ID   MYPC2_HUMAN             Reviewed;        1141 AA.
AC   Q14324; A1L4G9;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   27-MAR-2024, entry version 198.
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; Synonyms=MYBPCF;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal skeletal muscle;
RX   PubMed=8375400; DOI=10.1111/j.1432-1033.1993.tb18186.x;
RA   Weber F.E., Vaughan K.T., Reinach F.C., Fischman D.A.;
RT   "Complete sequence of human fast-type and slow-type muscle myosin-binding-
RT   protein C (MyBP-C). Differential expression, conserved domain structure and
RT   chromosome assignment.";
RL   Eur. J. Biochem. 216:661-669(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   STRUCTURE BY NMR OF 44-157; 345-438 AND 825-935.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the first, third and 6th Ig-like domains from human
RT   myosin-binding protein c, fast-type.";
RL   Submitted (AUG-2007) 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.
CC   -!- INTERACTION:
CC       Q14324; Q00872: MYBPC1; NbExp=3; IntAct=EBI-5653200, EBI-5652924;
CC       Q14324; Q8IVP1: SH3GL3; NbExp=3; IntAct=EBI-5653200, EBI-6503765;
CC       Q14324; Q8WZ42: TTN; NbExp=14; IntAct=EBI-5653200, EBI-681210;
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
CC       {ECO:0000305}.
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DR   EMBL; X73113; CAA51544.1; -; mRNA.
DR   EMBL; AC020909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471135; EAW71866.1; -; Genomic_DNA.
DR   EMBL; BC130536; AAI30537.1; -; mRNA.
DR   EMBL; BC136389; AAI36390.1; -; mRNA.
DR   CCDS; CCDS46152.1; -.
DR   PIR; S36845; S36845.
DR   RefSeq; NP_004524.3; NM_004533.3.
DR   PDB; 2E7C; NMR; -; A=824-934.
DR   PDB; 2EDK; NMR; -; A=345-438.
DR   PDB; 2EDN; NMR; -; A=47-157.
DR   PDBsum; 2E7C; -.
DR   PDBsum; 2EDK; -.
DR   PDBsum; 2EDN; -.
DR   AlphaFoldDB; Q14324; -.
DR   SMR; Q14324; -.
DR   BioGRID; 110691; 41.
DR   IntAct; Q14324; 33.
DR   MINT; Q14324; -.
DR   STRING; 9606.ENSP00000350332; -.
DR   CarbonylDB; Q14324; -.
DR   GlyGen; Q14324; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q14324; -.
DR   PhosphoSitePlus; Q14324; -.
DR   BioMuta; MYBPC2; -.
DR   DMDM; 296439237; -.
DR   REPRODUCTION-2DPAGE; IPI00030104; -.
DR   EPD; Q14324; -.
DR   MassIVE; Q14324; -.
DR   PaxDb; 9606-ENSP00000350332; -.
DR   PeptideAtlas; Q14324; -.
DR   ProteomicsDB; 59965; -.
DR   Antibodypedia; 32323; 197 antibodies from 32 providers.
DR   DNASU; 4606; -.
DR   Ensembl; ENST00000357701.6; ENSP00000350332.4; ENSG00000086967.10.
DR   GeneID; 4606; -.
DR   KEGG; hsa:4606; -.
DR   MANE-Select; ENST00000357701.6; ENSP00000350332.4; NM_004533.4; NP_004524.3.
DR   UCSC; uc002psf.3; human.
DR   AGR; HGNC:7550; -.
DR   CTD; 4606; -.
DR   DisGeNET; 4606; -.
DR   GeneCards; MYBPC2; -.
DR   HGNC; HGNC:7550; MYBPC2.
DR   HPA; ENSG00000086967; Group enriched (skeletal muscle, tongue).
DR   MIM; 160793; gene.
DR   neXtProt; NX_Q14324; -.
DR   OpenTargets; ENSG00000086967; -.
DR   PharmGKB; PA31350; -.
