GENTAUR Molecular Products.

 MYH13_HUMAN             Reviewed;        1938 AA.
 Q9UKX3; O95252; Q9P0U8;
 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
 08-FEB-2011, sequence version 2.
 12-SEP-2018, entry version 164.
 RecName: Full=Myosin-13;
 AltName: Full=Myosin heavy chain 13;
 AltName: Full=Myosin heavy chain, skeletal muscle, extraocular;
          Short=MyHC-EO;
 AltName: Full=Myosin heavy chain, skeletal muscle, laryngeal;
          Short=MyHC-IIL;
 AltName: Full=Superfast myosin;
 Name=MYH13;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLU-1076 AND ARG-1862.
 TISSUE=Extraocular muscle;
 PubMed=10388558; DOI=10.1006/jmbi.1999.2865;
 Weiss A., Schiaffino S., Leinwand L.A.;
 "Comparative sequence analysis of the complete human sarcomeric myosin
 heavy chain family: implications for functional diversity.";
 J. Mol. Biol. 290:61-75(1999).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=16625196; DOI=10.1038/nature04689;
 Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
 Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
 Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
 Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
 DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
 Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
 Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
 Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
 Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
 Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
 Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
 Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
 Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
 Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
 "DNA sequence of human chromosome 17 and analysis of rearrangement in
 the human lineage.";
 Nature 440:1045-1049(2006).
 [3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1656-1822.
 PubMed=11032345; DOI=10.1023/A:1005635030494;
 Shrager J.B., Desjardins P.R., Burkman J.M., Konig S.K., Stewart S.K.,
 Su L., Shah M.C., Bricklin E., Tewari M., Hoffman R., Rickels M.R.,
 Jullian E.H., Rubinstein N.A., Stedman H.H.;
 "Human skeletal myosin heavy chain genes are tightly linked in the
 order embryonic-IIa-IId/x-ILb-perinatal-extraocular.";
 J. Muscle Res. Cell Motil. 21:345-355(2000).
 [4]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1917-1938.
 TISSUE=Extraocular muscle;
 PubMed=9806854; DOI=10.1006/geno.1998.5558;
 Winters L.M., Briggs M.M., Schachat F.;
 "The human extraocular muscle myosin heavy chain gene (MYH13) maps to
 the cluster of fast and developmental myosin genes on chromosome 17.";
 Genomics 54:188-189(1998).
 [5]
 TISSUE SPECIFICITY.
 PubMed=12110653;
 Schachat F., Briggs M.M.;
 "Phylogenetic implications of the superfast myosin in extraocular
 muscles.";
 J. Exp. Biol. 205:2189-2201(2002).
 [6]
 FUNCTION.
 PubMed=23908353; DOI=10.1074/jbc.M113.488130;
 Bloemink M.J., Deacon J.C., Resnicow D.I., Leinwand L.A., Geeves M.A.;
 "The superfast human extraocular myosin is kinetically distinct from
 the fast skeletal IIa, IIb, and IId isoforms.";
 J. Biol. Chem. 288:27469-27479(2013).
 -!- FUNCTION: Fast twitching myosin mediating the high-velocity and
     low-tension contractions of specific striated muscles.
     {ECO:0000269|PubMed:23908353}.
 -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2
     heavy chain subunits (MHC), 2 alkali light chain subunits (MLC)
     and 2 regulatory light chain subunits (MLC-2).
 -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments
     of the myofibrils.
 -!- TISSUE SPECIFICITY: Specifically expressed in extraocular and
     laryngeal muscles. {ECO:0000269|PubMed:12110653}.
 -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing
     cycles of a 28-residue repeat pattern composed of 4 heptapeptides,
     characteristic for alpha-helical coiled coils.
 -!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light
     meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further
     cleaved into 2 globular subfragments (S1) and 1 rod-shaped
     subfragment (S2). {ECO:0000305}.
