ID   MYPC1_RAT               Reviewed;         621 AA.
AC   Q63518;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Myosin-binding protein C, slow-type;
DE            Short=Slow MyBP-C;
DE   AltName: Full=C-protein, skeletal muscle slow isoform;
DE   Flags: Fragment;
GN   Name=Mybpc1;
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 [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
RX   PubMed=7673161; DOI=10.1074/jbc.270.36.21264;
RA   Akopian A.N., Wood N.;
RT   "Peripheral nervous system-specific genes identified by subtractive cDNA
RT   cloning.";
RL   J. Biol. Chem. 270:21264-21270(1995).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28; SER-233; THR-420 AND
RP   TYR-445, AND IDENTIFICATION BY MASS SPECTROMETRY [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. Slow skeletal protein
CC       that binds to both myosin and actin. In vitro, binds to native thin
CC       filaments and modifies the activity of actin-activated myosin ATPase.
CC       May modulate muscle contraction or may play a more structural role.
CC       {ECO:0000250|UniProtKB:Q00872}.
CC   -!- SUBUNIT: Interacts with USP25 (isoform USP25m only); the interaction
CC       prevents proteasomal degradation of MYBPC1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
CC       {ECO:0000305}.
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DR   EMBL; X90475; CAA62085.1; -; mRNA.
DR   PIR; B57431; B57431.
DR   RefSeq; NP_001094228.2; NM_001100758.2.
DR   AlphaFoldDB; Q63518; -.
DR   SMR; Q63518; -.
DR   IntAct; Q63518; 1.
DR   STRING; 10116.ENSRNOP00000035289; -.
DR   iPTMnet; Q63518; -.
DR   GeneID; 362867; -.
DR   KEGG; rno:362867; -.
DR   UCSC; RGD:735102; rat.
DR   CTD; 4604; -.
DR   RGD; 735102; Mybpc1.
DR   eggNOG; ENOG502QPYI; Eukaryota.
DR   InParanoid; Q63518; -.
DR   OrthoDB; 67092at2759; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0017022; F:myosin binding; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006936; P:muscle contraction; ISO:RGD.
DR   CDD; cd00063; FN3; 3.
DR   Gene3D; 2.60.40.10; -; 7.
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   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 3.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00409; IG; 3.
DR   SUPFAM; SSF48726; SSF48726; 4.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   Actin-binding; Cell adhesion; Immunoglobulin domain; Muscle protein;
KW   Phosphoprotein; Reference proteome; Repeat; Thick filament.
FT   CHAIN           <1..>621
FT                   /note="Myosin-binding protein C, slow-type"
FT                   /id="PRO_0000072690"
FT   DOMAIN          <1..53
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          54..142
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          144..241
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          244..343
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          344..459
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          459..553
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          556..621
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   MOD_RES         28
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         420
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         445
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   NON_TER         1
FT   NON_TER         621
SQ   SEQUENCE   621 AA;  68737 MW;  07B68B1FB8793FEA CRC64;
     EEIVPGPKSR YRIKVEGKKH TLIIEGATKA DSAEYSVMTT GGQSSAKLSV DLRPLKITTP
     LTDQTVKLGK EVCLKCEISE NVPGKWTKNG LPVQEGERLK VVHKGRIHKL VIANALIEDE
     GEYVFTPDAI TVPLVCQIHV IDPPKIILDG LEADNTVTVI AGSKLRLEIP VTGEPPPKAI
     WSRADKAIME GSGRIRAESY PDSSTLVIDV AERDDSGVYN INLKNEAGEA HASIKLRLWI
     SLILRLAPNV TEVGDDWCIM NWEPPVYDGG SPILGYFIER KKKQSSRWMR LNFDLCKETT
     FEPKKMIEGV AYEVRIFAVN AIGISKPSMP SKPFVPLAVT SPPTLLAVDS VTDSSVTMKW
     RPPDQIGAAG LSGYVLEYCF EGSTSAKQSN ENGEAANDLP AEDWSLQTQT GSTRPKFTIT
     GLPTDAKIFV RVKAINAAGA SETKYYSQPI LVKEIIEPPK IRIPRHLKQT YIRRVGEAVN
     LVIPFQGKPR PELTWKKDGA EIDKNQINIR NSETDTIIFI RKAERSHSGK YDLEVKVDKY
     VENASIDIQI VDRPGPPQAV TIEDVWGENV ALTWTPPKDD GNAAITGYTI QKADKKSMEW
     FAVIEHYHRT NATITELVIG N