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   27-MAR-2024, entry version 197.
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; 48.
DR   IntAct; Q9UKX3; 29.
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; 9606-ENSP00000404570; -.
DR   PeptideAtlas; Q9UKX3; -.
DR   ProteomicsDB; 84904; -.
DR   Antibodypedia; 3434; 32 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   AGR; HGNC:7571; -.
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; TWDWFLL; -.
DR   OrthoDB; 2877572at2759; -.
DR   PhylomeDB; Q9UKX3; -.
DR   TreeFam; TF314375; -.
DR   PathwayCommons; Q9UKX3; -.
DR   SignaLink; Q9UKX3; -.
DR   BioGRID-ORCS; 8735; 15 hits in 1151 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 primordial germ cell in gonad and 29 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 5.
DR   Gene3D; 1.20.5.370; -; 4.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.10.250.2420; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 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   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF44; MYOSIN-13; 1.
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; SSF90257; Myosin rod fragments; 6.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
DR   Genevisible; Q9UKX3; HS.
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
//