DR   VEuPathDB; HostDB:ENSG00000086967; -.
DR   eggNOG; ENOG502QW17; Eukaryota.
DR   GeneTree; ENSGT00940000160092; -.
DR   HOGENOM; CLU_006405_1_1_1; -.
DR   InParanoid; Q14324; -.
DR   OMA; KNTACIL; -.
DR   OrthoDB; 4232090at2759; -.
DR   PhylomeDB; Q14324; -.
DR   TreeFam; TF351819; -.
DR   PathwayCommons; Q14324; -.
DR   Reactome; R-HSA-390522; Striated Muscle Contraction.
DR   SignaLink; Q14324; -.
DR   BioGRID-ORCS; 4606; 15 hits in 1144 CRISPR screens.
DR   ChiTaRS; MYBPC2; human.
DR   EvolutionaryTrace; Q14324; -.
DR   GenomeRNAi; 4606; -.
DR   Pharos; Q14324; Tbio.
DR   PRO; PR:Q14324; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q14324; Protein.
DR   Bgee; ENSG00000086967; Expressed in vastus lateralis and 115 other cell types or tissues.
DR   ExpressionAtlas; Q14324; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; 6.
DR   Pfam; PF18362; THB; 1.
DR   PRINTS; PR00014; FNTYPEIII.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00409; IG; 7.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 7.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 5.
DR   Genevisible; Q14324; HS.
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..1141
FT                   /note="Myosin-binding protein C, fast-type"
FT                   /id="PRO_0000072691"
FT   DOMAIN          50..153
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          255..344
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          345..437
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          438..538
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          539..638
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          641..737
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          739..834
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          838..932
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          935..1030
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1048..1141
FT                   /note="Ig-like C2-type 7"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         29
FT                   /note="E -> K (in dbSNP:rs57092106)"
FT                   /id="VAR_061321"
FT   VARIANT         52
FT                   /note="G -> S (in dbSNP:rs25669)"
FT                   /id="VAR_014657"
FT   VARIANT         282
FT                   /note="D -> N (in dbSNP:rs35951152)"
FT                   /id="VAR_056060"
FT   VARIANT         341
FT                   /note="V -> I (in dbSNP:rs58511181)"
FT                   /id="VAR_061322"
FT   VARIANT         514
FT                   /note="G -> S (in dbSNP:rs8104931)"
FT                   /id="VAR_056061"
FT   VARIANT         624
FT                   /note="V -> I (in dbSNP:rs25665)"
FT                   /id="VAR_014658"
FT   VARIANT         1089
FT                   /note="R -> H (in dbSNP:rs25667)"
FT                   /id="VAR_014659"
FT   CONFLICT        517
FT                   /note="L -> LG (in Ref. 1; CAA51544)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        820
FT                   /note="S -> T (in Ref. 1; CAA51544)"
FT                   /evidence="ECO:0000305"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   TURN            77..79
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   TURN            91..93
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   STRAND          105..110
