Full text data of MYL12A
MYL12A
(MLCB, MRLC3, RLC)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Myosin regulatory light chain 12A (MLC-2B; Myosin RLC; Myosin regulatory light chain 2, nonsarcomeric; Myosin regulatory light chain MRLC3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Myosin regulatory light chain 12A (MLC-2B; Myosin RLC; Myosin regulatory light chain 2, nonsarcomeric; Myosin regulatory light chain MRLC3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P19105
ID ML12A_HUMAN Reviewed; 171 AA.
AC P19105;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Myosin regulatory light chain 12A;
DE AltName: Full=MLC-2B;
DE AltName: Full=Myosin RLC;
DE AltName: Full=Myosin regulatory light chain 2, nonsarcomeric;
DE AltName: Full=Myosin regulatory light chain MRLC3;
GN Name=MYL12A; Synonyms=MLCB, MRLC3, RLC;
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].
RC TISSUE=Placenta;
RX PubMed=2216787; DOI=10.1093/nar/18.19.5892;
RA Grant J.W., Zhong R.Q., McEwen P., Church S.L.;
RT "Human nonsarcomeric 20,000 Da myosin regulatory light chain cDNA.";
RL Nucleic Acids Res. 18:5892-5892(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle, Skin, and Testis;
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).
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. Implicated in cytokinesis,
CC receptor capping, and cell locomotion (By similarity).
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC -!- INTERACTION:
CC Q62868:Rock2 (xeno); NbExp=2; IntAct=EBI-354418, EBI-1569209;
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 (By similarity).
CC -!- MISCELLANEOUS: This chain binds calcium.
CC -!- SIMILARITY: Contains 3 EF-hand domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X54304; CAA38201.1; -; mRNA.
DR EMBL; BC016372; AAH16372.1; -; mRNA.
DR EMBL; BC031972; AAH31972.1; -; mRNA.
DR EMBL; BC032748; AAH32748.1; -; mRNA.
DR PIR; S11493; MOHULP.
DR RefSeq; NP_006462.1; NM_006471.2.
DR RefSeq; XP_005258133.1; XM_005258076.1.
DR RefSeq; XP_005258135.1; XM_005258078.1.
DR UniGene; Hs.190086; -.
DR ProteinModelPortal; P19105; -.
DR SMR; P19105; 25-167.
DR IntAct; P19105; 19.
DR MINT; MINT-1159148; -.
DR STRING; 9606.ENSP00000217652; -.
DR PhosphoSite; P19105; -.
DR DMDM; 127169; -.
DR OGP; P19105; -.
DR SWISS-2DPAGE; P19105; -.
DR PaxDb; P19105; -.
DR PRIDE; P19105; -.
DR DNASU; 10627; -.
DR Ensembl; ENST00000217652; ENSP00000217652; ENSG00000101608.
DR Ensembl; ENST00000536605; ENSP00000441231; ENSG00000101608.
DR Ensembl; ENST00000578611; ENSP00000463614; ENSG00000101608.
DR Ensembl; ENST00000579226; ENSP00000462171; ENSG00000101608.
DR GeneID; 10627; -.
DR KEGG; hsa:10627; -.
DR UCSC; uc002klr.3; human.
DR CTD; 10627; -.
DR GeneCards; GC18P003238; -.
DR HGNC; HGNC:16701; MYL12A.
DR HPA; CAB004503; -.
DR HPA; HPA045244; -.
DR MIM; 609211; gene.
DR neXtProt; NX_P19105; -.
DR PharmGKB; PA164723273; -.
DR eggNOG; COG5126; -.
DR HOGENOM; HOG000233018; -.
DR InParanoid; P19105; -.
DR KO; K12757; -.
DR OrthoDB; EOG7992RX; -.
DR PhylomeDB; P19105; -.
DR ChiTaRS; MYL12A; human.
DR GeneWiki; MRCL3; -.
DR GenomeRNAi; 10627; -.
