ID   MYBPH_RAT               Reviewed;         484 AA.
AC   O88599;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Myosin-binding protein H;
DE            Short=MyBP-H;
DE   AltName: Full=H-protein;
GN   Name=Mybph;
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   TISSUE=Skeletal muscle;
RX   PubMed=9868543; DOI=10.1007/bf02976763;
RA   Jung J., Oh J., Lee K.;
RT   "Nucleotide and deduced amino acid sequences of rat myosin binding protein
RT   H (MyBP-H).";
RL   Arch. Pharm. Res. 21:712-717(1998).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2; THR-6 AND THR-26, AND
RP   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: Binds to myosin; probably involved in interaction with thick
CC       myofilaments in the A-band.
CC   -!- TISSUE SPECIFICITY: Skeletal muscle.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
CC       {ECO:0000305}.
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DR   EMBL; AF077338; AAC27526.1; -; mRNA.
DR   RefSeq; NP_114001.1; NM_031813.1.
DR   AlphaFoldDB; O88599; -.
DR   SMR; O88599; -.
DR   STRING; 10116.ENSRNOP00000044331; -.
DR   iPTMnet; O88599; -.
DR   PhosphoSitePlus; O88599; -.
DR   PaxDb; O88599; -.
DR   PRIDE; O88599; -.
DR   GeneID; 83708; -.
DR   KEGG; rno:83708; -.
DR   UCSC; RGD:620287; rat.
DR   CTD; 4608; -.
DR   RGD; 620287; Mybph.
DR   eggNOG; ENOG502QVIQ; Eukaryota.
DR   InParanoid; O88599; -.
DR   OrthoDB; 653839at2759; -.
DR   PhylomeDB; O88599; -.
DR   PRO; PR:O88599; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.40.10; -; 4.
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   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07679; I-set; 2.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   Cell adhesion; Immunoglobulin domain; Muscle protein; Phosphoprotein;
KW   Reference proteome; Repeat; Thick filament.
FT   CHAIN           1..484
FT                   /note="Myosin-binding protein H"
FT                   /id="PRO_0000072700"
FT   DOMAIN          80..175
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          179..267
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          276..371
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          389..479
FT                   /note="Ig-like C2-type 2"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         6
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         26
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   484 AA;  52656 MW;  42875199AAF8A6A0 CRC64;
     MTGKATPEAS VSTSEGTAPE PAKVPTPEPS GQVAASESTG QEQAPEPQKQ PQAQDPAAHE
     APATPATTKP EAPSEDVPSA PLQLTLEDVS HSSLTVSWEP PEDLGSWGSR AMCWSSVREG
     ASEWVPVNPR PVMVTQQTVR NLALGDKFFL RVTAVNSAGA GPPAVLDQPV HIQEITEAPK
     IRVPRHLRQT YIRQVGESVN LQIPFQGKPK PQASWTHNGH ALDSQRVNVR SGDQDSILFI
     RSAQRSDSGR YELTVRLEGL EAKAAIDILV IEKPGPPSSI KLLDVWGCNA ALEWMPPQDT
     GNTELLGYTV QKADKKTGQW FTVLERYHPT TCTVSDLIIG NSYSFRVFSE NLCGLSDLAT
     TTKELAHIHK AAITAKPREF TERDFSEPPS FTQPVADRTS TPGYSTQLFC SVRASPKPKI
     IWMKNKMSIQ GDPKYRAVSE QGVCTLEIRK PSPFDSGVYT CKAINVLGEP AVDCRLEVKA
     SATH