(data stored in ACNUC14238 zone)

SWISSPROT: MYH11_RAT

ID   MYH11_RAT               Reviewed;        1327 AA.
AC   Q63862; Q58GJ0; Q63338; Q63339; Q63861;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 3.
DT   10-MAY-2017, entry version 112.
DE   RecName: Full=Myosin-11;
DE   AltName: Full=Myosin heavy chain 11;
DE   AltName: Full=Myosin heavy chain, smooth muscle isoform;
DE   AltName: Full=SMMHC;
DE   Flags: Fragments;
GN   Name=Myh11 {ECO:0000312|RGD:3136};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAB26775.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-706 (ISOFORMS 1 AND 2), AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Fetal smooth muscle {ECO:0000269|PubMed:7684561}, and
RC   Stomach {ECO:0000269|PubMed:7684561};
RX   PubMed=7684561;
RA   White S., Martin A.F., Periasamy M.;
RT   "Identification of a novel smooth muscle myosin heavy chain cDNA:
RT   isoform diversity in the S1 head region.";
RL   Am. J. Physiol. 264:C1252-C1258(1993).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:CAA34348.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 707-1327 (ISOFORM 1), NUCLEOTIDE
RP   SEQUENCE [MRNA] OF 707-1327 (ISOFORM 3), AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley {ECO:0000312|EMBL:CAA34348.1};
RC   TISSUE=Fetal aorta {ECO:0000312|EMBL:CAA34348.1};
RX   PubMed=2614841; DOI=10.1016/0022-2836(89)90142-3;
RA   Babij P., Periasamy M.;
RT   "Myosin heavy chain isoform diversity in smooth muscle is produced by
RT   differential RNA processing.";
RL   J. Mol. Biol. 210:673-679(1989).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1039; SER-1077; THR-1306
RP   AND SER-1309, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Muscle contraction. {ECO:0000305}.
CC   -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2
CC       heavy chain subunits (MHC), 2 alkali light chain subunits (MLC)
CC       and 2 regulatory light chain subunits (MLC-2). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000250}. Cytoplasm,
CC       myofibril. Note=Thick filaments of the myofibrils.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:7684561}; Synonyms=SM1B
CC       {ECO:0000303|PubMed:7684561};
CC         IsoId=Q63862-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:7684561}; Synonyms=SM1A
CC       {ECO:0000303|PubMed:7684561};
CC         IsoId=Q63862-2; Sequence=VSP_050914;
CC       Name=3 {ECO:0000269|PubMed:2614841}; Synonyms=SM2
CC       {ECO:0000303|PubMed:2614841};
CC         IsoId=Q63862-3; Sequence=VSP_050915;
CC   -!- TISSUE SPECIFICITY: Both isoform 1 and isoform 2 are detected in
CC       small and large intestine, uterus, bladder, aorta, stomach, and at
CC       much lower levels in lung. All three isoforms are coexpressed in
CC       smooth muscle. Isoform 2 predominates in most of the smooth
CC       muscles tested, with the exception of intestine and urinary
CC       bladder, which show greater expression of isoform 1.
CC       {ECO:0000269|PubMed:2614841, ECO:0000269|PubMed:7684561}.
CC   -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing
CC       cycles of a 28-residue repeat pattern composed of 4 heptapeptides,
CC       characteristic for alpha-helical coiled coils. {ECO:0000305}.
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
CC       subfragment (S2). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
DR   EMBL; AY953023; AAX51987.1; -; mRNA.
DR   EMBL; S61948; AAB26775.1; -; mRNA.
DR   EMBL; X16261; CAA34347.1; -; mRNA.
DR   EMBL; X16262; CAA34348.1; -; mRNA.
DR   PIR; S07537; S07537.
DR   PIR; S10450; S10450.
DR   UniGene; Rn.94969; -.
DR   ProteinModelPortal; Q63862; -.
DR   SMR; Q63862; -.
DR   IntAct; Q63862; 1.
DR   STRING; 10116.ENSRNOP00000043197; -.
DR   iPTMnet; Q63862; -.
DR   PaxDb; Q63862; -.
DR   PRIDE; Q63862; -.
DR   RGD; 3136; Myh11.
DR   eggNOG; KOG0161; Eukaryota.
DR   eggNOG; COG5022; LUCA.
