MYH13_HUMAN
ID MYH13_HUMAN Reviewed; 1938 AA.
AC Q9UKX3; O95252; Q9P0U8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Myosin-13;
DE AltName: Full=Myosin heavy chain 13;
DE AltName: Full=Myosin heavy chain, skeletal muscle, extraocular;
DE Short=MyHC-EO;
DE AltName: Full=Myosin heavy chain, skeletal muscle, laryngeal;
DE Short=MyHC-IIL;
DE AltName: Full=Superfast myosin;
GN Name=MYH13;
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], AND VARIANTS GLU-1076 AND ARG-1862.
RC TISSUE=Extraocular muscle;
RX PubMed=10388558; DOI=10.1006/jmbi.1999.2865;
RA Weiss A., Schiaffino S., Leinwand L.A.;
RT "Comparative sequence analysis of the complete human sarcomeric myosin
RT heavy chain family: implications for functional diversity.";
RL J. Mol. Biol. 290:61-75(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1656-1822.
RX PubMed=11032345; DOI=10.1023/a:1005635030494;
RA Shrager J.B., Desjardins P.R., Burkman J.M., Konig S.K., Stewart S.K.,
RA Su L., Shah M.C., Bricklin E., Tewari M., Hoffman R., Rickels M.R.,
RA Jullian E.H., Rubinstein N.A., Stedman H.H.;
RT "Human skeletal myosin heavy chain genes are tightly linked in the order
RT embryonic-IIa-IId/x-ILb-perinatal-extraocular.";
RL J. Muscle Res. Cell Motil. 21:345-355(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1917-1938.
RC TISSUE=Extraocular muscle;
RX PubMed=9806854; DOI=10.1006/geno.1998.5558;
RA Winters L.M., Briggs M.M., Schachat F.;
RT "The human extraocular muscle myosin heavy chain gene (MYH13) maps to the
RT cluster of fast and developmental myosin genes on chromosome 17.";
RL Genomics 54:188-189(1998).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12110653; DOI=10.1242/jeb.205.15.2189;
RA Schachat F., Briggs M.M.;
RT "Phylogenetic implications of the superfast myosin in extraocular
RT muscles.";
RL J. Exp. Biol. 205:2189-2201(2002).
RN [6]
RP FUNCTION.
RX PubMed=23908353; DOI=10.1074/jbc.m113.488130;
RA Bloemink M.J., Deacon J.C., Resnicow D.I., Leinwand L.A., Geeves M.A.;
RT "The superfast human extraocular myosin is kinetically distinct from the
RT fast skeletal IIa, IIb, and IId isoforms.";
RL J. Biol. Chem. 288:27469-27479(2013).
CC -!- FUNCTION: Fast twitching myosin mediating the high-velocity and low-
CC tension contractions of specific striated muscles.
CC {ECO:0000269|PubMed:23908353}.
CC -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC regulatory light chain subunits (MLC-2).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC myofibrils.
CC -!- TISSUE SPECIFICITY: Specifically expressed in extraocular and laryngeal
CC muscles. {ECO:0000269|PubMed:12110653}.
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils.
CC -!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light
CC meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further
CC cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment
CC (S2). {ECO:0000305}.
CC -!- DOMAIN: The head-like domain S1 exhibits a much faster ATP-induced
CC detachment from actin, and ADP affinity is more than 3-fold weaker than
CC other myosins.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AF111782; AAD29948.1; -; mRNA.
DR EMBL; AC005291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AH009397; AAF73155.1; -; Genomic_DNA.
DR EMBL; AF075248; AAC83241.1; -; Genomic_DNA.
DR CCDS; CCDS45613.1; -.
DR RefSeq; NP_003793.2; NM_003802.2.
DR AlphaFoldDB; Q9UKX3; -.
DR SMR; Q9UKX3; -.
DR BioGRID; 114272; 39.
DR IntAct; Q9UKX3; 28.
DR MINT; Q9UKX3; -.
DR STRING; 9606.ENSP00000404570; -.
DR iPTMnet; Q9UKX3; -.
DR PhosphoSitePlus; Q9UKX3; -.
DR BioMuta; MYH13; -.
DR DMDM; 322510049; -.