DR NextBio; 40378; -.
DR PRO; PR:P19105; -.
DR ArrayExpress; P19105; -.
DR Bgee; P19105; -.
DR Genevestigator; P19105; -.
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:0072661; P:protein targeting to plasma membrane; IEA:Ensembl.
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; PF00036; EF-hand_1; 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; Reference proteome; Repeat.
FT CHAIN 1 171 Myosin regulatory light chain 12A.
FT /FTId=PRO_0000198733.
FT DOMAIN 28 63 EF-hand 1.
FT DOMAIN 97 132 EF-hand 2.
FT DOMAIN 133 168 EF-hand 3.
FT CA_BIND 41 52
FT MOD_RES 18 18 Phosphothreonine; by MLCK.
SQ SEQUENCE 171 AA; 19794 MW; C871AA881BF5C215 CRC64;
MSSKRTKTKT KKRPQRATSN VFAMFDQSQI QEFKEAFNMI DQNRDGFIDK EDLHDMLASL
GKNPTDEYLD AMMNEAPGPI NFTMFLTMFG EKLNGTDPED VIRNAFACFD EEATGTIQED
YLRELLTTMG DRFTDEEVDE LYREAPIDKK GNFNYIEFTR ILKHGAKDKD D
//
ID ML12A_HUMAN Reviewed; 171 AA.
AC P19105;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Myosin regulatory light chain 12A;
DE AltName: Full=MLC-2B;
DE AltName: Full=Myosin RLC;
DE AltName: Full=Myosin regulatory light chain 2, nonsarcomeric;
DE AltName: Full=Myosin regulatory light chain MRLC3;
GN Name=MYL12A; Synonyms=MLCB, MRLC3, RLC;
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].
RC TISSUE=Placenta;
RX PubMed=2216787; DOI=10.1093/nar/18.19.5892;
RA Grant J.W., Zhong R.Q., McEwen P., Church S.L.;
RT "Human nonsarcomeric 20,000 Da myosin regulatory light chain cDNA.";
RL Nucleic Acids Res. 18:5892-5892(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle, Skin, and Testis;
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).
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. Implicated in cytokinesis,
CC receptor capping, and cell locomotion (By similarity).
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC -!- INTERACTION:
CC Q62868:Rock2 (xeno); NbExp=2; IntAct=EBI-354418, EBI-1569209;
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 (By similarity).
CC -!- MISCELLANEOUS: This chain binds calcium.
CC -!- SIMILARITY: Contains 3 EF-hand domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X54304; CAA38201.1; -; mRNA.
DR EMBL; BC016372; AAH16372.1; -; mRNA.
DR EMBL; BC031972; AAH31972.1; -; mRNA.
DR EMBL; BC032748; AAH32748.1; -; mRNA.
DR PIR; S11493; MOHULP.
DR RefSeq; NP_006462.1; NM_006471.2.
DR RefSeq; XP_005258133.1; XM_005258076.1.
DR RefSeq; XP_005258135.1; XM_005258078.1.
DR UniGene; Hs.190086; -.
DR ProteinModelPortal; P19105; -.
DR SMR; P19105; 25-167.
DR IntAct; P19105; 19.
DR MINT; MINT-1159148; -.
DR STRING; 9606.ENSP00000217652; -.
DR PhosphoSite; P19105; -.
DR DMDM; 127169; -.
DR OGP; P19105; -.
DR SWISS-2DPAGE; P19105; -.
DR PaxDb; P19105; -.
DR PRIDE; P19105; -.
DR DNASU; 10627; -.
DR Ensembl; ENST00000217652; ENSP00000217652; ENSG00000101608.
DR Ensembl; ENST00000536605; ENSP00000441231; ENSG00000101608.
DR Ensembl; ENST00000578611; ENSP00000463614; ENSG00000101608.
DR Ensembl; ENST00000579226; ENSP00000462171; ENSG00000101608.
DR GeneID; 10627; -.
