MYPC3_CHICK
ID MYPC3_CHICK Reviewed; 1272 AA.
AC Q90688; Q90907;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 772-777.
RC TISSUE=Embryonic heart, and Embryonic skeletal muscle;
RX PubMed=8576942; DOI=10.1016/s0022-2828(95)91731-4;
RA Yasuda M., Koshida S., Sato N., Obinata T.;
RT "Complete primary structure of chicken cardiac C-protein (MyBP-C) and its
RT expression in developing striated muscles.";
RL J. Mol. Cell. Cardiol. 27:2275-2286(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mohamed A.S., Dignam J.D., Schlender K.K.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE, AND
RP PHOSPHORYLATION AT SER-265; THR-274; SER-300 AND SER-1169.
RC TISSUE=Heart;
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).
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. May be involved in the early phase of
CC myofibrillogenesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Type I;
CC IsoId=Q90688-1; Sequence=Displayed;
CC Name=Type II;
CC IsoId=Q90688-2; Sequence=VSP_002546;
CC -!- TISSUE SPECIFICITY: Expressed specifically in cardiac muscle among
CC adult tissues, but is also expressed transiently in the skeletal muscle
CC at early developmental stages. Isoform Type I is found in embryonic
CC skeletal muscle and isoform Type II is found in both embryonic skeletal
CC and cardiac muscle.
CC -!- PTM: Substrate for phosphorylation by PKA and PKC. Reversible
CC phosphorylation appears to modulate contraction.
CC {ECO:0000269|PubMed:9784245}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
CC {ECO:0000305}.
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DR EMBL; D43697; BAA07799.1; -; mRNA.
DR EMBL; U38949; AAA92617.1; -; mRNA.
DR AlphaFoldDB; Q90688; -.
DR STRING; 9031.ENSGALP00000032013; -.
DR iPTMnet; Q90688; -.
DR PaxDb; Q90688; -.
DR PRIDE; Q90688; -.
DR VEuPathDB; HostDB:geneid_396013; -.
DR eggNOG; ENOG502QWRQ; Eukaryota.
DR InParanoid; Q90688; -.
DR OrthoDB; 67092at2759; -.
DR PhylomeDB; Q90688; -.
DR PRO; PR:Q90688; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0001671; F:ATPase activator activity; IDA:BHF-UCL.
DR GO; GO:0032036; F:myosin heavy chain binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:BHF-UCL.
DR GO; GO:0032971; P:regulation of muscle filament sliding; IDA:BHF-UCL.
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; 6.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell adhesion;
KW Direct protein sequencing; Immunoglobulin domain; Muscle protein;
KW Phosphoprotein; Reference proteome; Repeat; Thick filament.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..1272
FT /note="Myosin-binding protein C, cardiac-type"
FT /id="PRO_0000072696"
FT DOMAIN 137..252
FT /note="Ig-like C2-type 1"
FT DOMAIN 359..451
FT /note="Ig-like C2-type 2"
FT DOMAIN 452..542
FT /note="Ig-like C2-type 3"
FT DOMAIN 543..640
FT /note="Ig-like C2-type 4"
FT DOMAIN 644..763
FT /note="Ig-like C2-type 5"
FT DOMAIN 772..868
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 870..965
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 969..1057
FT /note="Ig-like C2-type 6"
FT DOMAIN 1066..1161
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1179..1263
FT /note="Ig-like C2-type 7"
FT REGION 95..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 265
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000269|PubMed:9784245"
FT MOD_RES 274
FT /note="Phosphothreonine; by PKA and PKC"
FT /evidence="ECO:0000269|PubMed:9784245"
FT MOD_RES 300
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:9784245"
FT MOD_RES 1169
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:9784245"
FT VAR_SEQ 265..279
FT /note="Missing (in isoform Type II)"
FT /evidence="ECO:0000305"
FT /id="VSP_002546"
FT CONFLICT 110
FT /note="Missing (in Ref. 1; BAA07799)"
FT /evidence="ECO:0000305"
FT CONFLICT 681..683
FT /note="IWQ -> SGR (in Ref. 1; BAA07799)"
FT /evidence="ECO:0000305"
FT CONFLICT 1244
FT /note="L -> F (in Ref. 1; BAA07799)"
FT /evidence="ECO:0000305"
SQ 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
