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

 MYPC3_CHICK             Reviewed;        1272 AA.
Q90688; Q90907;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 122.
RecName: Full=Myosin-binding protein C, cardiac-type;
Short=Cardiac MyBP-C;
AltName: Full=C-protein, cardiac muscle isoform;
Name=MYBPC3;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 772-777.
TISSUE=Embryonic heart, and Embryonic skeletal muscle;
PubMed=8576942; DOI=10.1016/S0022-2828(95)91731-4;
Yasuda M., Koshida S., Sato N., Obinata T.;
"Complete primary structure of chicken cardiac C-protein (MyBP-C) and
its expression in developing striated muscles.";
J. Mol. Cell. Cardiol. 27:2275-2286(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Mohamed A.S., Dignam J.D., Schlender K.K.;
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE, AND
PHOSPHORYLATION AT SER-265; THR-274; SER-300 AND SER-1169.
TISSUE=Heart;
PubMed=9784245; DOI=10.1006/abbi.1998.0857;
Mohamed A.S., Dignam J.D., Schlender K.K.;
"Cardiac myosin-binding protein C (MyBP-C): identification of protein
kinase A and protein kinase C phosphorylation sites.";
Arch. Biochem. Biophys. 358:313-319(1998).
-!- 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. May be involved in
the early phase of myofibrillogenesis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Type I;
IsoId=Q90688-1; Sequence=Displayed;
Name=Type II;
IsoId=Q90688-2; Sequence=VSP_002546;
-!- TISSUE SPECIFICITY: Expressed specifically in cardiac muscle among
adult tissues, but is also expressed transiently in the skeletal
muscle at early developmental stages. Isoform Type I is found in
embryonic skeletal muscle and isoform Type II is found in both
embryonic skeletal and cardiac muscle.
-!- PTM: Substrate for phosphorylation by PKA and PKC. Reversible
phosphorylation appears to modulate contraction.
{ECO:0000269|PubMed:9784245}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP
family. {ECO:0000305}.
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EMBL; D43697; BAA07799.1; -; mRNA.
EMBL; U38949; AAA92617.1; -; mRNA.
UniGene; Gga.39829; -.
ProteinModelPortal; Q90688; -.
SMR; Q90688; -.
STRING; 9031.ENSGALP00000032013; -.
iPTMnet; Q90688; -.
PaxDb; Q90688; -.
PRIDE; Q90688; -.
eggNOG; ENOG410IFCI; Eukaryota.
eggNOG; ENOG4110AYI; LUCA.
HOGENOM; HOG000220906; -.
HOVERGEN; HBG052560; -.
InParanoid; Q90688; -.
PhylomeDB; Q90688; -.
PRO; PR:Q90688; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0031430; C:M band; IBA:GO_Central.
GO; GO:0005859; C:muscle myosin complex; IBA:GO_Central.
GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
GO; GO:0030018; C:Z disc; IBA:GO_Central.
GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
GO; GO:0001671; F:ATPase activator activity; IDA:BHF-UCL.
GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
GO; GO:0008307; F:structural constituent of muscle; IBA:GO_Central.
GO; GO:0097493; F:structural molecule activity conferring elasticity; IBA:GO_Central.
GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:BHF-UCL.
GO; GO:0032971; P:regulation of muscle filament sliding; IDA:BHF-UCL.
GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
GO; GO:0006941; P:striated muscle contraction; IBA:GO_Central.
GO; GO:0071688; P:striated muscle myosin thick filament assembly; IBA:GO_Central.
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; 5.
SUPFAM; SSF48726; SSF48726; 8.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 3.
PROSITE; PS50835; IG_LIKE; 6.
1: Evidence at protein level;
Actin-binding; Alternative splicing; Cell adhesion; Complete proteome;
Direct protein sequencing; Immunoglobulin domain; Muscle protein;
Phosphoprotein; Reference proteome; Repeat; Thick filament.
INIT_MET 1 1 Removed.
CHAIN 2 1272 Myosin-binding protein C, cardiac-type.
/FTId=PRO_0000072696.
DOMAIN 137 252 Ig-like C2-type 1.
DOMAIN 359 451 Ig-like C2-type 2.
DOMAIN 452 542 Ig-like C2-type 3.
DOMAIN 543 640 Ig-like C2-type 4.
DOMAIN 644 763 Ig-like C2-type 5.
