MYPC_RAT
ID MYPC_RAT Reviewed; 1274 AA.
AC P56741;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 115.
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 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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 276-310.
RC TISSUE=Heart muscle;
RX PubMed=9784245; DOI=10.1006/abbi.1998.0857;
RA Mohamed A.S., Dignam J.D., Schlender K.K.;
RT "Cardiac myosin-binding protein C (MyBP-C): identification of protein
RT kinase A and protein kinase C phosphorylation sites.";
RL Arch. Biochem. Biophys. 358:313-319(1998).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-117; SER-279; SER-288;
RP SER-312; SER-459 AND THR-607, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- PTM: Substrate for phosphorylation by PKA and PKC. Reversible
CC phosphorylation appears to modulate contraction.
CC -!- PTM: Polyubiquitinated. {ECO:0000250|UniProtKB:Q14896}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
CC {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; CH473949; EDL79508.1; -; Genomic_DNA.
DR RefSeq; NP_001099960.1; NM_001106490.1.
DR AlphaFoldDB; P56741; -.
DR SMR; P56741; -.
DR BioGRID; 255188; 2.
DR STRING; 10116.ENSRNOP00000016652; -.
DR CarbonylDB; P56741; -.
DR iPTMnet; P56741; -.
DR PhosphoSitePlus; P56741; -.
DR PaxDb; P56741; -.
DR PRIDE; P56741; -.
DR GeneID; 295929; -.
DR KEGG; rno:295929; -.
DR UCSC; RGD:1305950; rat.
DR CTD; 4607; -.
DR RGD; 1305950; Mybpc3.
DR VEuPathDB; HostDB:ENSRNOG00000012307; -.
DR eggNOG; ENOG502QWRQ; Eukaryota.
DR HOGENOM; CLU_006405_1_1_1; -.
DR InParanoid; P56741; -.
DR OMA; DKLHFRI; -.
DR OrthoDB; 67092at2759; -.
DR PhylomeDB; P56741; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR PRO; PR:P56741; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000012307; Expressed in heart and 12 other tissues.
DR Genevisible; P56741; RN.
DR GO; GO:0031672; C:A band; ISO:RGD.
DR GO; GO:0097512; C:cardiac myofibril; ISO:RGD.
DR GO; GO:0030016; C:myofibril; ISO:RGD.
DR GO; GO:0030017; C:sarcomere; ISO:RGD.
DR GO; GO:0005863; C:striated muscle myosin thick filament; IDA:BHF-UCL.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017022; F:myosin binding; ISO:RGD.
DR GO; GO:0032036; F:myosin heavy chain binding; ISO:RGD.
DR GO; GO:0008307; F:structural constituent of muscle; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; IEP:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
DR GO; GO:0006936; P:muscle contraction; ISO:RGD.
DR GO; GO:0031034; P:myosin filament assembly; ISO:RGD.
DR GO; GO:0008016; P:regulation of heart contraction; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0006942; P:regulation of striated muscle contraction; IEP:BHF-UCL.
DR GO; GO:0045214; P:sarcomere organization; ISO:RGD.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:RGD.
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; 5.
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 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..1274
FT /note="Myosin-binding protein C, cardiac-type"
FT /id="PRO_0000072695"
FT DOMAIN 8..95
FT /note="Ig-like C2-type 1"
FT DOMAIN 157..259
FT /note="Ig-like C2-type 2"
FT DOMAIN 361..452
FT /note="Ig-like C2-type 3"
FT DOMAIN 452..546
FT /note="Ig-like C2-type 4"
FT DOMAIN 645..765
FT /note="Ig-like C2-type 5"
FT DOMAIN 774..870
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 872..967
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 971..1059
FT /note="Ig-like C2-type 6"
FT DOMAIN 1068..1163
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1181..1269
FT /note="Ig-like C2-type 7"
FT REGION 95..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O70468"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70468"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 287
FT /note="Phosphothreonine; by PKA and PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 307
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O70468"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70468"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70468"
FT MOD_RES 607
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1241
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O70468"
FT DISULFID 436..443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 306
FT /note="S -> RD (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1274 AA; 140762 MW; 6669E4F41B52B9E3 CRC64;
MPEPGKRPVS AFTKKPRSVE VTAGSAAVFE AETERSGLKV QWQRDGSDIA ANDKYGLAAE
GKRHTLTVRD VGPDDQGSYA VIAGSSKVKF DLKVTEPAPP EKAESAVAPT SMEAPETPKE
VPALATQLEG NVSSPEGSVS VTQDGSVAGS QGAPDDPIGL FLMRPQDGEV TVGGSIVFSA
RVAGASLLKP PVVKWFKGKW VDLSSKVGQH LQLHDSYDRA SKVYLFELHI TDAQATSAGG
YRCEVSTKDK FDSCNFNLTV HEAIGSGDLD LRSAFRRTSL AGTGRRTSDS HEDAGTLDFS
SLLKKSSFRR DSKLEAPAEE DVWEILRQAP PSEYERIAFQ HGVTDLRGML KRLKGMKHDE
KKSTAFQKKL EPAYQVNKGH KIRLTVELAD PDAEVKWLKN GQEIQMSGRY IFESIGAKRT
LTISQCSLAD DAAYQCVVGG EKCSTELFVK EPPVLITRSL EDQLVMVGQR VEFECEVSEE
GAQVKWLKDG VELTREETFK YRFKKDGRKH HLIINEATLE DAGHYAVRTS GGQALAELIV
QEKKLEVYQS IADLAVGAKD QAVFKCEVSD ENVRGVWLKN GKELVPDNRI KVSHIGRVHK
LTIDDVTPAD EADYSFVPEG FACNLSAKLH FMEVKIDFVP RQEPPKIHLD CPGSTPDTIV
VVAGNKLRLD VPISGDPAPT VIWQKTITQG KKASAGPPPG APEDAGADEE WVFDKKLLCE
TEGRVRVETT KDRSVFTVEG AEKEDEGVYT VTVKNPVGED QVNLTVKVID VPDAPAAPKI
SNVGEDSCIV QWEPPAYDGG QPVLGYILER KKKKSYRWMR LNFDLLRELS HEARRMIEGV
AYEMRVYAVN AVGMSRPSPA SQPFMPIGPP GEPTHLTVED VSDTTVSLKW RPPERVGAGG
LDGYSVEYCQ EGCSEWVTAL QGLTERTSLL VKDLPTGARL LFRVRAHNVA GPGGPIITKE
PVTVQEILQR PRLQLPRHLR QTIQKKVGEP VNLLIPFQGK PRPQVTWTKE GQPLAGEEVS
IRNSPTDTIL FIRAAHRTHS GTYQVTVRIE NMEDKATLVL QIVDKPSPPL DIRVVETWGF
SVALEWKPPQ DDGNTEIWGY TVQKADKKTM EWFTVLEHYR QTHCVVSELI IGNGYYFRVF
SHNMVGSSDR AAATKEPIFI PRPGITYEPP KYKALDFSEA PSFTQPLTNR SIIAGYNAIL
CCAVRGSPKP KISWFKNGLD LGEDARFRMF CKQGVLTLEI RKPCPYDGGV YVCRATNLQG
EAQCECRLEV RVPQ
