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Myosin-binding protein C, cardiac-type (Cardiac MyBP-C) (C-protein, cardiac muscle isoform)

 MYPC3_MOUSE             Reviewed;        1270 AA.
O70468; O88997;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
12-SEP-2018, entry version 128.
RecName: Full=Myosin-binding protein C, cardiac-type;
Short=Cardiac MyBP-C;
AltName: Full=C-protein, cardiac muscle isoform;
Name=Mybpc3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=FVB/NJ; TISSUE=Heart muscle;
PubMed=10532952; DOI=10.1161/01.RES.85.9.841;
Yang Q., Sanbe A., Osinska H., Hewett T.E., Klevitsky R., Robbins J.;
"In vivo modeling of myosin binding protein C familial hypertrophic
cardiomyopathy.";
Circ. Res. 85:841-847(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart muscle;
McDonald K.S., Hollander M.S., Moss R.L.;
"Sequence of the cardiac isoform of murine myosin binding protein-C
(MyBP-C) cDNA.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[3]
ACETYLATION AT MET-1, AND PHOSPHORYLATION AT SER-273; SER-282 AND
SER-302.
PubMed=19541641; DOI=10.1073/pnas.0813369106;
Ge Y., Rybakova I.N., Xu Q., Moss R.L.;
"Top-down high-resolution mass spectrometry of cardiac myosin binding
protein C revealed that truncation alters protein phosphorylation
state.";
Proc. Natl. Acad. Sci. U.S.A. 106:12658-12663(2009).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-72; SER-307;
SER-423; SER-455 AND SER-546, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Heart, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1237, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Thick filament-associated protein located in the
crossbridge region of vertebrate striated muscle a bands. In vitro
it binds MHC, F-actin and native thin filaments, and modifies the
activity of actin-activated myosin ATPase. It may modulate muscle
contraction or may play a more structural role.
-!- INTERACTION:
P68135:ACTA1 (xeno); NbExp=2; IntAct=EBI-8347074, EBI-367540;
P68033:Actc1; NbExp=3; IntAct=EBI-8347074, EBI-352284;
Q02566:Myh6; NbExp=5; IntAct=EBI-8347074, EBI-299157;
-!- PTM: Substrate for phosphorylation by PKA and PKC. Reversible
phosphorylation appears to modulate contraction (By similarity).
{ECO:0000250}.
-!- PTM: Polyubiquitinated. {ECO:0000250|UniProtKB:Q14896}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF059576; AAC14570.1; -; mRNA.
EMBL; AF097333; AAC64202.1; -; mRNA.
UniGene; Mm.10728; -.
PDB; 4EDQ; X-ray; 1.64 A; A/B=149-269.
PDBsum; 4EDQ; -.
ProteinModelPortal; O70468; -.
SMR; O70468; -.
DIP; DIP-48624N; -.
IntAct; O70468; 35.
MINT; O70468; -.
STRING; 10090.ENSMUSP00000127070; -.
iPTMnet; O70468; -.
PhosphoSitePlus; O70468; -.
MaxQB; O70468; -.
PaxDb; O70468; -.
PeptideAtlas; O70468; -.
PRIDE; O70468; -.
MGI; MGI:102844; Mybpc3.
eggNOG; ENOG410IFCI; Eukaryota.
eggNOG; ENOG4110AYI; LUCA.
HOVERGEN; HBG052560; -.
InParanoid; O70468; -.
ChiTaRS; Mybpc3; mouse.
PRO; PR:O70468; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_MYBPC3; -.
GO; GO:0031672; C:A band; IDA:MGI.
GO; GO:0097512; C:cardiac myofibril; ISO:MGI.
GO; GO:0005856; C:cytoskeleton; TAS:MGI.
GO; GO:0031430; C:M band; IBA:GO_Central.
GO; GO:0005859; C:muscle myosin complex; IBA:GO_Central.
GO; GO:0030016; C:myofibril; IDA:MGI.
GO; GO:0030017; C:sarcomere; IDA:MGI.
GO; GO:0005863; C:striated muscle myosin thick filament; ISO:MGI.
GO; GO:0030018; C:Z disc; IBA:GO_Central.
GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
GO; GO:0017022; F:myosin binding; ISO:MGI.
GO; GO:0032036; F:myosin heavy chain binding; IPI:MGI.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:MGI.
GO; GO:0008307; F:structural constituent of muscle; ISO:MGI.
GO; GO:0097493; F:structural molecule activity conferring elasticity; IBA:GO_Central.
GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
GO; GO:0060048; P:cardiac muscle contraction; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
GO; GO:0006936; P:muscle contraction; IDA:MGI.
GO; GO:0031034; P:myosin filament assembly; IMP:MGI.
GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
GO; GO:0045214; P:sarcomere organization; IMP:MGI.
GO; GO:0071688; P:striated muscle myosin thick filament assembly; IBA:GO_Central.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:MGI.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 11.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF00041; fn3; 3.
Pfam; PF07679; I-set; 8.
SMART; SM00060; FN3; 3.
SMART; SM00409; IG; 8.
SMART; SM00408; IGc2; 6.
SUPFAM; SSF48726; SSF48726; 9.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 3.
PROSITE; PS50835; IG_LIKE; 7.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Cell adhesion;
Complete proteome; Disulfide bond; Immunoglobulin domain;
Metal-binding; Methylation; Muscle protein; Phosphoprotein;
Reference proteome; Repeat; Thick filament; Ubl conjugation; Zinc.
CHAIN 1 1270 Myosin-binding protein C, cardiac-type.
/FTId=PRO_0000072694.
DOMAIN 151 254 Ig-like C2-type 1.
DOMAIN 358 448 Ig-like C2-type 2.
DOMAIN 449 539 Ig-like C2-type 3.
DOMAIN 540 629 Ig-like C2-type 4.
DOMAIN 641 767 Ig-like C2-type 5.
DOMAIN 770 866 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 868 963 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 967 1061 Ig-like C2-type 6.
DOMAIN 1064 1159 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1177 1270 Ig-like C2-type 7.
COMPBIAS 100 150 Pro-rich.
METAL 206 206 Zinc. {ECO:0000250|UniProtKB:Q14896}.
METAL 208 208 Zinc. {ECO:0000250|UniProtKB:Q14896}.
METAL 221 221 Zinc. {ECO:0000250|UniProtKB:Q14896}.
METAL 223 223 Zinc. {ECO:0000250|UniProtKB:Q14896}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:19541641}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 273 273 Phosphoserine; by PKA and PKC.
{ECO:0000269|PubMed:19541641}.
MOD_RES 282 282 Phosphoserine; by PKA and PKC.
{ECO:0000269|PubMed:19541641}.
MOD_RES 302 302 Phosphoserine; by PKA and PKC.
{ECO:0000269|PubMed:19541641}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 455 455 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 546 546 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 603 603 Phosphothreonine.
{ECO:0000250|UniProtKB:P56741}.
MOD_RES 1237 1237 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
DISULFID 432 439 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CONFLICT 32 32 E -> G (in Ref. 2; AAC64202).
{ECO:0000305}.
CONFLICT 39 39 M -> K (in Ref. 2; AAC64202).
{ECO:0000305}.
CONFLICT 113 113 E -> K (in Ref. 2; AAC64202).
{ECO:0000305}.
CONFLICT 249 249 N -> S (in Ref. 2; AAC64202).
{ECO:0000305}.
CONFLICT 291 291 P -> L (in Ref. 2; AAC64202).
{ECO:0000305}.
CONFLICT 339 344 EACHRP -> TDLRGM (in Ref. 2; AAC64202).
{ECO:0000305}.
CONFLICT 659 659 T -> A (in Ref. 2; AAC64202).
{ECO:0000305}.
CONFLICT 691 691 A -> T (in Ref. 2; AAC64202).
{ECO:0000305}.
CONFLICT 738 738 E -> G (in Ref. 2; AAC64202).
{ECO:0000305}.
CONFLICT 923 923 R -> T (in Ref. 2; AAC64202).
{ECO:0000305}.
STRAND 155 157 {ECO:0000244|PDB:4EDQ}.
