ID   MYPC2_MOUSE             Reviewed;        1136 AA.
AC   Q5XKE0; Q8C109; Q8K2V0;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   07-NOV-2018, entry version 108.
DE   RecName: Full=Myosin-binding protein C, fast-type;
DE            Short=Fast MyBP-C;
DE   AltName: Full=C-protein, skeletal muscle fast isoform;
GN   Name=Mybpc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, and Heart;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   STRUCTURE BY NMR OF 731-828.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the fibronectin type-III domain of mouse
RT   myosin-binding protein C, fast-type homolog.";
RL   Submitted (JAN-2006) to the PDB data bank.
CC   -!- FUNCTION: Thick filament-associated protein located in the
CC       crossbridge region of vertebrate striated muscle a bands. In vitro
CC       it binds MHC, F-actin and native thin filaments, and modifies the
CC       activity of actin-activated myosin ATPase. It may modulate muscle
CC       contraction or may play a more structural role (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP
CC       family. {ECO:0000305}.
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DR   EMBL; AK029282; BAC26371.1; -; mRNA.
DR   EMBL; BC029762; AAH29762.1; -; mRNA.
DR   EMBL; BC039184; AAH39184.1; -; mRNA.
DR   CCDS; CCDS52233.1; -.
DR   RefSeq; NP_666301.2; NM_146189.3.
DR   UniGene; Mm.358888; -.
DR   PDB; 1X5Y; NMR; -; A=731-828.
DR   PDB; 2DLT; NMR; -; A=433-525.
DR   PDBsum; 1X5Y; -.
DR   PDBsum; 2DLT; -.
DR   ProteinModelPortal; Q5XKE0; -.
DR   SMR; Q5XKE0; -.
DR   BioGrid; 231385; 2.
DR   STRING; 10090.ENSMUSP00000130127; -.
DR   CarbonylDB; Q5XKE0; -.
DR   iPTMnet; Q5XKE0; -.
DR   PhosphoSitePlus; Q5XKE0; -.
DR   MaxQB; Q5XKE0; -.
DR   PaxDb; Q5XKE0; -.
DR   PeptideAtlas; Q5XKE0; -.
DR   PRIDE; Q5XKE0; -.
DR   Ensembl; ENSMUST00000165208; ENSMUSP00000130127; ENSMUSG00000038670.
DR   GeneID; 233199; -.
DR   KEGG; mmu:233199; -.
DR   UCSC; uc009gpv.2; mouse.
DR   CTD; 4606; -.
DR   MGI; MGI:1336170; Mybpc2.
DR   eggNOG; ENOG410IFCI; Eukaryota.
DR   eggNOG; ENOG4110AYI; LUCA.
DR   GeneTree; ENSGT00860000133685; -.
DR   HOGENOM; HOG000220906; -.
DR   HOVERGEN; HBG052560; -.
DR   InParanoid; Q5XKE0; -.
DR   KO; K12558; -.
DR   OMA; KEHDFRT; -.
DR   OrthoDB; EOG091G00ND; -.
DR   PhylomeDB; Q5XKE0; -.
DR   TreeFam; TF351819; -.
DR   Reactome; R-MMU-390522; Striated Muscle Contraction.
DR   EvolutionaryTrace; Q5XKE0; -.
DR   PRO; PR:Q5XKE0; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000038670; Expressed in 79 organ(s), highest expression level in muscle of leg.
DR   CleanEx; MM_MYBPC2; -.
DR   ExpressionAtlas; Q5XKE0; baseline and differential.
DR   Genevisible; Q5XKE0; MM.
DR   GO; GO:0005856; C:cytoskeleton; TAS:MGI.
DR   GO; GO:0031430; C:M band; IBA:GO_Central.
DR   GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR   GO; GO:0030017; C:sarcomere; IBA:GO_Central.
DR   GO; GO:0005865; C:striated muscle thin filament; IBA:GO_Central.
DR   GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:MGI.
DR   GO; GO:0008307; F:structural constituent of muscle; IBA:GO_Central.
DR   GO; GO:0048739; P:cardiac muscle fiber development; IBA:GO_Central.
DR   GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IBA:GO_Central.
DR   GO; GO:0055003; P:cardiac myofibril assembly; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006936; P:muscle contraction; IDA:MGI.
DR   GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR   GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IBA:GO_Central.
DR   GO; GO:0030240; P:skeletal muscle thin filament assembly; IBA:GO_Central.
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   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 7.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00409; IG; 7.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; SSF48726; 7.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Cell adhesion; Complete proteome;
KW   Immunoglobulin domain; Muscle protein; Reference proteome; Repeat;
KW   Thick filament.
FT   CHAIN         1   1136       Myosin-binding protein C, fast-type.
FT                                /FTId=PRO_0000253051.
FT   DOMAIN       46    149       Ig-like C2-type 1.
FT   DOMAIN      250    339       Ig-like C2-type 2.