DR KEGG; hsa:10627; -.
DR UCSC; uc002klr.3; human.
DR CTD; 10627; -.
DR GeneCards; GC18P003238; -.
DR HGNC; HGNC:16701; MYL12A.
DR HPA; CAB004503; -.
DR HPA; HPA045244; -.
DR MIM; 609211; gene.
DR neXtProt; NX_P19105; -.
DR PharmGKB; PA164723273; -.
DR eggNOG; COG5126; -.
DR HOGENOM; HOG000233018; -.
DR InParanoid; P19105; -.
DR KO; K12757; -.
DR OrthoDB; EOG7992RX; -.
DR PhylomeDB; P19105; -.
DR ChiTaRS; MYL12A; human.
DR GeneWiki; MRCL3; -.
DR GenomeRNAi; 10627; -.
DR NextBio; 40378; -.
DR PRO; PR:P19105; -.
DR ArrayExpress; P19105; -.
DR Bgee; P19105; -.
DR Genevestigator; P19105; -.
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:0072661; P:protein targeting to plasma membrane; IEA:Ensembl.
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; PF00036; EF-hand_1; 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; Reference proteome; Repeat.
FT CHAIN 1 171 Myosin regulatory light chain 12A.
FT /FTId=PRO_0000198733.
FT DOMAIN 28 63 EF-hand 1.
FT DOMAIN 97 132 EF-hand 2.
FT DOMAIN 133 168 EF-hand 3.
FT CA_BIND 41 52
FT MOD_RES 18 18 Phosphothreonine; by MLCK.
SQ SEQUENCE 171 AA; 19794 MW; C871AA881BF5C215 CRC64;
MSSKRTKTKT KKRPQRATSN VFAMFDQSQI QEFKEAFNMI DQNRDGFIDK EDLHDMLASL
GKNPTDEYLD AMMNEAPGPI NFTMFLTMFG EKLNGTDPED VIRNAFACFD EEATGTIQED
YLRELLTTMG DRFTDEEVDE LYREAPIDKK GNFNYIEFTR ILKHGAKDKD D
//
MIM
609211
*RECORD*
*FIELD* NO
609211
*FIELD* TI
*609211 MYOSIN, LIGHT CHAIN 12B, REGULATORY; MYL12B
;;MYOSIN REGULATORY LIGHT CHAIN 2; MRLC2
read more*FIELD* TX
DESCRIPTION
The activity of nonmuscle myosin II (see MYH9; 160775) is regulated by
phosphorylation of a regulatory light chain, such as MRLC2. This
phosphorylation results in higher MgATPase activity and the assembly of
myosin II filaments (Iwasaki et al., 2001).
CLONING
Grant et al. (1990) cloned MRLC2 from a placenta cDNA library. The
deduced protein contains 171 amino acids.
Using primers designed from chicken Mrlc, Iwasaki et al. (2001)
amplified MRLC2 from a HeLa cell cDNA library. The deduced 172-amino
acid protein contains thr18 and ser19, which are conserved
phosphorylation sites in myosin regulatory light chains.
GENE FUNCTION
Diphosphorylation of MRLCs on thr18 and ser19 results in higher MgATPase
activity and myosin filament formation than monophosphorylation at ser19
in vitro. By site-directed mutagenesis, Iwasaki et al. (2001) created
MRLC2 mutants that mimicked diphosphorylated, monophosphorylated, and
unphosphorylated forms of MRLC2. Overexpression of the diphosphorylated
form, and to a lesser degree the monophosphorylated form, caused the
formation of a large number of actin filament bundles in transfected
HeLa cells. Overexpression of the unphosphorylated form caused a
decrease in the number of actin filament bundles. Immunolocalization of
the mutant proteins in dividing cells revealed colocalization of the 2
phosphorylated forms with actin filaments in the peripheral region and
with the contractile ring, while the unphosphorylated form localized
diffusely throughout the cytoplasm. Iwasaki et al. (2001) concluded that
phosphorylation of MRLC2 is required for organization of stress fibers
in interphase cells and the contractile ring in dividing cells. They
suggested that diphosphorylated MRLC may be more effective in organizing
actin filaments than monophosphorylated MRLC.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the MYL12B
gene to chromosome 18 (TMAP SHGC-12353).