 -!- DOMAIN: The head-like domain S1 exhibits a much faster ATP-induced
     detachment from actin, and ADP affinity is more than 3-fold weaker
     than other myosins.
 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
     superfamily. Myosin family. {ECO:0000305}.
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 EMBL; AF111782; AAD29948.1; -; mRNA.
 EMBL; AC005291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AH009397; AAF73155.1; -; Genomic_DNA.
 EMBL; AF075248; AAC83241.1; -; Genomic_DNA.
 CCDS; CCDS45613.1; -.
 RefSeq; NP_003793.2; NM_003802.2.
 UniGene; Hs.711142; -.
 ProteinModelPortal; Q9UKX3; -.
 SMR; Q9UKX3; -.
 BioGrid; 114272; 28.
 IntAct; Q9UKX3; 27.
 MINT; Q9UKX3; -.
 STRING; 9606.ENSP00000252172; -.
 iPTMnet; Q9UKX3; -.
 PhosphoSitePlus; Q9UKX3; -.
 BioMuta; MYH13; -.
 DMDM; 322510049; -.
 EPD; Q9UKX3; -.
 MaxQB; Q9UKX3; -.
 PaxDb; Q9UKX3; -.
 PeptideAtlas; Q9UKX3; -.
 PRIDE; Q9UKX3; -.
 ProteomicsDB; 84904; -.
 Ensembl; ENST00000252172; ENSP00000252172; ENSG00000006788.
 Ensembl; ENST00000418404; ENSP00000404570; ENSG00000006788.
 Ensembl; ENST00000621918; ENSP00000480864; ENSG00000006788.
 GeneID; 8735; -.
 KEGG; hsa:8735; -.
 UCSC; uc002gmk.1; human.
 CTD; 8735; -.
 DisGeNET; 8735; -.
 EuPathDB; HostDB:ENSG00000006788.12; -.
 GeneCards; MYH13; -.
 H-InvDB; HIX0039060; -.
 HGNC; HGNC:7571; MYH13.
 MIM; 603487; gene.
 neXtProt; NX_Q9UKX3; -.
 OpenTargets; ENSG00000006788; -.
 PharmGKB; PA31368; -.
 eggNOG; KOG0161; Eukaryota.
 eggNOG; COG5022; LUCA.
 GeneTree; ENSGT00760000118919; -.
 HOGENOM; HOG000173959; -.
 HOVERGEN; HBG004704; -.
 InParanoid; Q9UKX3; -.
 KO; K10352; -.
 OMA; DDMASNI; -.
 OrthoDB; EOG091G07UM; -.
 PhylomeDB; Q9UKX3; -.
 TreeFam; TF314375; -.
 ChiTaRS; MYH13; human.
 GeneWiki; MYH13; -.
 GenomeRNAi; 8735; -.
 PRO; PR:Q9UKX3; -.
 Proteomes; UP000005640; Chromosome 17.
 Bgee; ENSG00000006788; Expressed in 31 organ(s), highest expression level in quadriceps femoris.
 CleanEx; HS_MYH13; -.
 Genevisible; Q9UKX3; HS.
 GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
 GO; GO:0005859; C:muscle myosin complex; TAS:UniProtKB.
 GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
 GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
 GO; GO:0051015; F:actin filament binding; IEA:InterPro.
 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
 GO; GO:0000146; F:microfilament motor activity; TAS:UniProtKB.
 GO; GO:0006936; P:muscle contraction; TAS:UniProtKB.
 Gene3D; 2.30.30.360; -; 1.
 Gene3D; 3.40.850.10; -; 3.
 Gene3D; 4.10.270.10; -; 1.
 InterPro; IPR000048; IQ_motif_EF-hand-BS.
 InterPro; IPR036961; Kinesin_motor_dom_sf.
 InterPro; IPR001609; Myosin_head_motor_dom.
 InterPro; IPR027401; Myosin_IQ_contain_sf.