FT   DOMAIN      340    432       Ig-like C2-type 3.
FT   DOMAIN      433    533       Ig-like C2-type 4.
FT   DOMAIN      534    633       Ig-like C2-type 5.
FT   DOMAIN      636    732       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      734    829       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      833    927       Ig-like C2-type 6.
FT   DOMAIN      930   1025       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1043   1136       Ig-like C2-type 7.
FT   CONFLICT    619    619       V -> A (in Ref. 2; AAH29762).
FT                                {ECO:0000305}.
FT   CONFLICT    648    648       D -> N (in Ref. 1; BAC26371).
FT                                {ECO:0000305}.
FT   CONFLICT    900    900       S -> T (in Ref. 1; BAC26371).
FT                                {ECO:0000305}.
FT   STRAND      436    438       {ECO:0000244|PDB:2DLT}.
FT   STRAND      443    448       {ECO:0000244|PDB:2DLT}.
FT   STRAND      456    458       {ECO:0000244|PDB:2DLT}.
FT   STRAND      463    470       {ECO:0000244|PDB:2DLT}.
FT   STRAND      480    484       {ECO:0000244|PDB:2DLT}.
FT   STRAND      487    494       {ECO:0000244|PDB:2DLT}.
FT   TURN        497    499       {ECO:0000244|PDB:2DLT}.
FT   STRAND      503    508       {ECO:0000244|PDB:2DLT}.
FT   STRAND      518    521       {ECO:0000244|PDB:2DLT}.
FT   STRAND      736    743       {ECO:0000244|PDB:1X5Y}.
FT   STRAND      745    753       {ECO:0000244|PDB:1X5Y}.
FT   STRAND      765    772       {ECO:0000244|PDB:1X5Y}.
FT   STRAND      779    784       {ECO:0000244|PDB:1X5Y}.
FT   STRAND      786    794       {ECO:0000244|PDB:1X5Y}.
FT   STRAND      802    810       {ECO:0000244|PDB:1X5Y}.
SQ   SEQUENCE   1136 AA;  127352 MW;  D79F73721397DE0D CRC64;
     MPEAKPAAKK ASKGKDAPKE APAKQTPEEP PKEAPPEDQS PTAEEPTGIF LKKPDSVSVE
     TGKDAVILAK VNGKELPGKP TIKWFKGKWQ ELGSKSGARF IFKESHDSTS NVYTVELHIG
     KVVLGDRGDY RLEIKAKDVC DSCSFNVDVE APRQDSSGQS LESFKRSGDG KSEDAGELDF
     SGLLKKREVV EEEKKKKKDD DDLGIPPEIW ELLKGAKKSE YEKIAFQYGI TDLRGMLKRL
     KKAKVEVKKS AAFTKKLDPA YQVDRGNKIK LVVEISDPDL PLKWFKNGQE IKPSSKYVFE
     NVGKKRILTI NKCTLADDAA YEVAVQDEKC FTELFVKEPP VLIVTPLEDQ QVFVGDRVEM
     SVEVSEEGAQ VMWMKDGVEM TREDSYKARY RFKKDGKRHI LIYSDVAQED GGRYQVITNG
     GQCEAELIVE EKQLEVLQDI ADLTVKAAEQ AVFKCEVSDE KVTGKWYKNG VEVRPSKRIT
     ISHVGRFHKL VIDDVRPEDE GDYTFVPDGY ALSLSAKLNF LEIKVEYVPK QEPPKIHLDC
     SGKTSDNSIV VVAGNKLRLD VAITGEPPPT ATWLRGDEVF TATEGRTHIE QRPDCSSFVI
     ESAERSDEGR YTIKVTNPVG EDVASIFLRV VDVPDPPEAV RVTSVGEDWA ILVWEPPKYD
     GGQPVTGYLM ERKKKGSQRW MKINFEVFTD TTYESTKMIE GVLYEMRVFA VNAIGVSQPS
     MNTKPFMPIA PTSAPQHLTV EDVTDTTTTL KWRPPDRIGA GGIDGYLVEY CLEGSEEWVP
     ANKEPVERCG FTVKDLPTGA RILFRVVGVN IAGRSEPATL LQPVTIREIV EQPKIRLPRH
     LRQTYIRKVG EALNLVIPFQ GKPRPQVVWT KGGAPLDTSR VNVRTSDFDT VFFVRQAARS
     DSGEYELSVQ IENMKDTATI RIRVVEKAGP AENVMVKEVW GTNALVEWQP PKDDGNSEIT
     GYFVQKADKK TMEWFNVYEH NRHTSCTVSD LIVGNEYYFR IFSENICGLS DSPGVSKNTA
     RILKTGITLK PLEYKEHDFR TAPKFLTPLM DRVVVAGYTA ALNCAVRGHP KPKVVWMKNK
     MEIHEDPKFL ITNYQGILTL NIRRPSPFDA GTYSCRAFNE LGEALAECKL DVRVPQ
//