ML12B_RAT
ID ML12B_RAT Reviewed; 172 AA.
AC P18666; Q6P9V4;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Myosin regulatory light chain 12B;
DE AltName: Full=Myosin RLC-B;
DE AltName: Full=Myosin regulatory light chain 2-B, smooth muscle isoform;
DE Short=MLC-2;
DE AltName: Full=Myosin regulatory light chain 20 kDa;
DE Short=MLC20;
DE AltName: Full=Myosin regulatory light chain MRLC2;
GN Name=Myl12b; Synonyms=Mrlc2, Mrlcb, Mylc2b;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Liver;
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 [2]
RP SEQUENCE REVISION.
RA Grant J.W.;
RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION AT THR-19 AND SER-20 BY ZIPK/DAPK3.
RX PubMed=11384979; DOI=10.1074/jbc.m102753200;
RA Niiro N., Ikebe M.;
RT "Zipper-interacting protein kinase induces Ca(2+)-free smooth muscle
RT contraction via myosin light chain phosphorylation.";
RL J. Biol. Chem. 276:29567-29574(2001).
RN [5]
RP FUNCTION.
RX PubMed=18835913; DOI=10.1152/ajpheart.91437.2007;
RA Chen X., Pavlish K., Benoit J.N.;
RT "Myosin phosphorylation triggers actin polymerization in vascular smooth
RT muscle.";
RL Am. J. Physiol. 295:H2172-H2177(2008).
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. Phosphorylation triggers actin
CC polymerization in vascular smooth muscle. Implicated in cytokinesis,
CC receptor capping, and cell locomotion. {ECO:0000269|PubMed:18835913}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains:
CC interacts with myosin heavy chain MYO19.
CC {ECO:0000250|UniProtKB:Q3THE2}.
CC -!- PTM: Phosphorylation increases the actin-activated myosin ATPase
CC activity and thereby regulates the contractile activity. It is required
CC to generate the driving force in the migration of the cells but not
CC necessary for localization of myosin-2 at the leading edge.
CC Phosphorylation is reduced following epigallocatechin-3-O-gallate
CC treatment. {ECO:0000250|UniProtKB:O14950}.
CC -!- MISCELLANEOUS: This chain binds calcium.
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DR EMBL; X52840; CAA37024.1; -; mRNA.
DR EMBL; BC060577; AAH60577.1; -; mRNA.
DR PIR; B37100; B37100.
DR PIR; S11632; S11632.
DR RefSeq; NP_059039.2; NM_017343.2.
DR AlphaFoldDB; P18666; -.
DR SMR; P18666; -.
DR BioGRID; 248423; 3.
DR CORUM; P18666; -.
DR IntAct; P18666; 3.
DR STRING; 10116.ENSRNOP00000045992; -.
DR iPTMnet; P18666; -.
DR PhosphoSitePlus; P18666; -.
DR jPOST; P18666; -.
DR PaxDb; P18666; -.
DR PRIDE; P18666; -.
DR GeneID; 50685; -.
DR KEGG; rno:50685; -.
DR CTD; 103910; -.
DR RGD; 628855; Myl12b.
DR eggNOG; KOG0031; Eukaryota.
DR InParanoid; P18666; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; P18666; -.
DR TreeFam; TF314218; -.
DR BRENDA; 2.7.11.18; 5301.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR Reactome; R-RNO-5627123; RHO GTPases activate PAKs.
DR PRO; PR:P18666; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0032036; F:myosin heavy chain binding; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR015070; EF_hand_DJBP.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF08976; EF-hand_11; 1.
DR Pfam; PF13405; EF-hand_6; 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 1: Evidence at protein 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 12B"
FT /id="PRO_0000198740"
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 and ZIPK/DAPK3"
FT /evidence="ECO:0000269|PubMed:11384979"
FT MOD_RES 20
FT /note="Phosphoserine; by MLCK and ZIPK/DAPK3"
FT /evidence="ECO:0000269|PubMed:11384979"
FT CONFLICT 80
FT /note="R -> P (in Ref. 3; AAH60577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 19838 MW; 4D9CC47632D1852B CRC64;
MSSKKAKTKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS
LGKNPTDAYL DAMMNEAPGR INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEATGTIQE
DYLRELLTTM GDRFTDEEVD ELYREAPIDK KGNFNYIEFT RILKHGAKDK DD