 InterPro; IPR004009; Myosin_N.
 InterPro; IPR008989; Myosin_S1_N.
 InterPro; IPR002928; Myosin_tail.
 InterPro; IPR027417; P-loop_NTPase.
 Pfam; PF00063; Myosin_head; 1.
 Pfam; PF02736; Myosin_N; 1.
 Pfam; PF01576; Myosin_tail_1; 1.
 PRINTS; PR00193; MYOSINHEAVY.
 SMART; SM00242; MYSc; 1.
 SUPFAM; SSF52540; SSF52540; 1.
 PROSITE; PS50096; IQ; 1.
 PROSITE; PS51456; MYOSIN_MOTOR; 1.
 PROSITE; PS51844; SH3_LIKE; 1.
 2: Evidence at transcript level;
 Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil;
 Complete proteome; Cytoplasm; Methylation; Motor protein;
 Muscle protein; Myosin; Nucleotide-binding; Polymorphism;
 Reference proteome; Thick filament.
 CHAIN         1   1938       Myosin-13.
                              /FTId=PRO_0000123430.
 DOMAIN       33     82       Myosin N-terminal SH3-like.
                              {ECO:0000255|PROSITE-ProRule:PRU01190}.
 DOMAIN       86    782       Myosin motor. {ECO:0000255|PROSITE-
                              ProRule:PRU00782}.
 DOMAIN      785    814       IQ. {ECO:0000255|PROSITE-
                              ProRule:PRU00116}.
 NP_BIND     179    186       ATP. {ECO:0000255}.
 REGION      659    681       Actin-binding. {ECO:0000250}.
 REGION      761    775       Actin-binding. {ECO:0000250}.
 COILED      843   1938       {ECO:0000255}.
 MOD_RES     130    130       N6,N6,N6-trimethyllysine. {ECO:0000255}.
 VARIANT     701    701       G -> R (in dbSNP:rs2190729).
                              /FTId=VAR_030231.
 VARIANT    1071   1071       M -> V (in dbSNP:rs2074877).
                              /FTId=VAR_024543.
 VARIANT    1076   1076       D -> E (in dbSNP:rs2074876).
                              {ECO:0000269|PubMed:10388558}.
                              /FTId=VAR_030232.
 VARIANT    1294   1294       R -> Q (in dbSNP:rs17690195).
                              /FTId=VAR_030233.
 VARIANT    1862   1862       H -> R (in dbSNP:rs3744550).
                              {ECO:0000269|PubMed:10388558}.
                              /FTId=VAR_030234.
 CONFLICT   1097   1097       K -> R (in Ref. 1; AAD29948).
                              {ECO:0000305}.
 CONFLICT   1376   1376       R -> K (in Ref. 1; AAD29948).
                              {ECO:0000305}.
 CONFLICT   1407   1407       N -> K (in Ref. 1; AAD29948).
                              {ECO:0000305}.
 CONFLICT   1645   1645       K -> R (in Ref. 1; AAD29948).
                              {ECO:0000305}.
