MYPC2_MOUSE
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 03-AUG-2022, entry version 125.
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; Q5XKE0; -.
DR PeptideAtlas; Q5XKE0; -.
DR PRIDE; Q5XKE0; -.
DR ProteomicsDB; 287597; -.
DR Antibodypedia; 32323; 186 antibodies from 32 providers.
DR DNASU; 233199; -.
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 VEuPathDB; HostDB:ENSMUSG00000038670; -.
DR eggNOG; ENOG502QW17; Eukaryota.
DR GeneTree; ENSGT00940000160092; -.
DR HOGENOM; CLU_006405_1_1_1; -.
DR InParanoid; Q5XKE0; -.
DR OMA; CSFNIDV; -.
DR OrthoDB; 67092at2759; -.
DR PhylomeDB; Q5XKE0; -.
DR TreeFam; TF351819; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 233199; 2 hits in 74 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 73 other tissues.
DR ExpressionAtlas; Q5XKE0; baseline and differential.
DR Genevisible; Q5XKE0; MM.
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 CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 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 Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 7.
DR Pfam; PF18362; THB; 1.
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; 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
