MRLCA_RAT
ID MRLCA_RAT Reviewed; 172 AA.
AC P13832;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Myosin regulatory light chain RLC-A;
DE Short=Myosin RLC-A;
DE AltName: Full=Myosin regulatory light chain 2-A, smooth muscle isoform;
GN Name=Rlc-a;
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]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3584239; DOI=10.1083/jcb.104.6.1505;
RA Taubman M.B., Grant J.W., Nadal-Ginard B.;
RT "Cloning and characterization of mammalian myosin regulatory light chain
RT (RLC) cDNA: the RLC gene is expressed in smooth, sarcomeric, and nonmuscle
RT tissues.";
RL J. Cell Biol. 104:1505-1513(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Fischer;
RX PubMed=2391362; DOI=10.1083/jcb.111.3.1127;
RA Grant J.W., Taubmann M.B., Church S.L., Johnson R.L., Nadal-Ginard B.;
RT "Mammalian nonsarcomeric myosin regulatory light chains are encoded by two
RT differentially regulated and linked genes.";
RL J. Cell Biol. 111:1127-1135(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1649372; DOI=10.1016/0169-328x(91)90099-j;
RA Feinstein D.L., Durand M., Milner R.J.;
RT "Expression of myosin regulatory light chains in rat brain:
RT characterization of a novel isoform.";
RL Brain Res. Mol. Brain Res. 10:97-105(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8034049; DOI=10.1016/0014-5793(94)00613-x;
RA Wang Y., Chantler P.D.;
RT "Functional analysis of individual brain myosin II isoforms through hybrid
RT formation.";
RL FEBS Lett. 348:244-248(1994).
CC -!- FUNCTION: Myosin regulatory subunit that plays an important role in
CC regulation of both smooth muscle and nonmuscle cell contractile
CC activity via its phosphorylation. Implicated in cytokinesis, receptor
CC capping, and cell locomotion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation increases the actin-activated myosin ATPase
CC activity and thereby regulates the contractile activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: This chain binds calcium.
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DR EMBL; X05566; CAA29080.1; -; mRNA.
DR EMBL; X54616; CAB38864.1; -; Genomic_DNA.
DR EMBL; X54617; CAA38437.1; -; Genomic_DNA.
DR EMBL; Z32519; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A37100; A37100.
DR RefSeq; NP_001128489.1; NM_001135017.1.
DR RefSeq; XP_006245730.1; XM_006245668.3.
DR AlphaFoldDB; P13832; -.
DR SMR; P13832; -.
DR BioGRID; 272510; 1.
DR CORUM; P13832; -.
DR IntAct; P13832; 2.
DR MINT; P13832; -.
DR STRING; 10116.ENSRNOP00000021048; -.
DR iPTMnet; P13832; -.
DR PhosphoSitePlus; P13832; -.
DR jPOST; P13832; -.
DR PaxDb; P13832; -.
DR PRIDE; P13832; -.
DR Ensembl; ENSRNOT00000108694; ENSRNOP00000096383; ENSRNOG00000015278.
DR GeneID; 501203; -.
DR KEGG; rno:501203; -.
DR UCSC; RGD:1309537; rat.
DR CTD; 10627; -.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000153607; -.
DR HOGENOM; CLU_061288_9_3_1; -.
DR InParanoid; P13832; -.
DR OMA; MIQEEHL; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; P13832; -.
DR TreeFam; TF314218; -.
DR Reactome; R-RNO-3928664; Ephrin signaling.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR PRO; PR:P13832; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000015278; Expressed in lung and 20 other tissues.
DR Genevisible; P13832; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0032036; F:myosin heavy chain binding; IBA:GO_Central.
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; PF13405; EF-hand_6; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 2: Evidence at transcript level;
KW Calcium; Metal-binding; Motor protein; Muscle protein; Myosin;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..172
FT /note="Myosin regulatory light chain RLC-A"
FT /id="PRO_0000198739"
FT DOMAIN 29..64
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 98..133
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 134..169
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 19
FT /note="Phosphothreonine; by MLCK"
FT /evidence="ECO:0000250"
FT MOD_RES 20
FT /note="Phosphoserine; by MLCK"
FT /evidence="ECO:0000250"
SQ SEQUENCE 172 AA; 19895 MW; 50DB8144B916141A CRC64;
MSSKRAKTKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS
MGKNPTDEYL DAMMNEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEAIGTIQE
DYLRELLTTM GDRFTDEEVD ELYREAPIDK KGNFNYIEFT RILKHGAKDK DD