STRAND 162 165 {ECO:0000244|PDB:4EDQ}.
STRAND 170 177 {ECO:0000244|PDB:4EDQ}.
STRAND 181 183 {ECO:0000244|PDB:4EDQ}.
STRAND 186 191 {ECO:0000244|PDB:4EDQ}.
TURN 192 194 {ECO:0000244|PDB:4EDQ}.
HELIX 197 200 {ECO:0000244|PDB:4EDQ}.
STRAND 205 212 {ECO:0000244|PDB:4EDQ}.
TURN 213 216 {ECO:0000244|PDB:4EDQ}.
STRAND 217 224 {ECO:0000244|PDB:4EDQ}.
HELIX 229 231 {ECO:0000244|PDB:4EDQ}.
STRAND 233 240 {ECO:0000244|PDB:4EDQ}.
STRAND 245 255 {ECO:0000244|PDB:4EDQ}.
SEQUENCE 1270 AA; 140632 MW; 699947C3C9B58931 CRC64;
MPEPGKKPVS AFNKKPRSAE VTAGSAAVFE AETERSGVMV RWQRDGSDIT ANDKYGLAAE
GKRHTLTVRD ASPDDQGSYA VIAGSSKVKF DLKVTEPAPP EKAESEVAPG APEEVPAPAT
ELEESVSSPE GSVSVTQDGS AAEHQGAPDD PIGLFLMRPQ DGEVTVGGSI VFSARVAGAS
LLKPPVVKWF KGKWVDLSSK VGQHLQLHDS YDRASKVYLF ELHITDAQTT SAGGYRCEVS
TKDKFDSCNF NLTVHEAIGS GDLDLRSAFR RTSLAGAGRR TSDSHEDAGT PDFSSLLKKR
DSFRRDSKLE APAEEDVWEI LRQAPPSEYE RIAFQHGVEA CHRPLKRLKG MKQDEKKSTA
FQKKLEPAYQ VNKGHKIRLT VELADPDAEV KWLKNGQEIQ MSGSKYIFES VGAKRTLTIS
QCSLADDAAY QCVVGGEKCS TELFVKEPPV LITRSLEDQL VMVGQRVEFE CEVSEEGAQV
KWLKDGVELT REETFKYRFK KDGRKHHLII NEATLEDAGH YAVRTSGGQS LAELIVQEKK
LEVYQSIADL AVGAKDQAVF KCEVSDENVR GVWLKNGKEL VPDNRIKVSH IGRVHKLTID
DVTPADEADY SFVPEGFACN LSAKLHFMEV KIDFVPRQEP PKIHLDCPGS TPDTIVVVTG
NKLRLDVPIS GDPAPTVVWQ KTVTQGKKAS AGPHPDAPED AGADEEWVFD KKLLCETEGR
VRVETTKDRS VFTVEGAEKE DEGVYTVTVK NPVGEDQVNL TVKVIDVPDA PAAPKISNVG
EDSCTVQWEP PAYDGGQPVL GYILERKKKK SYRWMRLNFD LLRELSHEAR RMIEGVAYEM
RVYAVNAVGM SRPSPASQPF MPIGPPGEPT HLAVEDVSDT TVSLKWRPPE RVGAGGLDGY
SVEYCQEGCS EWTPALQGLT ERRSMLVKDL PTGARLLFRV RAHNVAGPGG PIVTKEPVTV
QEILQRPRLQ LPRHLRQTIQ KKVGEPVNLL IPFQGKPRPQ VTWTKEGQPL AGEEVSIRNS
PTDTILFIRA ARRTHSGTYQ VTVRIENMED KATLILQIVD KPSPPQDIRI VETWGFNVAL
EWKPPQDDGN TEIWGYTVQK ADKKTMEWFT VLEHYRRTHC VVSELIIGNG YYFRVFSHNM
VGSSDKAAAT KEPVFIPRPG ITYEPPKYKA LDFSEAPSFT QPLANRSIIA GYNAILCCAV
RGSPKPKISW FKNGLDLGED ARFRMFCKQG VLTLEIRKPC PYDGGVYVCR ATNLQGEAQC
ECRLEVRVPQ


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