Full text data of MYL12B
MYL12B
(MRLC2, MYLC2B)
[Confidence: high (present in two of the MS resources)]
Myosin regulatory light chain 12B (MLC-2A; MLC-2; Myosin regulatory light chain 2-B, smooth muscle isoform; Myosin regulatory light chain 20 kDa; MLC20; Myosin regulatory light chain MRLC2; SHUJUN-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Myosin regulatory light chain 12B (MLC-2A; MLC-2; Myosin regulatory light chain 2-B, smooth muscle isoform; Myosin regulatory light chain 20 kDa; MLC20; Myosin regulatory light chain MRLC2; SHUJUN-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00033494
IPI00033494 Myosin regulatory light chain Myosin regulatory light chain membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a not mentioned n/a expected molecular weight found in band ~ 62 kDa
IPI00033494 Myosin regulatory light chain Myosin regulatory light chain membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a not mentioned n/a expected molecular weight found in band ~ 62 kDa
UniProt
O14950
ID ML12B_HUMAN Reviewed; 172 AA.
AC O14950; D3DUH6; Q13182; Q7Z5Z4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Myosin regulatory light chain 12B;
DE AltName: Full=MLC-2A;
DE Short=MLC-2;
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;
DE AltName: Full=SHUJUN-1;
GN Name=MYL12B; Synonyms=MRLC2, MYLC2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-19 AND SER-20, AND
RP MUTAGENESIS OF 19-THR-SER-20.
RX PubMed=11942626; DOI=10.1247/csf.26.677;
RA Iwasaki T., Murata-Hori M., Ishitobi S., Hosoya H.;
RT "Diphosphorylated MRLC is required for organization of stress fibers
RT in interphase cells and the contractile ring in dividing cells.";
RL Cell Struct. Funct. 26:677-683(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11436981; DOI=10.1540/jsmr.37.25;
RA Watanabe M., Kohri M., Takaishi M., Horie R., Higashihara M.;
RT "Molecular cloning and sequencing of myosin light chains in human
RT megakaryoblastic leukemia cells.";
RL J. Smooth Muscle Res. 37:25-38(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S.,
RA Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M.,
RA Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E.,
RA Hirai Y.;
RT "Molecular cloning of a novel human myosin regulatory light chain.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Brodie S.G., Rubin S.E., Montoya G.D., Garry P.J., Williams T.M.;
RT "Human myosin regulatory light chain cDNA homologous to the rat myosin
RT regulatory light chain B (MLC-B).";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Nasopharyngeal carcinoma;
RA Shu J., Li G., He X.;
RT "Construction of cDNA expression library from nasopharyngeal carcinoma
RT tissue and screening of antigenic genes.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION.
RX PubMed=10965042;
RA Suizu F., Ueda K., Iwasaki T., Murata-Hori M., Hosoya H.;
RT "Activation of actin-activated MgATPase activity of myosin II by
RT phosphorylation with MAPK-activated protein kinase-1b (RSK-2).";
RL J. Biochem. 128:435-440(2000).
RN [10]
RP PHOSPHORYLATION AT THR-19 AND SER-20, AND MUTAGENESIS OF
RP 19-THR-SER-20.
RX PubMed=12429016; DOI=10.1042/BJ20021559;
RA Fumoto K., Uchimura T., Iwasaki T., Ueda K., Hosoya H.;
RT "Phosphorylation of myosin II regulatory light chain is necessary for
RT migration of HeLa cells but not for localization of myosin II at the
RT leading edge.";
RL Biochem. J. 370:551-556(2003).
RN [11]
RP MUTAGENESIS OF 19-THR-SER-20.
RX PubMed=12589046; DOI=10.1091/mbc.E02-04-0214;
RA Duran J.M., Valderrama F., Castel S., Magdalena J., Tomas M.,
RA Hosoya H., Renau-Piqueras J., Malhotra V., Egea G.;
RT "Myosin motors and not actin comets are mediators of the actin-based
RT Golgi-to-endoplasmic reticulum protein transport.";
RL Mol. Biol. Cell 14:445-459(2003).
