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   29-MAY-2024, entry version 135.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT   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 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 myosin-
RT   binding protein C, fast-type homolog.";
RL   Submitted (JAN-2006) to the PDB data bank.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
CC       {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   PDB; 1X5Y; NMR; -; A=731-828.
DR   PDB; 2DLT; NMR; -; A=433-525.
DR   PDBsum; 1X5Y; -.
DR   PDBsum; 2DLT; -.
DR   AlphaFoldDB; Q5XKE0; -.
DR   SMR; Q5XKE0; -.
DR   BioGRID; 231385; 6.
DR   IntAct; Q5XKE0; 1.
DR   MINT; Q5XKE0; -.
DR   STRING; 10090.ENSMUSP00000130127; -.
DR   CarbonylDB; Q5XKE0; -.
DR   iPTMnet; Q5XKE0; -.
DR   PhosphoSitePlus; Q5XKE0; -.
DR   MaxQB; Q5XKE0; -.
DR   PaxDb; 10090-ENSMUSP00000130127; -.
DR   PeptideAtlas; Q5XKE0; -.
DR   ProteomicsDB; 287597; -.
DR   Antibodypedia; 32323; 197 antibodies from 32 providers.
DR   DNASU; 233199; -.
DR   Ensembl; ENSMUST00000165208.4; ENSMUSP00000130127.3; ENSMUSG00000038670.12.
DR   GeneID; 233199; -.
DR   KEGG; mmu:233199; -.
DR   UCSC; uc009gpv.2; mouse.
DR   AGR; MGI:1336170; -.
DR   CTD; 4606; -.
DR   MGI; MGI:1336170; Mybpc2.
DR   VEuPathDB; HostDB:ENSMUSG00000038670; -.
DR   eggNOG; ENOG502QW17; Eukaryota.
DR   GeneTree; ENSGT00940000160092; -.
DR   HOGENOM; CLU_006405_1_1_1; -.
DR   InParanoid; Q5XKE0; -.
DR   OMA; KNTACIL; -.
DR   OrthoDB; 4232090at2759; -.
DR   PhylomeDB; Q5XKE0; -.
DR   TreeFam; TF351819; -.
DR   Reactome; R-MMU-390522; Striated Muscle Contraction.
DR   BioGRID-ORCS; 233199; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Mybpc2; mouse.
DR   EvolutionaryTrace; Q5XKE0; -.
DR   PRO; PR:Q5XKE0; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q5XKE0; Protein.
DR   Bgee; ENSMUSG00000038670; Expressed in triceps brachii and 74 other cell types or tissues.
DR   ExpressionAtlas; Q5XKE0; baseline and differential.
DR   GO; GO:0005856; C:cytoskeleton; TAS:MGI.
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; TAS:MGI.
DR   GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd05894; Ig_C5_MyBP-C; 1.
DR   CDD; cd05748; Ig_Titin_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 10.
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   PANTHER; PTHR13817:SF17; MYOSIN-BINDING PROTEIN C, FAST-TYPE; 1.
DR   PANTHER; PTHR13817; TITIN; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 7.
DR   Pfam; PF18362; THB; 1.
DR   PRINTS; PR00014; FNTYPEIII.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00409; IG; 7.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 7.
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; Reference proteome; Repeat; Thick filament.
FT   CHAIN           1..1136
FT                   /note="Myosin-binding protein C, fast-type"
FT                   /id="PRO_0000253051"
FT   DOMAIN          46..149
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          250..339
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          340..432
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          433..533
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          534..633
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          636..732
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          734..829
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          833..927
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          930..1025
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1043..1136
FT                   /note="Ig-like C2-type 7"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        619
FT                   /note="V -> A (in Ref. 2; AAH29762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        648
FT                   /note="D -> N (in Ref. 1; BAC26371)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        900
FT                   /note="S -> T (in Ref. 1; BAC26371)"
FT                   /evidence="ECO:0000305"
FT   STRAND          436..438
FT                   /evidence="ECO:0007829|PDB:2DLT"
FT   STRAND          443..448
FT                   /evidence="ECO:0007829|PDB:2DLT"
FT   STRAND          456..458
FT                   /evidence="ECO:0007829|PDB:2DLT"
FT   STRAND          463..470
FT                   /evidence="ECO:0007829|PDB:2DLT"
FT   STRAND          480..484
FT                   /evidence="ECO:0007829|PDB:2DLT"
FT   STRAND          487..494
FT                   /evidence="ECO:0007829|PDB:2DLT"
FT   TURN            497..499
FT                   /evidence="ECO:0007829|PDB:2DLT"
FT   STRAND          503..508
FT                   /evidence="ECO:0007829|PDB:2DLT"
FT   STRAND          518..521
FT                   /evidence="ECO:0007829|PDB:2DLT"
FT   STRAND          736..743
FT                   /evidence="ECO:0007829|PDB:1X5Y"
FT   STRAND          745..753
FT                   /evidence="ECO:0007829|PDB:1X5Y"
FT   STRAND          765..772
FT                   /evidence="ECO:0007829|PDB:1X5Y"
FT   STRAND          779..784
FT                   /evidence="ECO:0007829|PDB:1X5Y"
FT   STRAND          786..794
FT                   /evidence="ECO:0007829|PDB:1X5Y"
FT   STRAND          802..810
FT                   /evidence="ECO:0007829|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
//