ID   ML12B_BOVIN             Reviewed;         171 AA.
AC   A4IF97;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Myosin regulatory light chain 12B;
DE   AltName: Full=Myosin regulatory light chain 2-B, smooth muscle isoform;
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, MYLC2B;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons, and Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:O14950}.
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. {ECO:0000250}.
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DR   EMBL; BC134471; AAI34472.1; -; mRNA.
DR   EMBL; BC142028; AAI42029.1; -; mRNA.
DR   RefSeq; NP_001077233.1; NM_001083764.2.
DR   AlphaFoldDB; A4IF97; -.
DR   SMR; A4IF97; -.
DR   STRING; 9913.ENSBTAP00000037091; -.
DR   PaxDb; A4IF97; -.
DR   PeptideAtlas; A4IF97; -.
DR   PRIDE; A4IF97; -.
DR   Ensembl; ENSBTAT00000037254; ENSBTAP00000037091; ENSBTAG00000026266.
DR   GeneID; 614055; -.
DR   KEGG; bta:614055; -.
DR   CTD; 103910; -.
DR   VEuPathDB; HostDB:ENSBTAG00000026266; -.
DR   eggNOG; KOG0031; Eukaryota.
DR   GeneTree; ENSGT00940000153607; -.
DR   HOGENOM; CLU_061288_9_3_1; -.
DR   InParanoid; A4IF97; -.
DR   OMA; MIQEEHL; -.
DR   OrthoDB; 1435392at2759; -.
DR   TreeFam; TF314218; -.
DR   Proteomes; UP000009136; Chromosome 24.
DR   Bgee; ENSBTAG00000026266; Expressed in abomasum and 103 other tissues.
DR   GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR   GO; GO:0005903; C:brush border; IEA:Ensembl.
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; IBA:GO_Central.
DR   GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0032036; F:myosin heavy chain binding; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Calcium; Metal-binding; Motor protein; Muscle protein; Myosin;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..171
FT                   /note="Myosin regulatory light chain 12B"
FT                   /id="PRO_0000349363"
FT   DOMAIN          28..63
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          97..132
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          133..168
FT                   /note="EF-hand 3"
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         43
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         45
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         52
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         18
FT                   /note="Phosphothreonine; by MLCK and ZIPK/DAPK3"
FT                   /evidence="ECO:0000250|UniProtKB:O14950"
FT   MOD_RES         19
FT                   /note="Phosphoserine; by MLCK and ZIPK/DAPK3"
FT                   /evidence="ECO:0000250|UniProtKB:O14950"
SQ   SEQUENCE   171 AA;  19692 MW;  E32E32610466BB56 CRC64;
     MSSKKAKTKT KKRPQRATSN VFAMFDQSQI QEFKEAFNMI DQNRDGFIDK EDLHDMLASL
     GKNPTDAYLE AMMNEAPGPI NFTMFLTMFG EKLNGTDPED VIRNAFACFD EEATGTIQED
     YLRELLTTMG DRFTDEEVDE LYREAPIDKK GNFNYIEFTR ILKHGAKDKD D