RN [12]
RP PHOSPHORYLATION AT THR-19 AND SER-20.
RX PubMed=15946647; DOI=10.1016/j.bbrc.2005.05.108;
RA Umeda D., Tachibana H., Yamada K.;
RT "Epigallocatechin-3-O-gallate disrupts stress fibers and the
RT contractile ring by reducing myosin regulatory light chain
RT phosphorylation mediated through the target molecule 67 kDa laminin
RT receptor.";
RL Biochem. Biophys. Res. Commun. 333:628-635(2005).
RN [13]
RP PHOSPHORYLATION BY ZIPK/DAPK3.
RX PubMed=17126281; DOI=10.1016/j.abb.2006.09.026;
RA Takamoto N., Komatsu S., Komaba S., Niiro N., Ikebe M.;
RT "Novel ZIP kinase isoform lacks leucine zipper.";
RL Arch. Biochem. Biophys. 456:194-203(2006).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=18480596; DOI=10.1540/jsmr.44.29;
RA Higashihara M., Watanabe M., Usuda S., Miyazaki K.;
RT "Smooth muscle type isoform of 20 kDa myosin light chain is expressed
RT in monocyte/macrophage cell lineage.";
RL J. Smooth Muscle Res. 44:29-40(2008).
CC -!- FUNCTION: Myosin regulatory subunit that plays an important role
CC in 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
CC cytokinesis, receptor capping, and cell locomotion (By
CC similarity).
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC -!- INTERACTION:
CC P60709:ACTB; NbExp=3; IntAct=EBI-1642165, EBI-353944;
CC P35749:MYH11; NbExp=2; IntAct=EBI-1642165, EBI-1052928;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in various
CC hematopoietic cells.
CC -!- PTM: Phosphorylation increases the actin-activated myosin ATPase
CC activity and thereby regulates the contractile activity. It is
CC required to generate the driving force in the migration of the
CC cells but not necessary for localization of myosin-2 at the
CC leading edge. Phosphorylation is reduced following
CC epigallocatechin-3-O-gallate treatment.
CC -!- MISCELLANEOUS: This chain binds calcium (By similarity).
CC -!- SIMILARITY: Contains 3 EF-hand domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP73808.1; Type=Frameshift; Positions=4;
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DR EMBL; D82058; BAB88918.1; -; mRNA.
DR EMBL; AB046614; BAB62403.1; -; mRNA.
DR EMBL; D50372; BAA23323.1; -; mRNA.
DR EMBL; U26162; AAA67367.1; -; mRNA.
DR EMBL; AY320408; AAP73808.1; ALT_FRAME; mRNA.
DR EMBL; AK291726; BAF84415.1; -; mRNA.
DR EMBL; CH471113; EAX01675.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01676.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01677.1; -; Genomic_DNA.
DR EMBL; BC004994; AAH04994.1; -; mRNA.
DR RefSeq; NP_001138416.1; NM_001144944.1.
DR RefSeq; NP_001138417.1; NM_001144945.1.
DR RefSeq; NP_291024.1; NM_033546.3.
DR RefSeq; XP_005258132.1; XM_005258075.1.
DR UniGene; Hs.190086; -.
DR UniGene; Hs.464472; -.
DR ProteinModelPortal; O14950; -.
DR SMR; O14950; 26-168.
DR IntAct; O14950; 11.
DR STRING; 9606.ENSP00000237500; -.
DR PhosphoSite; O14950; -.
DR PaxDb; O14950; -.
DR PeptideAtlas; O14950; -.
DR PRIDE; O14950; -.
DR Ensembl; ENST00000237500; ENSP00000237500; ENSG00000118680.
DR Ensembl; ENST00000400175; ENSP00000383037; ENSG00000118680.
DR Ensembl; ENST00000581193; ENSP00000463559; ENSG00000118680.
