ML12B_MOUSE
ID ML12B_MOUSE Reviewed; 172 AA.
AC Q3THE2; Q3TVH2; Q9CQL8;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Cerebellum, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, Colon, and Thyroid;
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 [3]
RP PROTEIN SEQUENCE OF 134-144, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH MYO19.
RX PubMed=24825904; DOI=10.1074/jbc.m114.569087;
RA Lu Z., Ma X.N., Zhang H.M., Ji H.H., Ding H., Zhang J., Luo D., Sun Y.,
RA Li X.D.;
RT "Mouse myosin-19 is a plus-end-directed, high-duty ratio molecular motor.";
RL J. Biol. Chem. 289:18535-18548(2014).
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. {ECO:0000269|PubMed:24825904}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE35646.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK002885; BAB22432.1; -; mRNA.
DR EMBL; AK005133; BAB23832.1; -; mRNA.
DR EMBL; AK146115; BAE26912.1; -; mRNA.
DR EMBL; AK160123; BAE35646.1; ALT_FRAME; mRNA.
DR EMBL; AK168316; BAE40255.1; -; mRNA.
DR EMBL; BC028878; AAH28878.1; -; mRNA.
DR EMBL; BC099425; AAH99425.1; -; mRNA.
DR EMBL; BC131925; AAI31926.1; -; mRNA.
DR EMBL; BC131927; AAI31928.1; -; mRNA.
DR CCDS; CCDS28954.1; -.
DR RefSeq; NP_075891.1; NM_023402.2.
DR AlphaFoldDB; Q3THE2; -.
DR SMR; Q3THE2; -.
DR BioGRID; 212551; 16.
DR DIP; DIP-31955N; -.
DR IntAct; Q3THE2; 19.
DR MINT; Q3THE2; -.
DR STRING; 10090.ENSMUSP00000042364; -.
DR iPTMnet; Q3THE2; -.
DR PhosphoSitePlus; Q3THE2; -.
DR SwissPalm; Q3THE2; -.
DR EPD; Q3THE2; -.
DR jPOST; Q3THE2; -.
DR MaxQB; Q3THE2; -.
DR PaxDb; Q3THE2; -.
DR PeptideAtlas; Q3THE2; -.
DR PRIDE; Q3THE2; -.
DR ProteomicsDB; 295679; -.
DR TopDownProteomics; Q3THE2; -.
DR DNASU; 67938; -.
DR Ensembl; ENSMUST00000038446; ENSMUSP00000042364; ENSMUSG00000034868.
DR Ensembl; ENSMUST00000233004; ENSMUSP00000156763; ENSMUSG00000034868.
DR Ensembl; ENSMUST00000233357; ENSMUSP00000156883; ENSMUSG00000117098.
DR GeneID; 67938; -.
DR KEGG; mmu:67938; -.
DR UCSC; uc008dlv.1; mouse.
DR CTD; 103910; -.
DR MGI; MGI:107494; Myl12b.
DR VEuPathDB; HostDB:ENSMUSG00000034868; -.
DR VEuPathDB; HostDB:ENSMUSG00000117098; -.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000153607; -.
DR HOGENOM; CLU_061288_9_3_1; -.
DR InParanoid; Q3THE2; -.
DR OMA; DAYLETM; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; Q3THE2; -.
DR TreeFam; TF314218; -.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR BioGRID-ORCS; 67938; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Myl12b; mouse.
DR PRO; PR:Q3THE2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3THE2; protein.
DR Bgee; ENSMUSG00000034868; Expressed in granulocyte and 108 other tissues.
DR ExpressionAtlas; Q3THE2; baseline and differential.
DR Genevisible; Q3THE2; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
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; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0032036; F:myosin heavy chain binding; IPI:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IMP:MGI.
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; Direct protein sequencing; Metal-binding; Motor protein;
KW Muscle protein; Myosin; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..172
FT /note="Myosin regulatory light chain 12B"
FT /id="PRO_0000284383"
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:0000250|UniProtKB:O14950"
FT MOD_RES 20
FT /note="Phosphoserine; by MLCK and ZIPK/DAPK3"
FT /evidence="ECO:0000250|UniProtKB:O14950"
FT CONFLICT 45
FT /note="R -> Q (in Ref. 1; BAE40255)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="G -> A (in Ref. 1; BAE35646)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="F -> V (in Ref. 1; BAE35646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 19779 MW; 78FF911630F3870B CRC64;
MSSKKAKTKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS
LGKNPTDAYL DAMMNEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEATGTIQE
DYLRELLTTM GDRFTDEEVD ELYREAPIDK KGNFNYIEFT RILKHGAKDK DD
