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 03-AUG-2022, entry version 132.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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; DOI=10.1152/ajpcell.1993.264.5.c1252;
RA White S., Martin A.F., Periasamy M.;
RT "Identification of a novel smooth muscle myosin heavy chain cDNA: isoform
RT 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 SEQUENCE
RP [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 AND
RP SER-1309, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT 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 heavy
CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC regulatory light chain subunits (MLC-2). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000250}. Cytoplasm, myofibril.
CC 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 small
CC and large intestine, uterus, bladder, aorta, stomach, and at much lower
CC levels in lung. All three isoforms are coexpressed in smooth muscle.
CC Isoform 2 predominates in most of the smooth muscles tested, with the
CC exception of intestine and urinary bladder, which show greater
CC expression of isoform 1. {ECO:0000269|PubMed:2614841,
CC ECO:0000269|PubMed:7684561}.
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. {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 subfragment
CC (S2). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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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 AlphaFoldDB; Q63862; -.
DR SMR; Q63862; -.
DR IntAct; Q63862; 1.
DR iPTMnet; Q63862; -.
DR jPOST; Q63862; -.
DR PaxDb; Q63862; -.
DR PRIDE; Q63862; -.
DR RGD; 3136; Myh11.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; Q63862; -.
DR PhylomeDB; Q63862; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005859; C:muscle myosin complex; ISO:RGD.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; ISO:RGD.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0030485; C:smooth muscle contractile fiber; ISO:RGD.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
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:0003774; F:cytoskeletal motor activity; ISO:RGD.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0008307; F:structural constituent of muscle; ISO:RGD.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0055013; P:cardiac muscle cell development; ISO:RGD.
DR GO; GO:0048251; P:elastic fiber assembly; ISO:RGD.
DR GO; GO:0006939; P:smooth muscle contraction; ISO:RGD.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
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;
KW Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Coiled coil; Cytoplasm; Motor protein; Muscle protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Thick filament.
FT CHAIN <1..1327
FT /note="Myosin-11"
FT /id="PRO_0000123428"
FT DOMAIN <1..646
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 649..678
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 524..546
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 625..639
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1127..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1327
FT /note="C-terminal"
FT COILED 707..1289
FT /evidence="ECO:0000255"
FT COMPBIAS 1127..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P10587"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1306
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08638"
FT VAR_SEQ 61..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7684561"
FT /id="VSP_050914"
FT VAR_SEQ 1285..1327
FT /note="RGNEASFVPSRRAGGRRVIENTDGSEEEMDARDSDFNGTKASE -> GPPPQ
FT ETSQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:2614841"
FT /id="VSP_050915"
FT NON_CONS 706..707
FT /evidence="ECO:0000305"
FT NON_TER 1
FT /evidence="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