DR Ensembl; ENST00000584539; ENSP00000464464; ENSG00000118680.
DR GeneID; 103910; -.
DR KEGG; hsa:103910; -.
DR UCSC; uc002klt.4; human.
DR CTD; 103910; -.
DR GeneCards; GC18P003254; -.
DR H-InvDB; HIX0014302; -.
DR HGNC; HGNC:29827; MYL12B.
DR HPA; HPA045244; -.
DR neXtProt; NX_O14950; -.
DR PharmGKB; PA164723274; -.
DR eggNOG; COG5126; -.
DR HOGENOM; HOG000233018; -.
DR InParanoid; O14950; -.
DR KO; K12757; -.
DR OMA; NEEHLRE; -.
DR OrthoDB; EOG7992RX; -.
DR PhylomeDB; O14950; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_17044; Muscle contraction.
DR GenomeRNAi; 103910; -.
DR NextBio; 78567; -.
DR PRO; PR:O14950; -.
DR Bgee; O14950; -.
DR Genevestigator; O14950; -.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016460; C:myosin II complex; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0006936; P:muscle contraction; TAS:Reactome.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR Gene3D; 1.10.238.10; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Complete proteome; Metal-binding; Motor protein;
KW Muscle protein; Myosin; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 172 Myosin regulatory light chain 12B.
FT /FTId=PRO_0000349364.
FT DOMAIN 29 64 EF-hand 1.
FT DOMAIN 98 133 EF-hand 2.
FT DOMAIN 134 169 EF-hand 3.
FT CA_BIND 42 53 Potential.
FT MOD_RES 19 19 Phosphothreonine; by MLCK and ZIPK/DAPK3.
FT MOD_RES 20 20 Phosphoserine; by MLCK and ZIPK/DAPK3.
FT VARIANT 141 141 E -> G (in dbSNP:rs14720).
FT /FTId=VAR_046371.
FT MUTAGEN 19 20 TS->AA: Shows a decrease in the number of
FT actin filament bundles.
FT MUTAGEN 19 20 TS->DD: Shows a larger number of actin
FT filament bundles.
FT CONFLICT 72 72 A -> V (in Ref. 5; AAP73808).
FT CONFLICT 89 89 M -> T (in Ref. 5; AAP73808).
FT CONFLICT 104 104 R -> G (in Ref. 5; AAP73808).
FT CONFLICT 138 138 E -> G (in Ref. 3; BAA23323).
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
//
ID ML12B_HUMAN Reviewed; 172 AA.
AC O14950; D3DUH6; Q13182; Q7Z5Z4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Myosin regulatory light chain 12B;
DE AltName: Full=MLC-2A;
DE Short=MLC-2;
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;
DE AltName: Full=SHUJUN-1;
GN Name=MYL12B; Synonyms=MRLC2, MYLC2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-19 AND SER-20, AND
RP MUTAGENESIS OF 19-THR-SER-20.
RX PubMed=11942626; DOI=10.1247/csf.26.677;
RA Iwasaki T., Murata-Hori M., Ishitobi S., Hosoya H.;
RT "Diphosphorylated MRLC is required for organization of stress fibers
RT in interphase cells and the contractile ring in dividing cells.";
RL Cell Struct. Funct. 26:677-683(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11436981; DOI=10.1540/jsmr.37.25;
RA Watanabe M., Kohri M., Takaishi M., Horie R., Higashihara M.;
RT "Molecular cloning and sequencing of myosin light chains in human
RT megakaryoblastic leukemia cells.";
RL J. Smooth Muscle Res. 37:25-38(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S.,
RA Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M.,
RA Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E.,
RA Hirai Y.;
RT "Molecular cloning of a novel human myosin regulatory light chain.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Brodie S.G., Rubin S.E., Montoya G.D., Garry P.J., Williams T.M.;
RT "Human myosin regulatory light chain cDNA homologous to the rat myosin
RT regulatory light chain B (MLC-B).";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Nasopharyngeal carcinoma;
RA Shu J., Li G., He X.;
RT "Construction of cDNA expression library from nasopharyngeal carcinoma
RT tissue and screening of antigenic genes.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION.