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   STRAND          116..125
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   TURN            128..130
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   STRAND          144..149
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:2EDN"
FT   STRAND          348..350
FT                   /evidence="ECO:0007829|PDB:2EDK"
FT   STRAND          355..360
FT                   /evidence="ECO:0007829|PDB:2EDK"
FT   STRAND          367..370
FT                   /evidence="ECO:0007829|PDB:2EDK"
FT   STRAND          377..382
FT                   /evidence="ECO:0007829|PDB:2EDK"
FT   STRAND          396..399
FT                   /evidence="ECO:0007829|PDB:2EDK"
FT   STRAND          401..407
FT                   /evidence="ECO:0007829|PDB:2EDK"
FT   HELIX           413..415
FT                   /evidence="ECO:0007829|PDB:2EDK"
FT   STRAND          417..422
FT                   /evidence="ECO:0007829|PDB:2EDK"
FT   STRAND          431..435
FT                   /evidence="ECO:0007829|PDB:2EDK"
FT   STRAND          835..840
FT                   /evidence="ECO:0007829|PDB:2E7C"
FT   TURN            844..846
FT                   /evidence="ECO:0007829|PDB:2E7C"
FT   STRAND          850..856
FT                   /evidence="ECO:0007829|PDB:2E7C"
FT   STRAND          858..868
FT                   /evidence="ECO:0007829|PDB:2E7C"
FT   STRAND          871..876
FT                   /evidence="ECO:0007829|PDB:2E7C"
FT   STRAND          887..890
FT                   /evidence="ECO:0007829|PDB:2E7C"
FT   STRAND          892..901
FT                   /evidence="ECO:0007829|PDB:2E7C"
FT   TURN            904..906
FT                   /evidence="ECO:0007829|PDB:2E7C"
FT   STRAND          908..915
FT                   /evidence="ECO:0007829|PDB:2E7C"
FT   STRAND          924..930
FT                   /evidence="ECO:0007829|PDB:2E7C"
SQ   SEQUENCE   1141 AA;  128072 MW;  91F4B18C4367743A CRC64;
     MPEAKPAAKK APKGKDAPKG APKEAPPKEA PAEAPKEAPP EDQSPTAEEP TGVFLKKPDS
     VSVETGKDAV VVAKVNGKEL PDKPTIKWFK GKWLELGSKS GARFSFKESH NSASNVYTVE
     LHIGKVVLGD RGYYRLEVKA KDTCDSCGFN IDVEAPRQDA SGQSLESFKR TSEKKSDTAG
     ELDFSGLLKK REVVEEEKKK KKKDDDDLGI PPEIWELLKG AKKSEYEKIA FQYGITDLRG
     MLKRLKKAKV EVKKSAAFTK KLDPAYQVDR GNKIKLMVEI SDPDLTLKWF KNGQEIKPSS
     KYVFENVGKK RILTINKCTL ADDAAYEVAV KDEKCFTELF VKEPPVLIVT PLEDQQVFVG
     DRVEMAVEVS EEGAQVMWMK DGVELTREDS FKARYRFKKD GKRHILIFSD VVQEDRGRYQ
     VITNGGQCEA ELIVEEKQLE VLQDIADLTV KASEQAVFKC EVSDEKVTGK WYKNGVEVRP
     SKRITISHVG RFHKLVIDDV RPEDEGDYTF VPDGYALSLS AKLNFLEIKV EYVPKQEPPK
     IHLDCSGKTS ENAIVVVAGN KLRLDVSITG EPPPVATWLK GDEVFTTTEG RTRIEKRVDC
     SSFVIESAQR EDEGRYTIKV TNPVGEDVAS IFLQVVDVPD PPEAVRITSV GEDWAILVWE
     PPMYDGGKPV TGYLVERKKK GSQRWMKLNF EVFTETTYES TKMIEGILYE MRVFAVNAIG
     VSQPSMNTKP FMPIAPTSEP LHLIVEDVTD TTTTLKWRPP NRIGAGGIDG YLVEYCLEGS
     EEWVPANTEP VERCGFTVKN LPTGARILFR VVGVNIAGRS EPATLAQPVT IREIAEPPKI
     RLPRHLRQTY IRKVGEQLNL VVPFQGKPRP QVVWTKGGAP LDTSRVHVRT SDFDTVFFVR
     QAARSDSGEY ELSVQIENMK DTATIRIRVV EKAGPPINVM VKEVWGTNAL VEWQAPKDDG
     NSEIMGYFVQ KADKKTMEWF NVYERNRHTS CTVSDLIVGN EYYFRVYTEN ICGLSDSPGV
     SKNTARILKT GITFKPFEYK EHDFRMAPKF LTPLIDRVVV AGYSAALNCA VRGHPKPKVV
     WMKNKMEIRE DPKFLITNYQ GVLTLNIRRP SPFDAGTYTC RAVNELGEAL AECKLEVRVP
     Q
//