scheffold T., Dietz R.,
Osterziel K.J.;
"Mutations in the human muscle LIM protein gene in families with
hypertrophic cardiomyopathy.";
Circulation 107:1390-1395(2003).
[15]
VARIANT CMD1M ARG-72.
PubMed=19412328; DOI=10.1111/j.1752-8062.2008.00017.x;
Hershberger R.E., Parks S.B., Kushner J.D., Li D., Ludwigsen S.,
Jakobs P., Nauman D., Burgess D., Partain J., Litt M.;
"Coding sequence mutations identified in MYH7, TNNT2, SCN5A, CSRP3,
LBD3, and TCAP from 313 patients with familial or idiopathic dilated
cardiomyopathy.";
Clin. Transl. Sci. 1:21-26(2008).
[16]
CHARACTERIZATION OF VARIANT CMD1M ARG-4, VARIANT CMH12 GLY-58, AND
SUBCELLULAR LOCATION.
PubMed=18505755; DOI=10.1093/hmg/ddn160;
Geier C., Gehmlich K., Ehler E., Hassfeld S., Perrot A., Hayess K.,
Cardim N., Wenzel K., Erdmann B., Krackhardt F., Posch M.G.,
Osterziel K.J., Bublak A., Nagele H., Scheffold T., Dietz R.,
Chien K.R., Spuler S., Furst D.O., Nurnberg P., Ozcelik C.;
"Beyond the sarcomere: CSRP3 mutations cause hypertrophic
cardiomyopathy.";
Hum. Mol. Genet. 17:2753-2765(2008).
-!- FUNCTION: Positive regulator of myogenesis. Acts as cofactor for
myogenic bHLH transcription factors such as MYOD1, and probably
MYOG and MYF6. Enhances the DNA-binding activity of the MYOD1:TCF3
isoform E47 complex and may promote formation of a functional
MYOD1:TCF3 isoform E47:MEF2A complex involved in myogenesis (By
similarity). Plays a crucial and specific role in the organization
of cytosolic structures in cardiomyocytes. Could play a role in
mechanical stretch sensing. May be a scaffold protein that
promotes the assembly of interacting proteins at Z-line
structures. It is essential for calcineurin anchorage to the Z
line. Required for stress-induced calcineurin-NFAT activation (By
similarity). The role in regulation of cytoskeleton dynamics by
association with CFL2 is reported conflictingly: Shown to enhance
CFL2-mediated F-actin depolymerization dependent on the CSRP3:CFL2
molecular ratio, and also shown to reduce the ability of CLF1 and
CFL2 to enhance actin depolymerization (PubMed:19752190,
PubMed:24934443). Proposed to contribute to the maintenance of
muscle cell integerity through an actin-based mechanism. Can
directly bind to actin filaments, cross-link actin filaments into
bundles without polarity selectivity and protect them from
dilution- and cofilin-mediated depolymerization; the function
seems to involve its self-association (PubMed:24934443). In vitro
can inhibit PKC/PRKCA activity (PubMed:27353086). Proposed to be
involved in cardiac stress signaling by down-regulating excessive
PKC/PRKCA signaling (By similarity).
{ECO:0000250|UniProtKB:P50462, ECO:0000250|UniProtKB:P50463,
ECO:0000269|PubMed:19752190, ECO:0000269|PubMed:24934443,
ECO:0000269|PubMed:27353086}.
-!- FUNCTION: Isoform 2: May play a role in early sarcomere
organization. Overexpression in myotubes negatively regulates
myotube differentiation. By association with isoform 1 and thus
changing the CSRP3 isoform 1:CFL2 stoichiometry is proposed to
down-regulate CFL2-mediated F-actin depolymerization.
{ECO:0000269|PubMed:24860983}.
-!- SUBUNIT: Self-associates. Oligomeric in the cytoplasm and
monomeric in the nucleus (By similarity). Homooligomers
preferentially form along the actin cytoskeleton. Isoform 2
interacts with isoform 1 (PubMed:24934443, PubMed:24860983).
Isoform 1 but not isoform 2 interacts with MYOD1 and MYOG. Isoform
1 interacts with TCAP, ACTN2 and NRAP. Isoform 2 interacts with
TCAP and alpha-actinin (PubMed:24860983, PubMed:15582318,
PubMed:15205937, PubMed:12507422). Interacts with LDHD. Interacts
(via N-terminus)with GLRX3 (via C-terminus) and PPP3CA; GLRX3 and
calcineurin compete for interaction with CSRP3. Interacts with
MYF6 (By similarity). Interacts with CFL2; the stoichiometry
influences F-actin depolymerization and possibly two molecules of
CFL2 can interact with one molecule of CSRP3 resulting in the
highest functional impact; the interaction is stronger with
phosphorylated CFL2 (PubMed:19752190).