RX PubMed=10965042;
RA Suizu F., Ueda K., Iwasaki T., Murata-Hori M., Hosoya H.;
RT "Activation of actin-activated MgATPase activity of myosin II by
RT phosphorylation with MAPK-activated protein kinase-1b (RSK-2).";
RL J. Biochem. 128:435-440(2000).
RN [10]
RP PHOSPHORYLATION AT THR-19 AND SER-20, AND MUTAGENESIS OF
RP 19-THR-SER-20.
RX PubMed=12429016; DOI=10.1042/BJ20021559;
RA Fumoto K., Uchimura T., Iwasaki T., Ueda K., Hosoya H.;
RT "Phosphorylation of myosin II regulatory light chain is necessary for
RT migration of HeLa cells but not for localization of myosin II at the
RT leading edge.";
RL Biochem. J. 370:551-556(2003).
RN [11]
RP MUTAGENESIS OF 19-THR-SER-20.
RX PubMed=12589046; DOI=10.1091/mbc.E02-04-0214;
RA Duran J.M., Valderrama F., Castel S., Magdalena J., Tomas M.,
RA Hosoya H., Renau-Piqueras J., Malhotra V., Egea G.;
RT "Myosin motors and not actin comets are mediators of the actin-based
RT Golgi-to-endoplasmic reticulum protein transport.";
RL Mol. Biol. Cell 14:445-459(2003).
RN [12]
RP PHOSPHORYLATION AT THR-19 AND SER-20.
RX PubMed=15946647; DOI=10.1016/j.bbrc.2005.05.108;
RA Umeda D., Tachibana H., Yamada K.;
RT "Epigallocatechin-3-O-gallate disrupts stress fibers and the
RT contractile ring by reducing myosin regulatory light chain
RT phosphorylation mediated through the target molecule 67 kDa laminin
RT receptor.";
RL Biochem. Biophys. Res. Commun. 333:628-635(2005).
RN [13]
RP PHOSPHORYLATION BY ZIPK/DAPK3.
RX PubMed=17126281; DOI=10.1016/j.abb.2006.09.026;
RA Takamoto N., Komatsu S., Komaba S., Niiro N., Ikebe M.;
RT "Novel ZIP kinase isoform lacks leucine zipper.";
RL Arch. Biochem. Biophys. 456:194-203(2006).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=18480596; DOI=10.1540/jsmr.44.29;
RA Higashihara M., Watanabe M., Usuda S., Miyazaki K.;
RT "Smooth muscle type isoform of 20 kDa myosin light chain is expressed
RT in monocyte/macrophage cell lineage.";
RL J. Smooth Muscle Res. 44:29-40(2008).
CC -!- FUNCTION: Myosin regulatory subunit that plays an important role
CC in 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
CC cytokinesis, receptor capping, and cell locomotion (By
CC similarity).
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC -!- INTERACTION:
CC P60709:ACTB; NbExp=3; IntAct=EBI-1642165, EBI-353944;
CC P35749:MYH11; NbExp=2; IntAct=EBI-1642165, EBI-1052928;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in various
CC hematopoietic cells.
CC -!- PTM: Phosphorylation increases the actin-activated myosin ATPase
CC activity and thereby regulates the contractile activity. It is
CC required to generate the driving force in the migration of the
CC cells but not necessary for localization of myosin-2 at the
CC leading edge. Phosphorylation is reduced following
CC epigallocatechin-3-O-gallate treatment.
CC -!- MISCELLANEOUS: This chain binds calcium (By similarity).
CC -!- SIMILARITY: Contains 3 EF-hand domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP73808.1; Type=Frameshift; Positions=4;
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DR EMBL; D82058; BAB88918.1; -; mRNA.