DR   HOGENOM; HOG000173958; -.
DR   HOVERGEN; HBG004704; -.
DR   InParanoid; Q63862; -.
DR   PhylomeDB; Q63862; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005859; C:muscle myosin complex; NAS:UniProtKB.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:InterPro.
DR   GO; GO:0008307; F:structural constituent of muscle; NAS:UniProtKB.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00063; Myosin_head; 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.
PE   1: Evidence at protein level;
DR   PRODOM; Q63862.
DR   SWISS-2DPAGE; Q63862.
KW   Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW   Coiled coil; Complete proteome; Cytoplasm; Motor protein;
KW   Muscle protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Thick filament.
FT   CHAIN        <1   1327       Myosin-11.
FT                                /FTId=PRO_0000123428.
FT   DOMAIN       <1    646       Myosin motor.
FT   DOMAIN      649    678       IQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00116}.
FT   NP_BIND      34     41       ATP. {ECO:0000250|UniProtKB:P10587}.
FT   REGION      524    546       Actin-binding. {ECO:0000250}.
FT   REGION      625    639       Actin-binding. {ECO:0000250}.
FT   REGION     1290   1327       C-terminal.
FT   COILED      707   1289       {ECO:0000255}.
FT   MOD_RES    1039   1039       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1077   1077       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1306   1306       Phosphothreonine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1309   1309       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1326   1326       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O08638}.
FT   VAR_SEQ      61     67       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:7684561}.
FT                                /FTId=VSP_050914.
FT   VAR_SEQ    1285   1327       RGNEASFVPSRRAGGRRVIENTDGSEEEMDARDSDFNGTKA
FT                                SE -> GPPPQETSQ (in isoform 3).
FT                                {ECO:0000303|PubMed:2614841}.
FT                                /FTId=VSP_050915.
FT   NON_CONS    706    707       {ECO:0000305}.
FT   NON_TER       1      1       {ECO:0000305}.
SQ   SEQUENCE   1327 AA;  152492 MW;  EE56D86984389F04 CRC64;
     KKRHEMPPHI YAIADTAYRS MLQDREDQSI LCTGESGAGK TENTKKVIQY LAVVASSHKG
     KKDSSITQGP SFAYGELEKQ LLQANPILEA FGNAKTVKND NSSRFGKFIR INFDVTGYIV
     GANIETYLLE KSRAIRHARD ERTFHIFYYL IAGAKEKMRN DLLLESFNSY TFLSNGFVPI
     PAAQDDEMFQ ETLEAMSIMG FSEEEQLAIL KVVSSVLQLG NIVFKKERNT DQASMPDNTA
     AQKVCHLVGI NVTDFTRAIL TPRIKVGRDV VQKAQTKEQA DFAIEALAKA TYERLFRWIL
     SRVNKALDKT HRQGASFLGI LDIAGFEIFE VNSFEQLCIN YTNEKLQQLF NHTMFILEQE
     EYQREGIEWN FIDFGLDLQP CIELIERPNN PPGVLALLDE ECWFPKATDK SFVEKLCSEQ
     GNHPKFQKPK QLKDKTEFSI IHYAGKVDYN ASAWLTKNMD PLNDNVTSLL NASSDKFVAD
     LWKDVDRIVG LDQMAKMTES SLPSASKTKK GMFRTVGQLY KEQLGKLMTT LRNTTPNFVR
     CIIPNHEKRS GKLDAFLVLE QLRCNGVLEG IRICRQGFPN RIVFQEFRQR YEILAANAIP
     KGFMDGKQAC ILMIKALELD PNLYRIGQSK IFFRTGVLAH LEEERDLKIT DVIMAFQAMC
     RGYLARKAFT KRQQQLTASK VIQRNCAAYL KLRNWQWWRL FTKVKPLDEE MEAKQNLERH
     VSTLNIQLSD SKKKLQDLAS TIEVMEEGKK RLQKEMEGLG QQYEEKAAAY DKLEKTKNRL
     QQELDDLVVD LDNQRQLVSN LEKKQKKFDQ LLAEEKNISS KYADERDRAE AEAREKETKA
     LSLARALEEA LEAKEELERT NKMLKAEMED LVSSKDDVGK NVHELEKSKR ALETQMEEMR
     TQLEELEDEL QATEDAKLRL EVNMQALKGQ FERDLQARDE QNEEKRRQLQ RQLHEYETEL
     EDERKQRALA AAAKKKLEGD LKDLELQADS AVKGREEAIK QLRKLQAQMK DFQRELDDAR
     ASRDEIFATS KENEKKAKSL EAELMQLQED LAAAERARKQ ADLEKEELAE ELASSLSGRN
     TLQDEKRRLE ARIAQLEEEL EEEQGNMEAM SDRVRKATLQ AEQLSNELVT ERSAAQKNES
     ARQQLERQNK ELRSKLQEVE GAVKAKLKST VAALEAKIVQ LEEQIEQEAR EKQAATKLLK
     QKDKKLKEVL LQVEDERKMV EQYKEQAEKG NTKVKQLKRQ LEEAEEESQR INANRRKLQR
     ELDEATESNE AMGREVNALK SKLRRGNEAS FVPSRRAGGR RVIENTDGSE EEMDARDSDF
     NGTKASE
//

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