*FIELD* RF
1. Grant, J. W.; Zhong, R. Q.; McEwen, P. M.; Church, S. L.: Human
nonsarcomeric 20,000 Da myosin regulatory light chain cDNA. Nucleic
Acids Res. 18: 5892 only, 1990.
2. Iwasaki, T.; Murata-Hori, M.; Ishitobi, S.; Hosoya, H.: Diphosphorylated
MRLC is required for organization of stress fibers in interphase cells
and the contractile ring in dividing cells. Cell Struct. Func. 26:
677-683, 2001.
*FIELD* CD
Patricia A. Hartz: 2/18/2005
*FIELD* ED
alopez: 06/25/2009
mgross: 2/18/2005
*RECORD*
*FIELD* NO
609211
*FIELD* TI
*609211 MYOSIN, LIGHT CHAIN 12B, REGULATORY; MYL12B
;;MYOSIN REGULATORY LIGHT CHAIN 2; MRLC2
read more*FIELD* TX
DESCRIPTION
The activity of nonmuscle myosin II (see MYH9; 160775) is regulated by
phosphorylation of a regulatory light chain, such as MRLC2. This
phosphorylation results in higher MgATPase activity and the assembly of
myosin II filaments (Iwasaki et al., 2001).
CLONING
Grant et al. (1990) cloned MRLC2 from a placenta cDNA library. The
deduced protein contains 171 amino acids.
Using primers designed from chicken Mrlc, Iwasaki et al. (2001)
amplified MRLC2 from a HeLa cell cDNA library. The deduced 172-amino
acid protein contains thr18 and ser19, which are conserved
phosphorylation sites in myosin regulatory light chains.
GENE FUNCTION
Diphosphorylation of MRLCs on thr18 and ser19 results in higher MgATPase
activity and myosin filament formation than monophosphorylation at ser19
in vitro. By site-directed mutagenesis, Iwasaki et al. (2001) created
MRLC2 mutants that mimicked diphosphorylated, monophosphorylated, and
unphosphorylated forms of MRLC2. Overexpression of the diphosphorylated
form, and to a lesser degree the monophosphorylated form, caused the
formation of a large number of actin filament bundles in transfected
HeLa cells. Overexpression of the unphosphorylated form caused a
decrease in the number of actin filament bundles. Immunolocalization of
the mutant proteins in dividing cells revealed colocalization of the 2
phosphorylated forms with actin filaments in the peripheral region and
with the contractile ring, while the unphosphorylated form localized
diffusely throughout the cytoplasm. Iwasaki et al. (2001) concluded that
phosphorylation of MRLC2 is required for organization of stress fibers
in interphase cells and the contractile ring in dividing cells. They
suggested that diphosphorylated MRLC may be more effective in organizing
actin filaments than monophosphorylated MRLC.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the MYL12B
gene to chromosome 18 (TMAP SHGC-12353).
*FIELD* RF
1. Grant, J. W.; Zhong, R. Q.; McEwen, P. M.; Church, S. L.: Human
nonsarcomeric 20,000 Da myosin regulatory light chain cDNA. Nucleic
Acids Res. 18: 5892 only, 1990.
2. Iwasaki, T.; Murata-Hori, M.; Ishitobi, S.; Hosoya, H.: Diphosphorylated
MRLC is required for organization of stress fibers in interphase cells
and the contractile ring in dividing cells. Cell Struct. Func. 26:
677-683, 2001.
*FIELD* CD
Patricia A. Hartz: 2/18/2005
*FIELD* ED
alopez: 06/25/2009
mgross: 2/18/2005