MLRV_RABIT
ID MLRV_RABIT Reviewed; 165 AA.
AC Q7M2V4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Myosin regulatory light chain 2, ventricular/cardiac muscle isoform {ECO:0000305};
DE Short=MLC-2 {ECO:0000250|UniProtKB:P51667};
DE Short=MLC-2v;
DE AltName: Full=Myosin light chain 2, slow skeletal/ventricular muscle isoform {ECO:0000305|PubMed:3779041};
DE Short=MLC-2s/v {ECO:0000305|PubMed:3779041};
GN Name=MYL2 {ECO:0000250|UniProtKB:P10916};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-31.
RA Lindblad-Toh K., Chang J.L., Gnerre S., Clamp M., Lander E.S.;
RT "Annotating the human genome using low coverage mammalian genomes.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|PIR:A61567}
RP PROTEIN SEQUENCE OF 14-165.
RX PubMed=3779041; DOI=10.1007/bf01114760;
RA Collins J.H., Theibert J.L., Dalla Libera L.;
RT "Amino acid sequence of rabbit ventricular myosin light chain-2: identity
RT with the slow skeletal muscle isoform.";
RL Biosci. Rep. 6:655-661(1986).
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:0000255}.
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DR EMBL; AAGW01124952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A61567; A61567.
DR AlphaFoldDB; Q7M2V4; -.
DR SMR; Q7M2V4; -.
DR STRING; 9986.ENSOCUP00000015748; -.
DR eggNOG; KOG0031; Eukaryota.
DR InParanoid; Q7M2V4; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0031672; C:A band; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
DR GO; GO:0060047; P:heart contraction; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
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 CDD; cd00051; EFh; 1.
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; Direct protein sequencing; Metal-binding; Methylation;
KW Motor protein; Muscle protein; Myosin; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q3SZE5"
FT CHAIN 2..165
FT /note="Myosin regulatory light chain 2, ventricular/cardiac
FT muscle isoform"
FT /evidence="ECO:0000250|UniProtKB:P10916"
FT /id="PRO_0000282967"
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:0000250|UniProtKB:Q3SZE5"
FT MOD_RES 14
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P10916"
FT MOD_RES 15
FT /note="Phosphoserine"
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 165 AA; 18762 MW; C89510199DE6348C CRC64;
MSPKKAKKRA EGANSNVFSM FEQTQIQEFK EAFTIMDQNR DGFIDKNDLR DTFAALGRVN
VKNEEIDEMI KEAPGPINFT VFLTMFGEKL KGADPEETIL NAFKVFDPEG KGVLKADYVR
EMLTTQAERF SKDEIDQMFA AFPPDVTGNL DYKNLVHIIT HGEEK
