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   02-NOV-2010, entry version 53.
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; Sciurognathi;
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   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   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP
CC       family.
CC   -!- SIMILARITY: Contains 3 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 7 Ig-like C2-type (immunoglobulin-like)
CC       domains.
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DR   EMBL; AK029282; BAC26371.1; -; mRNA.
DR   EMBL; BC029762; AAH29762.1; -; mRNA.
DR   EMBL; BC039184; AAH39184.1; -; mRNA.
DR   IPI; IPI00169994; -.
DR   RefSeq; NP_666301.2; -.
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   STRING; Q5XKE0; -.
DR   PhosphoSite; Q5XKE0; -.
DR   PRIDE; Q5XKE0; -.
DR   Ensembl; ENSMUST00000064089; ENSMUSP00000067845; ENSMUSG00000038670.
DR   GeneID; 233199; -.
DR   KEGG; mmu:233199; -.
DR   NMPDR; fig|10090.3.peg.16416; -.
DR   UCSC; uc009gpv.1; mouse.
DR   CTD; 233199; -.
DR   MGI; MGI:1336170; Mybpc2.
DR   eggNOG; roNOG06139; -.
DR   HOGENOM; HBG445695; -.
DR   HOVERGEN; HBG052560; -.
DR   InParanoid; Q5XKE0; -.
DR   NextBio; 381603; -.
DR   ArrayExpress; Q5XKE0; -.
DR   Bgee; Q5XKE0; -.
DR   CleanEx; MM_MYBPC2; -.
DR   Genevestigator; Q5XKE0; -.
DR   GermOnline; ENSMUSG00000038670; Mus musculus.
DR   GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006936; P:muscle contraction; IPI:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 10.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 7.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF49265; FN_III-like; 3.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Cell adhesion; Immunoglobulin domain;
KW   Muscle protein; Repeat; 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      634    726       Fibronectin type-III 1.
FT   DOMAIN      731    824       Fibronectin type-III 2.
FT   DOMAIN      833    927       Ig-like C2-type 6.
FT   DOMAIN      927   1020       Fibronectin type-III 3.
FT   DOMAIN     1043   1136       Ig-like C2-type 7.
FT   CONFLICT    619    619       V -> A (in Ref. 2; AAH29762).
FT   CONFLICT    648    648       D -> N (in Ref. 1; BAC26371).
FT   CONFLICT    900    900       S -> T (in Ref. 1; BAC26371).
FT   STRAND      436    438
FT   STRAND      443    448
FT   STRAND      456    458
FT   STRAND      463    470
FT   STRAND      480    484
FT   STRAND      487    494
FT   TURN        497    499
FT   STRAND      503    508
FT   STRAND      518    521
FT   STRAND      736    743
FT   STRAND      745    753
FT   STRAND      765    772
FT   STRAND      779    784
FT   STRAND      786    794
FT   STRAND      802    810
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
//