MYH13_CANLF
ID MYH13_CANLF Reviewed; 1940 AA.
AC Q076A3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Myosin-13;
DE AltName: Full=Fast myosin heavy chain extraocular;
DE AltName: Full=Myosin heavy chain 13;
DE AltName: Full=Myosin heavy chain, skeletal muscle, extraocular;
DE Short=MyHC-eo;
GN Name=MYH13;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Maccatrozzo L., Patruno M., Mascarello F., Reggiani C.;
RT "Canine myosin heavy chain expression.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Fast twitching myosin mediating the high-velocity and low-
CC tension contractions of specific striated muscles. {ECO:0000250}.
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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril {ECO:0000250}. Note=Thick
CC filaments of the myofibrils. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; DQ227284; ABB96411.1; -; Genomic_DNA.
DR AlphaFoldDB; Q076A3; -.
DR SMR; Q076A3; -.
DR STRING; 9612.ENSCAFP00000025727; -.
DR PaxDb; Q076A3; -.
DR PRIDE; Q076A3; -.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; Q076A3; -.
DR Proteomes; UP000002254; Unplaced.
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: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 3: Inferred from homology;
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..1940
FT /note="Myosin-13"
FT /id="PRO_0000274172"
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 1886..1940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 843..1940
FT /evidence="ECO:0000255"
FT COMPBIAS 1903..1940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 1940 AA; 223341 MW; CB67DB4702D6B351 CRC64;
MSSDAEMAIF GEAAPYLRKP EKERIEAQNR PFDSKKACFA MDDKEMYVKG MIQSRENDKV
TVKTLDDRTL TLNSDQVFPM NPPKFDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNPEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR DNQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEQQ PGKMQGTLED QIIQANPLLE AFGNAKTVRN
DNSSRFGKFI RIHFGATGKL ASADIETYLL EKSRVTFQLS SERSYHIFYQ ILSNKKPELI
DLLLISTNPF DFPFVSQGEV TVASINDSEE 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 AGDSGGSKKG GKKKGSSFQT VSAVFRENLN
KLMTNLRSTH PHFVRCLIPN ETKTPGVMDH YLVMHQLRCN GVLEGIRICR KGFPSRILYA
DFKQRYRILN ASAIPEGQFI DSKNASEKLL SSIDVDREQY RFGHTKVFFK AGLLGLLEEM
RDEKLVTLMT RTQAICRGYL MRVEFKKMME RRESIFCIQY NIRSFMNVKH WPWMNLFFKI
KPLLKSAEAE REMATMKEDF ERAKEELARS EARRKELEEK MVSLLQEKND LQLQVQSETE
NLIDAEERCE GLIKSKIQLE AKVKELNERL EEEEEVNSDL VAKKRSLEDK CSSLKRDIDD
LELTLTKVEK EKHATENKVK NLSEEMTALE ENISKLTKEK KSLQEAHQQA LDDLQVEEDK
VNGLIKINVK LEQQTDDLEG SLEQEKKLRA DLERIKKKLE GDLKLSQESI MDLENDKQQV
EEKLKKKEFE ISQLQTKIDD EQVHSLQLQK KIKELQARIE ELEEEIEAER ASRAKAEKQR
SDLSRELEEI SERLEEASGV TSAQVEMNKK REAEFQKLRR DLEEATLQHE ATTAALRKKH
ADSVAELGEQ IDNLQRVKQK LEKEKSELKM EIDDLASNIE TVSKSKSNVE RMCRTVEDQF
NEIKAKDDQQ TQLIHDLNMQ KARLQTQNGE LSHQLEEKES LISQLTKGKQ ALTQQLEELK
RQLEEETKAK NALAHALQSS RHDCDLLREQ YEEEQEGKAE LQRALSKANS EVAQWRTKYE
TDAIQRTEEL EEAKKKLAQR LQEAEENTEA VSSKCASLEK TKQRLQGEVD DLMLDLERTS
TARAILDRKQ RDLDKVLAEW KQKLDGSQAE LEAAQKGSRS LSTEIFKMQN AYEEVVDQLE
TLRRENKNLQ EEISDLTEQI AETGKHLQEV EKSKKQVEQE KSDLQVALEE VEASGSLEHE
ESKILRVQLE LSQVKSELDR RVTEKDEEIE QLKRNSQRAA EAMQSMLDAE IRSRNDALRL
KKKMEGDLNE LEIQLGHSSR QVAETQKHLR TVQGQLKDSQ LHLDDALRSN EDLKEQLAIV
ERRNGLLLEE LEEMKAALEQ TERTRRLSEQ ELLDASDRVQ LLHSQNTSLI NTKKKLEVDI
AQCQAEVENS LQESRNAEEK AKKAITDAAM MAEELKKEQD TSAHLERMKK NLEQTVKDLQ
HRLDEAEQLA LKGGKKQIQK LEARVRELES ELDAEQKRGA EALKGAHKYE RKVKELTYQA
EEDRKNILRL QDLVDKLQAK VKAYKRQAEE AEEQANTQMS KCRRVQHELE EAEERADIAE
SQVNKLRAKS RDVGAQKMEE