{ECO:0000250|UniProtKB:P50462, ECO:0000250|UniProtKB:P50463,
ECO:0000269|PubMed:12507422, ECO:0000269|PubMed:15205937,
ECO:0000269|PubMed:15582318, ECO:0000269|PubMed:19752190,
ECO:0000269|PubMed:24860983, ECO:0000269|PubMed:24934443}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-5658719, EBI-5658719;
P35609:ACTN2; NbExp=4; IntAct=EBI-5658719, EBI-77797;
Q9Y281:CFL2; NbExp=2; IntAct=EBI-5658719, EBI-351218;
Q86VF7:NRAP; NbExp=2; IntAct=EBI-5658719, EBI-5660292;
O15273:TCAP; NbExp=3; IntAct=EBI-5658719, EBI-954089;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P50463}.
Cytoplasm {ECO:0000269|PubMed:18505755}. Cytoplasm, cytoskeleton
{ECO:0000305}. Cytoplasm, myofibril, sarcomere, Z line
{ECO:0000269|PubMed:24860983}. Cytoplasm, myofibril, sarcomere
{ECO:0000269|PubMed:24934443}. Note=Nucleocytoplasmic shuttling
protein. Mainly cytoplasmic. In the Z line, found associated with
GLRX3 (By similarity). {ECO:0000250|UniProtKB:P50462,
ECO:0000250|UniProtKB:P50463}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, myofibril, sarcomere,
Z line {ECO:0000269|PubMed:24860983}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=MLP-a;
IsoId=P50461-1; Sequence=Displayed;
Name=2; Synonyms=MLP-b;
IsoId=P50461-2; Sequence=VSP_058575, VSP_058576;
-!- TISSUE SPECIFICITY: Cardiac and slow-twitch skeletal muscles.
Isoform 2 is expressed in striated muscle. Isoform 2 is
specifically expressed at higher levels in patients with
neuromuscular diseases, such as limb-girdle muscular dystrophy 2A
(LGMD2A), Duchenne muscular dystrophy (DMD) and dermatomyositis
(PubMed:24860983). {ECO:0000269|PubMed:24860983}.
-!- DOMAIN: LIM zinc-binding domain 1 is required for self-
association. LIM zinc-binding domain 1 and LIM zinc-binding domain
2 both are required for optimal actin-bundling activity
(PubMed:24934443). LIM zinc-binding domain 1 mediates binding to
MYOD1. LIM zinc-binding domain 2 mediates binding to SPTB (By
similarity). {ECO:0000250|UniProtKB:P50463,
ECO:0000269|PubMed:24934443}.
-!- PTM: Phosphorylated by PKC/PRKCA. {ECO:0000305|PubMed:27353086}.
-!- DISEASE: Cardiomyopathy, dilated 1M (CMD1M) [MIM:607482]: A
disorder characterized by ventricular dilation and impaired
systolic function, resulting in congestive heart failure and
arrhythmia. Patients are at risk of premature death.
{ECO:0000269|PubMed:12507422, ECO:0000269|PubMed:18505755,
ECO:0000269|PubMed:19412328}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cardiomyopathy, familial hypertrophic 12 (CMH12)
[MIM:612124]: A hereditary heart disorder characterized by
ventricular hypertrophy, which is usually asymmetric and often
involves the interventricular septum. The symptoms include
dyspnea, syncope, collapse, palpitations, and chest pain. They can
be readily provoked by exercise. The disorder has inter- and
intrafamilial variability ranging from benign to malignant forms
with high risk of cardiac failure and sudden cardiac death.
{ECO:0000269|PubMed:12642359, ECO:0000269|PubMed:15205937,
ECO:0000269|PubMed:18505755, ECO:0000269|PubMed:27353086}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
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EMBL; U20324; AAA91104.1; -; mRNA.
EMBL; U49837; AAA92571.1; -; mRNA.
EMBL; U72898; AAD00189.1; -; Genomic_DNA.
EMBL; U72894; AAD00189.1; JOINED; Genomic_DNA.
EMBL; U72895; AAD00189.1; JOINED; Genomic_DNA.
EMBL; U72896; AAD00189.1; JOINED; Genomic_DNA.
EMBL; U72897; AAD00189.1; JOINED; Genomic_DNA.
EMBL; U72899; AAD00183.1; -; mRNA.
EMBL; AF121260; AAF28868.1; -; mRNA.
