MYPC3_MOUSE
ID MYPC3_MOUSE Reviewed; 1270 AA.
AC O70468; O88997;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Myosin-binding protein C, cardiac-type;
DE Short=Cardiac MyBP-C;
DE AltName: Full=C-protein, cardiac muscle isoform;
GN Name=Mybpc3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/NJ; TISSUE=Heart muscle;
RX PubMed=10532952; DOI=10.1161/01.res.85.9.841;
RA Yang Q., Sanbe A., Osinska H., Hewett T.E., Klevitsky R., Robbins J.;
RT "In vivo modeling of myosin binding protein C familial hypertrophic
RT cardiomyopathy.";
RL Circ. Res. 85:841-847(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart muscle;
RA McDonald K.S., Hollander M.S., Moss R.L.;
RT "Sequence of the cardiac isoform of murine myosin binding protein-C (MyBP-
RT C) cDNA.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP ACETYLATION AT MET-1, AND PHOSPHORYLATION AT SER-273; SER-282 AND SER-302.
RX PubMed=19541641; DOI=10.1073/pnas.0813369106;
RA Ge Y., Rybakova I.N., Xu Q., Moss R.L.;
RT "Top-down high-resolution mass spectrometry of cardiac myosin binding
RT protein C revealed that truncation alters protein phosphorylation state.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:12658-12663(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-72; SER-307; SER-423;
RP SER-455 AND SER-546, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1237, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Thick filament-associated protein located in the crossbridge
CC region of vertebrate striated muscle a bands. In vitro it binds MHC, F-
CC actin and native thin filaments, and modifies the activity of actin-
CC activated myosin ATPase. It may modulate muscle contraction or may play
CC a more structural role.
CC -!- INTERACTION:
CC O70468; P68033: Actc1; NbExp=3; IntAct=EBI-8347074, EBI-352284;
CC O70468; Q02566: Myh6; NbExp=5; IntAct=EBI-8347074, EBI-299157;
CC O70468; P68135: ACTA1; Xeno; NbExp=2; IntAct=EBI-8347074, EBI-367540;
CC -!- PTM: Substrate for phosphorylation by PKA and PKC. Reversible
CC phosphorylation appears to modulate contraction (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Polyubiquitinated. {ECO:0000250|UniProtKB:Q14896}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
CC {ECO:0000305}.
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DR EMBL; AF059576; AAC14570.1; -; mRNA.
DR EMBL; AF097333; AAC64202.1; -; mRNA.
DR PDB; 4EDQ; X-ray; 1.64 A; A/B=149-269.
DR PDBsum; 4EDQ; -.
DR AlphaFoldDB; O70468; -.
DR SMR; O70468; -.
DR DIP; DIP-48624N; -.
DR IntAct; O70468; 34.
DR STRING; 10090.ENSMUSP00000127070; -.
DR iPTMnet; O70468; -.
DR PhosphoSitePlus; O70468; -.
DR jPOST; O70468; -.
DR MaxQB; O70468; -.
DR PaxDb; O70468; -.
DR PeptideAtlas; O70468; -.
DR PRIDE; O70468; -.
DR ProteomicsDB; 287598; -.
DR MGI; MGI:102844; Mybpc3.
DR eggNOG; ENOG502QWRQ; Eukaryota.
DR InParanoid; O70468; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR ChiTaRS; Mybpc3; mouse.
DR PRO; PR:O70468; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70468; protein.
DR GO; GO:0031672; C:A band; IDA:MGI.
DR GO; GO:0097512; C:cardiac myofibril; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; TAS:MGI.
DR GO; GO:0030016; C:myofibril; IDA:MGI.
DR GO; GO:0030017; C:sarcomere; IDA:MGI.
DR GO; GO:0005863; C:striated muscle myosin thick filament; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017022; F:myosin binding; ISO:MGI.
DR GO; GO:0032036; F:myosin heavy chain binding; IPI:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:MGI.
DR GO; GO:0008307; F:structural constituent of muscle; ISO:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0006936; P:muscle contraction; TAS:MGI.
DR GO; GO:0031034; P:myosin filament assembly; IMP:MGI.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR GO; GO:0045214; P:sarcomere organization; IMP:MGI.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:MGI.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 11.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR040849; MyBP-C_THB.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 8.
DR Pfam; PF18362; THB; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 8.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 8.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell adhesion; Disulfide bond;
KW Immunoglobulin domain; Metal-binding; Methylation; Muscle protein;
KW Phosphoprotein; Reference proteome; Repeat; Thick filament;
KW Ubl conjugation; Zinc.
FT CHAIN 1..1270
FT /note="Myosin-binding protein C, cardiac-type"
FT /id="PRO_0000072694"
FT DOMAIN 151..254
FT /note="Ig-like C2-type 1"
FT DOMAIN 358..448
FT /note="Ig-like C2-type 2"
FT DOMAIN 449..539
FT /note="Ig-like C2-type 3"
FT DOMAIN 540..629
FT /note="Ig-like C2-type 4"
FT DOMAIN 641..767
FT /note="Ig-like C2-type 5"
FT DOMAIN 770..866
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 868..963
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 967..1061
FT /note="Ig-like C2-type 6"
FT DOMAIN 1064..1159
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1177..1270
FT /note="Ig-like C2-type 7"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q14896"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q14896"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q14896"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q14896"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:19541641"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 273
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000269|PubMed:19541641"
FT MOD_RES 282
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000269|PubMed:19541641"
FT MOD_RES 302
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000269|PubMed:19541641"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 603
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P56741"
FT MOD_RES 1237
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT DISULFID 432..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 32
FT /note="E -> G (in Ref. 2; AAC64202)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="M -> K (in Ref. 2; AAC64202)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="E -> K (in Ref. 2; AAC64202)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="N -> S (in Ref. 2; AAC64202)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="P -> L (in Ref. 2; AAC64202)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..344
FT /note="EACHRP -> TDLRGM (in Ref. 2; AAC64202)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="T -> A (in Ref. 2; AAC64202)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="A -> T (in Ref. 2; AAC64202)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="E -> G (in Ref. 2; AAC64202)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="R -> T (in Ref. 2; AAC64202)"
FT /evidence="ECO:0000305"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4EDQ"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:4EDQ"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:4EDQ"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4EDQ"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:4EDQ"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:4EDQ"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:4EDQ"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:4EDQ"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:4EDQ"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:4EDQ"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4EDQ"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:4EDQ"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:4EDQ"
SQ 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
