MLRV_BOVIN
ID MLRV_BOVIN Reviewed; 166 AA.
AC Q3SZE5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Myosin regulatory light chain 2, ventricular/cardiac muscle isoform {ECO:0000305};
DE Short=MLC-2 {ECO:0000250|UniProtKB:P08733};
DE Short=MLC-2v;
DE AltName: Full=Myosin light chain 2, slow skeletal/ventricular muscle isoform {ECO:0000250|UniProtKB:Q7M2V4};
DE Short=MLC-2s/v {ECO:0000250|UniProtKB:Q7M2V4};
GN Name=MYL2 {ECO:0000250|UniProtKB:P10916};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI02915.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI02915.1};
RC TISSUE=Heart ventricle {ECO:0000312|EMBL:AAI02915.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP METHYLATION AT SER-2.
RX PubMed=3979397; DOI=10.1111/j.1432-1033.1985.tb08809.x;
RA Henry G.D., Trayer I.P., Brewer S., Levine B.A.;
RT "The widespread distribution of alpha-N-trimethylalanine as the N-terminal
RT amino acid of light chains from vertebrate striated muscle myosins.";
RL Eur. J. Biochem. 148:75-82(1985).
CC -!- FUNCTION: Contractile protein that plays a role in heart development
CC and function (By similarity). Following phosphorylation, plays a role
CC in cross-bridge cycling kinetics and cardiac muscle contraction by
CC increasing myosin lever arm stiffness and promoting myosin head
CC diffusion; as a consequence of the increase in maximum contraction
CC force and calcium sensitivity of contraction force. These events
CC altogether slow down myosin kinetics and prolong duty cycle resulting
CC in accumulated myosins being cooperatively recruited to actin binding
CC sites to sustain thin filament activation as a means to fine-tune
CC myofilament calcium sensitivity to force (By similarity). During
CC cardiogenesis plays an early role in cardiac contractility by promoting
CC cardiac myofibril assembly (By similarity).
CC {ECO:0000250|UniProtKB:P08733, ECO:0000250|UniProtKB:P51667}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains (By
CC similarity). Interacts with MYOC (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P10916}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band
CC {ECO:0000250|UniProtKB:P08733}.
CC -!- PTM: N-terminus is methylated by METTL11A/NTM1.
CC {ECO:0000250|UniProtKB:P51667}.
CC -!- PTM: Phosphorylated by MYLK3 and MYLK2; promotes cardiac muscle
CC contraction and function (By similarity). Dephosphorylated by PPP1CB
CC complexed to PPP1R12B (By similarity). The phosphorylated form in adult
CC is expressed as gradients across the heart from endocardium (low
CC phosphorylation) to epicardium (high phosphorylation); regulates
CC cardiac torsion and workload distribution (By similarity).
CC {ECO:0000250|UniProtKB:P08733, ECO:0000250|UniProtKB:P51667}.
CC -!- MISCELLANEOUS: This chain binds calcium. {ECO:0000305}.
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DR EMBL; BC102914; AAI02915.1; -; mRNA.
DR RefSeq; NP_001030197.1; NM_001035025.2.
DR AlphaFoldDB; Q3SZE5; -.
DR SMR; Q3SZE5; -.
DR STRING; 9913.ENSBTAP00000024444; -.
DR iPTMnet; Q3SZE5; -.
DR PaxDb; Q3SZE5; -.
DR GeneID; 505519; -.
DR KEGG; bta:505519; -.
DR CTD; 4633; -.
DR eggNOG; KOG0031; Eukaryota.
DR InParanoid; Q3SZE5; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031672; C:A band; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
DR GO; GO:0060047; P:heart contraction; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0042694; P:muscle cell fate specification; IBA:GO_Central.
DR GO; GO:0098735; P:positive regulation of the force of heart contraction; ISS:UniProtKB.
DR GO; GO:0002026; P:regulation of the force of heart contraction; ISS:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF00036; EF-hand_1; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Metal-binding; Methylation; Motor protein;
KW Muscle protein; Myosin; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..166
FT /note="Myosin regulatory light chain 2, ventricular/cardiac
FT muscle isoform"
FT /evidence="ECO:0000250|UniProtKB:P10916"
FT /id="PRO_0000283744"
FT DOMAIN 24..59
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 94..129
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 130..165
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N,N,N-trimethylserine"
FT /evidence="ECO:0000305|PubMed:3979397"
FT MOD_RES 14
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P10916"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51667"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08733"
SQ SEQUENCE 166 AA; 18981 MW; E8AC5EC7DF56E839 CRC64;
MSPKKAKKRA EGANYNVFSM FEQTQIQEFK EAFTIMDQNR DGFIDKNDLR DTFAALGRVN
VKNEEIDEML KEAPGPINFT VFLQMFGEKL KGADPEETIL NAFKVFDPEG KGVLKADYIK
EMLTTQAERF SKEEIDQMFA AFPPDVTGNL DYKNLVHIIT HGEEKD