EMBL; JN898958; AFH66949.1; -; mRNA.
EMBL; BC005900; AAH05900.1; -; mRNA.
EMBL; BC024010; AAH24010.1; -; mRNA.
EMBL; BC057221; AAH57221.1; -; mRNA.
CCDS; CCDS7848.1; -. [P50461-1]
RefSeq; NP_003467.1; NM_003476.4. [P50461-1]
UniGene; Hs.83577; -.
PDB; 2O10; NMR; -; A=7-66.
PDB; 2O13; NMR; -; A=119-176.
PDBsum; 2O10; -.
PDBsum; 2O13; -.
ProteinModelPortal; P50461; -.
SMR; P50461; -.
BioGrid; 113736; 7.
IntAct; P50461; 9.
STRING; 9606.ENSP00000265968; -.
iPTMnet; P50461; -.
PhosphoSitePlus; P50461; -.
BioMuta; CSRP3; -.
DMDM; 1705933; -.
EPD; P50461; -.
MaxQB; P50461; -.
PaxDb; P50461; -.
PeptideAtlas; P50461; -.
PRIDE; P50461; -.
DNASU; 8048; -.
Ensembl; ENST00000265968; ENSP00000265968; ENSG00000129170. [P50461-1]
Ensembl; ENST00000533783; ENSP00000431813; ENSG00000129170. [P50461-1]
GeneID; 8048; -.
KEGG; hsa:8048; -.
UCSC; uc001mpk.4; human. [P50461-1]
CTD; 8048; -.
DisGeNET; 8048; -.
EuPathDB; HostDB:ENSG00000129170.8; -.
GeneCards; CSRP3; -.
GeneReviews; CSRP3; -.
HGNC; HGNC:2472; CSRP3.
HPA; HPA042581; -.
MalaCards; CSRP3; -.
MIM; 600824; gene.
MIM; 607482; phenotype.
MIM; 612124; phenotype.
neXtProt; NX_P50461; -.
OpenTargets; ENSG00000129170; -.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 155; Familial isolated hypertrophic cardiomyopathy.
PharmGKB; PA26971; -.
eggNOG; ENOG410ITI8; Eukaryota.
eggNOG; ENOG410Z840; LUCA.
GeneTree; ENSGT00550000074548; -.
HOGENOM; HOG000111233; -.
HOVERGEN; HBG051143; -.
InParanoid; P50461; -.
KO; K09377; -.
OMA; SEIYCKS; -.
OrthoDB; EOG091G11RX; -.
PhylomeDB; P50461; -.
TreeFam; TF313758; -.
SIGNOR; P50461; -.
EvolutionaryTrace; P50461; -.
GeneWiki; CSRP3; -.
GenomeRNAi; 8048; -.
PRO; PR:P50461; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000129170; -.
CleanEx; HS_CSRP3; -.
ExpressionAtlas; P50461; baseline and differential.
Genevisible; P50461; HS.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0042805; F:actinin binding; ISS:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008307; F:structural constituent of muscle; IMP:BHF-UCL.
GO; GO:0031433; F:telethonin binding; IDA:BHF-UCL.
GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0003300; P:cardiac muscle hypertrophy; IMP:BHF-UCL.
GO; GO:0048738; P:cardiac muscle tissue development; ISS:BHF-UCL.
GO; GO:0055003; P:cardiac myofibril assembly; ISS:BHF-UCL.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:BHF-UCL.
GO; GO:0035995; P:detection of muscle stretch; IMP:BHF-UCL.
GO; GO:1903919; P:negative regulation of actin filament severing; IDA:MGI.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IDA:MGI.
GO; GO:1903920; P:positive regulation of actin filament severing; IDA:MGI.
GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0033365; P:protein localization to organelle; IMP:BHF-UCL.
GO; GO:0002026; P:regulation of the force of heart contraction; ISS:BHF-UCL.
GO; GO:0007519; P:skeletal muscle tissue development; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR001781; Znf_LIM.
Pfam; PF00412; LIM; 2.
SMART; SM00132; LIM; 2.
PROSITE; PS00478; LIM_DOMAIN_1; 2.
PROSITE; PS50023; LIM_DOMAIN_2; 2.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative splicing; Cardiomyopathy;
Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
Differentiation; Disease mutation; LIM domain; Metal-binding;
Myogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Transcription; Transcription regulation; Zinc.
CHAIN 1 194 Cysteine and glycine-rich protein 3.
/FTId=PRO_0000075727.
DOMAIN 10 61 LIM zinc-binding 1. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 120 171 LIM zinc-binding 2. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
REGION 1 5 Interaction with TCAP.