DR EMBL; AB046614; BAB62403.1; -; mRNA.
DR EMBL; D50372; BAA23323.1; -; mRNA.
DR EMBL; U26162; AAA67367.1; -; mRNA.
DR EMBL; AY320408; AAP73808.1; ALT_FRAME; mRNA.
DR EMBL; AK291726; BAF84415.1; -; mRNA.
DR EMBL; CH471113; EAX01675.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01676.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01677.1; -; Genomic_DNA.
DR EMBL; BC004994; AAH04994.1; -; mRNA.
DR RefSeq; NP_001138416.1; NM_001144944.1.
DR RefSeq; NP_001138417.1; NM_001144945.1.
DR RefSeq; NP_291024.1; NM_033546.3.
DR RefSeq; XP_005258132.1; XM_005258075.1.
DR UniGene; Hs.190086; -.
DR UniGene; Hs.464472; -.
DR ProteinModelPortal; O14950; -.
DR SMR; O14950; 26-168.
DR IntAct; O14950; 11.
DR STRING; 9606.ENSP00000237500; -.
DR PhosphoSite; O14950; -.
DR PaxDb; O14950; -.
DR PeptideAtlas; O14950; -.
DR PRIDE; O14950; -.
DR Ensembl; ENST00000237500; ENSP00000237500; ENSG00000118680.
DR Ensembl; ENST00000400175; ENSP00000383037; ENSG00000118680.
DR Ensembl; ENST00000581193; ENSP00000463559; ENSG00000118680.
DR Ensembl; ENST00000584539; ENSP00000464464; ENSG00000118680.
DR GeneID; 103910; -.
DR KEGG; hsa:103910; -.
DR UCSC; uc002klt.4; human.
DR CTD; 103910; -.
DR GeneCards; GC18P003254; -.
DR H-InvDB; HIX0014302; -.
DR HGNC; HGNC:29827; MYL12B.
DR HPA; HPA045244; -.
DR neXtProt; NX_O14950; -.
DR PharmGKB; PA164723274; -.
DR eggNOG; COG5126; -.
DR HOGENOM; HOG000233018; -.
DR InParanoid; O14950; -.
DR KO; K12757; -.
DR OMA; NEEHLRE; -.
DR OrthoDB; EOG7992RX; -.
DR PhylomeDB; O14950; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_17044; Muscle contraction.
DR GenomeRNAi; 103910; -.
DR NextBio; 78567; -.
DR PRO; PR:O14950; -.
DR Bgee; O14950; -.
DR Genevestigator; O14950; -.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016460; C:myosin II complex; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0006936; P:muscle contraction; TAS:Reactome.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR Gene3D; 1.10.238.10; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Complete proteome; Metal-binding; Motor protein;
KW Muscle protein; Myosin; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 172 Myosin regulatory light chain 12B.
FT /FTId=PRO_0000349364.
FT DOMAIN 29 64 EF-hand 1.
FT DOMAIN 98 133 EF-hand 2.
FT DOMAIN 134 169 EF-hand 3.
FT CA_BIND 42 53 Potential.
FT MOD_RES 19 19 Phosphothreonine; by MLCK and ZIPK/DAPK3.
FT MOD_RES 20 20 Phosphoserine; by MLCK and ZIPK/DAPK3.
FT VARIANT 141 141 E -> G (in dbSNP:rs14720).
FT /FTId=VAR_046371.
FT MUTAGEN 19 20 TS->AA: Shows a decrease in the number of
FT actin filament bundles.
FT MUTAGEN 19 20 TS->DD: Shows a larger number of actin
FT filament bundles.
FT CONFLICT 72 72 A -> V (in Ref. 5; AAP73808).
FT CONFLICT 89 89 M -> T (in Ref. 5; AAP73808).
FT CONFLICT 104 104 R -> G (in Ref. 5; AAP73808).
FT CONFLICT 138 138 E -> G (in Ref. 3; BAA23323).
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
//