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Myosin-13 (Myosin heavy chain 13) (Myosin heavy chain, skeletal muscle, extraocular) (MyHC-EO) (Myosin heavy chain, skeletal muscle, laryngeal) (MyHC-IIL) (Superfast myosin)

 MYH13_HUMAN             Reviewed;        1938 AA.
Q9UKX3; O95252; Q9P0U8;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 2.
18-JUL-2018, entry version 163.
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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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
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; 28.
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; -.
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:0008017; F:microtubule binding; IEA:InterPro.
GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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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