 SEQUENCE   1938 AA;  223605 MW;  66DD43A84F5D38DA CRC64;
 MSSDAEMAIF GEAAPYLRKP EKERIEAQNR PFDSKKACFV ADNKEMYVKG MIQTRENDKV
 IVKTLDDRML TLNNDQVFPM NPPKFDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
 LFCVTVNPYK WLPVYKPEVV AAYRGKKRQE APPHIFSISD NAYQFMLTDR DNQSILITGE
 SGAGKTVNTK RVIQYFATIA VTGDKKKETQ PGKMQGTLED QIIQANPLLE AFGNAKTVRN
 DNSSRFGKFI RIHFGATGKL ASADIETYLL EKSRVTFQLS SERSYHIFYQ IMSNKKPELI
 DLLLISTNPF DFPFVSQGEV TVASIDDSEE LLATDNAIDI LGFSSEEKVG IYKLTGAVMH
 YGNMKFKQKQ REEQAEPDGT EVADKAGYLM GLNSAEMLKG LCCPRVKVGN EYVTKGQNVQ
 QVTNSVGALA KAVYEKMFLW MVTRINQQLD TKQPRQYFIG VLDIAGFEIF DFNSLEQLCI
 NFTNEKLQQF FNHHMFVLEQ EEYKKEGIEW EFIDFGMDLA ACIELIEKPM GIFSILEEEC
 MFPKATDTSF KNKLYDQHLG KSNNFQKPKP AKGKAEAHFS LVHYAGTVDY NIAGWLDKNK
 DPLNETVVGL YQKSSLKLLS FLFSNYAGAE TGDSGGSKKG GKKKGSSFQT VSAVFRENLN
 KLMTNLRSTH PHFVRCLIPN ETKTPGVMDH YLVMHQLRCN GVLEGIRICR KGFPSRILYA
 DFKQRYRILN ASAIPEGQFI DSKNASEKLL NSIDVDREQF RFGNTKVFFK AGLLGLLEEM
 RDEKLVTLMT STQAVCRGYL MRVEFKKMME RRDSIFCIQY NIRSFMNVKH WPWMNLFFKI
 KPLLKSAEAE KEMATMKEDF ERTKEELARS EARRKELEEK MVSLLQEKND LQLQVQSETE
 NLMDAEERCE GLIKSKILLE AKVKELTERL EEEEEMNSEL VAKKRNLEDK CSSLKRDIDD
 LELTLTKVEK EKHATENKVK NLSEEMTALE ENISKLTKEK KSLQEAHQQT LDDLQVEEDK
 VNGLIKINAK LEQQTDDLEG SLEQEKKLRA DLERAKRKLE GDLKMSQESI MDLENDKQQI
 EEKLKKKEFE LSQLQAKIDD EQVHSLQFQK KIKELQARIE ELEEEIEAEH TLRAKIEKQR
 SDLARELEEI SERLEEASGA TSAQIEMNKK REAEFQKMRR DLEEATLQHE ATAATLRKKQ
 ADSVAELGEQ IDNLQRVKQK LEKEKSELKM EIDDMASNIE ALSKSKSNIE RTCRTVEDQF
 SEIKAKDEQQ TQLIHDLNMQ KARLQTQNGE LSHRVEEKES LISQLTKSKQ ALTQQLEELK
 RQMEEETKAK NAMAHALQSS RHDCDLLREQ YEEEQEAKAE LQRALSKANS EVAQWRTKYE
 TDAIQRTEEL EEAKKKLAQR LQEAEENTET ANSKCASLEK TKQRLQGEVE DLMRDLERSH
 TACATLDKKQ RNFDKVLAEW KQKLDESQAE LEAAQKESRS LSTELFKMRN AYEEVVDQLE
 TLRRENKNLQ EEISDLTEQI AETGKNLQEA EKTKKLVEQE KSDLQVALEE VEGSLEHEES
 KILRVQLELS QVKSELDRKV IEKDEEIEQL KRNSQRAAEA LQSVLDAEIR SRNDALRLKK
 KMEGDLNEME IQLGHSNRQM AETQKHLRTV QGQLKDSQLH LDDALRSNED LKEQLAIVER
 RNGLLLEELE EMKVALEQTE RTRRLSEQEL LDASDRVQLL HSQNTSLINT KKKLEADIAQ
 CQAEVENSIQ ESRNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNL EQTVKDLQHR
 LDEAEQLALK GGKKQIQKLE NRVRELENEL DVEQKRGAEA LKGAHKYERK VKEMTYQAEE
 DHKNILRLQD LVDKLQAKVK SYKRQAEEAE EQANTQLSRC RRVQHELEEA AERADIAESQ
 VNKLRAKSRD VGSQKMEE

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