{ECO:0000269|PubMed:12507422}.
REGION 94 105 Interaction with CLF2 and isoform 2.
{ECO:0000269|PubMed:19752190,
ECO:0000269|PubMed:24860983}.
MOTIF 64 69 Nuclear localization signal.
{ECO:0000250|UniProtKB:P50463,
ECO:0000255}.
COMPBIAS 63 78 Gly-rich.
COMPBIAS 177 185 Gly-rich.
MOD_RES 95 95 Phosphoserine.
{ECO:0000250|UniProtKB:P50462}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000250|UniProtKB:P50463}.
VAR_SEQ 38 59 MACRKALDSTTVAAHESEIYCK -> TLAQDLFPLCHLWEE
SGVHKC (in isoform 2).
/FTId=VSP_058575.
VAR_SEQ 60 194 Missing (in isoform 2).
/FTId=VSP_058576.
VARIANT 4 4 W -> R (in CMD1M; unknown pathological
significance; decreases interaction with
TCAP; dbSNP:rs45550635).
{ECO:0000269|PubMed:12507422,
ECO:0000269|PubMed:18505755}.
/FTId=VAR_015401.
VARIANT 44 44 L -> P (in CMH12; decreases PKC/PRKCA
activity; dbSNP:rs104894205).
{ECO:0000269|PubMed:12642359,
ECO:0000269|PubMed:27353086}.
/FTId=VAR_045932.
VARIANT 54 55 SE -> RG (in CMH12; decreases PKC/PRKCA
activity; dbSNP:rs281865416).
{ECO:0000269|PubMed:27353086}.
/FTId=VAR_045933.
VARIANT 58 58 C -> G (in CMH12; decreases interaction
with NRAP and ACTN2, decreases zinc-
binding and impairs protein stability,
decreases PKC/PRKCA activity;
dbSNP:rs104894204).
{ECO:0000269|PubMed:12642359,
ECO:0000269|PubMed:15205937,
ECO:0000269|PubMed:18505755}.
/FTId=VAR_045934.
VARIANT 72 72 G -> R (in CMD1M; unknown pathological
significance; increases PKC/PRKCA
activity; dbSNP:rs45552933).
{ECO:0000269|PubMed:19412328,
ECO:0000269|PubMed:27353086}.
/FTId=VAR_076805.
MUTAGEN 69 69 K->R: Increases PKC/PRKCA activity.
{ECO:0000269|PubMed:27353086}.
CONFLICT 26 26 N -> H (in Ref. 4; AAF28868).
{ECO:0000305}.
STRAND 14 17 {ECO:0000244|PDB:2O10}.
HELIX 19 21 {ECO:0000244|PDB:2O10}.
STRAND 22 25 {ECO:0000244|PDB:2O10}.
STRAND 28 31 {ECO:0000244|PDB:2O10}.
TURN 32 34 {ECO:0000244|PDB:2O10}.
STRAND 38 40 {ECO:0000244|PDB:2O10}.
TURN 46 48 {ECO:0000244|PDB:2O10}.
STRAND 50 52 {ECO:0000244|PDB:2O10}.
STRAND 55 57 {ECO:0000244|PDB:2O10}.
HELIX 59 65 {ECO:0000244|PDB:2O10}.
TURN 121 124 {ECO:0000244|PDB:2O13}.
TURN 129 131 {ECO:0000244|PDB:2O13}.
STRAND 133 135 {ECO:0000244|PDB:2O13}.
STRAND 138 140 {ECO:0000244|PDB:2O13}.
TURN 142 144 {ECO:0000244|PDB:2O13}.
STRAND 145 147 {ECO:0000244|PDB:2O13}.
TURN 148 151 {ECO:0000244|PDB:2O13}.
STRAND 159 162 {ECO:0000244|PDB:2O13}.
STRAND 165 168 {ECO:0000244|PDB:2O13}.
HELIX 169 175 {ECO:0000244|PDB:2O13}.
SEQUENCE 194 AA; 20969 MW; FDB6E4F8D258C35F CRC64;
MPNWGGGAKC GACEKTVYHA EEIQCNGRSF HKTCFHCMAC RKALDSTTVA AHESEIYCKV
CYGRRYGPKG IGYGQGAGCL STDTGEHLGL QFQQSPKPAR SVTTSNPSKF TAKFGESEKC
PRCGKSVYAA EKVMGGGKPW HKTCFRCAIC GKSLESTNVT DKDGELYCKV CYAKNFGPTG
IGFGGLTQQV EKKE


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