DR EPD; Q9UKX3; -.
DR jPOST; Q9UKX3; -.
DR MassIVE; Q9UKX3; -.
DR MaxQB; Q9UKX3; -.
DR PaxDb; Q9UKX3; -.
DR PeptideAtlas; Q9UKX3; -.
DR PRIDE; Q9UKX3; -.
DR ProteomicsDB; 84904; -.
DR Antibodypedia; 3434; 23 antibodies from 13 providers.
DR DNASU; 8735; -.
DR Ensembl; ENST00000252172.9; ENSP00000252172.4; ENSG00000006788.14.
DR Ensembl; ENST00000418404.8; ENSP00000404570.3; ENSG00000006788.14.
DR Ensembl; ENST00000621918.1; ENSP00000480864.1; ENSG00000006788.14.
DR GeneID; 8735; -.
DR KEGG; hsa:8735; -.
DR MANE-Select; ENST00000252172.9; ENSP00000252172.4; NM_003802.3; NP_003793.2.
DR UCSC; uc002gmk.1; human.
DR CTD; 8735; -.
DR DisGeNET; 8735; -.
DR GeneCards; MYH13; -.
DR HGNC; HGNC:7571; MYH13.
DR HPA; ENSG00000006788; Tissue enhanced (skeletal muscle, stomach).
DR MIM; 603487; gene.
DR neXtProt; NX_Q9UKX3; -.
DR OpenTargets; ENSG00000006788; -.
DR PharmGKB; PA31368; -.
DR VEuPathDB; HostDB:ENSG00000006788; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000162543; -.
DR HOGENOM; CLU_000192_8_1_1; -.
DR InParanoid; Q9UKX3; -.
DR OMA; QFKFGHT; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; Q9UKX3; -.
DR TreeFam; TF314375; -.
DR PathwayCommons; Q9UKX3; -.
DR SignaLink; Q9UKX3; -.
DR BioGRID-ORCS; 8735; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; MYH13; human.
DR GeneWiki; MYH13; -.
DR GenomeRNAi; 8735; -.
DR Pharos; Q9UKX3; Tbio.
DR PRO; PR:Q9UKX3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UKX3; protein.
DR Bgee; ENSG00000006788; Expressed in skeletal muscle tissue and 29 other tissues.
DR Genevisible; Q9UKX3; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005859; C:muscle myosin complex; TAS:UniProtKB.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR CDD; cd14923; MYSc_Myh13; 1.
DR Gene3D; 1.20.5.370; -; 4.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR042702; Myh13_MYSc.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014751; XRCC4-like_C.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Methylation; Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW Reference proteome; Thick filament.
FT CHAIN 1..1938
FT /note="Myosin-13"
FT /id="PRO_0000123430"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..782
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 785..814
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 659..681
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 761..775
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1917..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 843..1938
FT /evidence="ECO:0000255"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 130
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT VARIANT 701
FT /note="G -> R (in dbSNP:rs2190729)"
FT /id="VAR_030231"
FT VARIANT 1071
FT /note="M -> V (in dbSNP:rs2074877)"
FT /id="VAR_024543"
FT VARIANT 1076
FT /note="D -> E (in dbSNP:rs2074876)"
FT /evidence="ECO:0000269|PubMed:10388558"
FT /id="VAR_030232"
FT VARIANT 1294
FT /note="R -> Q (in dbSNP:rs17690195)"
FT /id="VAR_030233"
FT VARIANT 1862
FT /note="H -> R (in dbSNP:rs3744550)"
FT /evidence="ECO:0000269|PubMed:10388558"
FT /id="VAR_030234"
FT CONFLICT 1097
FT /note="K -> R (in Ref. 1; AAD29948)"
FT /evidence="ECO:0000305"
FT CONFLICT 1376
FT /note="R -> K (in Ref. 1; AAD29948)"
FT /evidence="ECO:0000305"
FT CONFLICT 1407
FT /note="N -> K (in Ref. 1; AAD29948)"
FT /evidence="ECO:0000305"
FT CONFLICT 1645
FT /note="K -> R (in Ref. 1; AAD29948)"
FT /evidence="ECO:0000305"
SQ 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