DOMAIN 772 868 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 870 965 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 969 1057 Ig-like C2-type 6.
DOMAIN 1066 1161 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1179 1263 Ig-like C2-type 7.
COMPBIAS 97 142 Pro-rich.
MOD_RES 265 265 Phosphoserine; by PKA and PKC.
{ECO:0000269|PubMed:9784245}.
MOD_RES 274 274 Phosphothreonine; by PKA and PKC.
{ECO:0000269|PubMed:9784245}.
MOD_RES 300 300 Phosphoserine; by PKA.
{ECO:0000269|PubMed:9784245}.
MOD_RES 1169 1169 Phosphoserine; by PKC.
{ECO:0000269|PubMed:9784245}.
VAR_SEQ 265 279 Missing (in isoform Type II).
{ECO:0000305}.
/FTId=VSP_002546.
CONFLICT 110 110 Missing (in Ref. 1; BAA07799).
{ECO:0000305}.
CONFLICT 681 683 IWQ -> SGR (in Ref. 1; BAA07799).
{ECO:0000305}.
CONFLICT 1244 1244 L -> F (in Ref. 1; BAA07799).
{ECO:0000305}.
SEQUENCE 1272 AA; 142288 MW; 14DD2912518A025E CRC64;
MPEPAKKAVS AFTKKPKTTE VAAGSTAVFE AETEKTGIKV KWQRAGTEIT DSEKYAIKAE
GNKHSLTISN VGKDDEVTYA VIAGTSKVKF ELKVKEPEKS EPVAPAEASP APAASELPAP
PVESNQNPEV PPAETQPEEP VDPIGLFVTR PQDGEVTVGG NITFTAKVAG ESLLKKPSVK
WFKGKWMDLA SKVGKHLQLH DNYDRNNKVY TFEMEIIEAN MTFAGGYRCE VSTKDKFDSS
NFNLIVNEAP VSGEMDIRAA FRRTSLAGGG RRMTSAFLST EGLEESGELN FSALLKKRDS
FLRTANRGDG KSDSQPDVDV WEILRKAPPS EYEKIAFQYG ITDLRGMLKR LKRIKKEEKK
STAFLKKLDP AYQVDKGQKI KLMVEVANPD ADVKWLKNGQ EIQVSGSKYI FEAIGNKRIL
TINHCSLADD AAYECVVAEE KSFTELFVKE PPILITHPLE DQMVMVGERV EFECEVSEEG
ATVKWEKDGV ELTREETFKY RFKKDGKKQY LIINESTKED SGHYTVKTNG GVSVAELIVQ
EKKLEVYQSI ADLTVKARDQ AVFKCEVSDE NVKGIWLKNG KEVVPDERIK ISHIGRIHKL
TIEDVTPGDE ADYSFIPQGF AYNLSAKLQF LEVKIDFVPR EEPPKIHLDC LGQSPDTIVV
VAGNKLRLDV PISGDPTPTV IWQKVNKKGE LVHQSNEDSL TPSENSSDLS TDSKLLFESE
GRVRVEKHED HCVFIIEGAE KEDEGVYRVI VKNPVGEDKA DITVKVIDVP DPPEAPKISN
IGEDYCTVQW QPPTYDGGQP VLGYILERKK KKSYRWMRLN FDLLKELTYE AKRMIEGVVY
EMRIYAVNSI GMSRPSPASQ PFMPIAPPSE PTHFTVEDVS DTTVALKWRP PERIGAGGLD
GYIVEYCKDG SAEWTPALPG LTERTSALIK DLVTGDKLYF RVKAINLAGE SGAAIIKEPV
TVQEIMQRPK ICVPRHLRQT LVKKVGETIN IMIPFQGKPR PKISWMKDGQ TLDSKDVGIR
NSSTDTILFI RKAELHHSGA YEVTLQIENM TDTVAITIQI IDKPGPPQNI KLADVWGFNV
ALEWTPPQDD GNAQILGYTV QKADKKTMEW YTVYDHYRRT NCVVSDLIMG NEYFFRVFSE
NLCGLSETAA TTKNPAYIQK TGTTYKPPSY KEHDFSEPPK FTHPLVNRSV IAGYNTTLSC
AVRGIPKPKI FWYKNKVDLS GDAKYRMFSK QGVLTLEIRK PTPLDGGFYT CKAVNERGEA
EIECRLDVRV PQ


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