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Myosin light chain kinase, smooth muscle (MLCK) (smMLCK) (EC 2.7.11.18) (Kinase-related protein) (KRP) (Telokin) [Cleaved into: Myosin light chain kinase, smooth muscle, deglutamylated form]

 MYLK_MOUSE              Reviewed;        1941 AA.
Q6PDN3; Q3TSJ7; Q80UX0; Q80YN7; Q80YN8; Q8K026; Q924D2; Q9ERD3;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
02-MAY-2006, sequence version 3.
25-OCT-2017, entry version 125.
RecName: Full=Myosin light chain kinase, smooth muscle;
Short=MLCK;
Short=smMLCK;
EC=2.7.11.18;
AltName: Full=Kinase-related protein;
Short=KRP;
AltName: Full=Telokin;
Contains:
RecName: Full=Myosin light chain kinase, smooth muscle, deglutamylated form;
Name=Mylk {ECO:0000312|EMBL:AAH58610.2, ECO:0000312|MGI:MGI:894806};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAO85808.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
STRAIN=C3H/HeJ {ECO:0000269|PubMed:11029314};
TISSUE=Cardiac myocyte {ECO:0000269|PubMed:11029314};
PubMed=11029314;
Herring B.P., Dixon S.A., Gallagher P.J.;
"Smooth muscle myosin light chain kinase expression in cardiac and
skeletal muscle.";
Am. J. Physiol. 279:C1656-C1664(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:AAG34169.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=Swiss Webster / NIH {ECO:0000312|EMBL:AAG34169.1};
PubMed=11121372;
Herring B.P., Lyons G.E., Hoggatt A.M., Gallagher P.J.;
"Telokin expression is restricted to smooth muscle tissues during
mouse development.";
Am. J. Physiol. 280:C12-C21(2001).
[3] {ECO:0000305, ECO:0000312|EMBL:AAO85807.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=C3H/HeJ {ECO:0000312|EMBL:AAO85807.1};
TISSUE=Cardiac myocyte {ECO:0000269|PubMed:11832329};
PubMed=11832329; DOI=10.1152/ajpcell.00333.2001;
Blue E.K., Goeckeler Z.M., Jin Y., Hou L., Dixon S.A., Herring B.P.,
Wysolmerski R.B., Gallagher P.J.;
"220- and 130-kDa MLCKs have distinct tissue distributions and
intracellular localization patterns.";
Am. J. Physiol. 282:C451-C460(2002).
[4] {ECO:0000312|EMBL:BAE36678.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE36678.1};
TISSUE=Wolffian duct {ECO:0000312|EMBL:BAE36678.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5] {ECO:0000312|EMBL:AAH58610.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C3H/He {ECO:0000312|EMBL:AAH58610.2}, and
FVB/N {ECO:0000312|EMBL:AAH34209.1};
TISSUE=Colon {ECO:0000312|EMBL:AAH34209.1},
Mammary gland {ECO:0000312|EMBL:AAH45197.1}, and
Osteoblast {ECO:0000312|EMBL:AAH58610.2};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6] {ECO:0000312|EMBL:AAK53241.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1561 (ISOFORM 1).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAK53241.1};
PubMed=11472067; DOI=10.1006/geno.2001.6571;
Giorgi D.G., Ferraz C., Mattei M.-G., Demaille J., Rouquier S.;
"The myosin light chain kinase gene is not duplicated in mouse:
partial structure and chromosomal localization of Mylk.";
Genomics 75:49-56(2001).
[7]
FUNCTION IN GIARDIASIS.
PubMed=12360480; DOI=10.1053/gast.2002.36002;
Scott K.G.-E., Meddings J.B., Kirk D.R., Lees-Miller S.P., Buret A.G.;
"Intestinal infection with Giardia spp. reduces epithelial barrier
function in a myosin light chain kinase-dependent fashion.";
Gastroenterology 123:1179-1190(2002).
[8] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16055522; DOI=10.1152/ajpheart.00511.2004;
Ohlmann P., Tesse A., Loichot C., Ralay Ranaivo H., Roul G.,
Philippe C., Watterson D.M., Haiech J., Andriantsitohaina R.;
"Deletion of MLCK210 induces subtle changes in vascular reactivity but
does not affect cardiac function.";
Am. J. Physiol. 289:H2342-H2349(2005).
[9]
FUNCTION IN INTESTINAL BARRIER DYSFUNCTION.
PubMed=16184195; DOI=10.1172/JCI24970;
Clayburgh D.R., Barrett T.A., Tang Y., Meddings J.B., Van Eldik L.J.,
Watterson D.M., Clarke L.L., Mrsny R.J., Turner J.R.;
"Epithelial myosin light chain kinase-dependent barrier dysfunction
mediates T cell activation-induced diarrhea in vivo.";
J. Clin. Invest. 115:2702-2715(2005).
[10]
INTERACTION WITH SVIL.
PubMed=17925381; DOI=10.1242/jcs.008219;
Takizawa N., Ikebe R., Ikebe M., Luna E.J.;
"Supervillin slows cell spreading by facilitating myosin II activation
at the cell periphery.";
J. Cell Sci. 120:3792-3803(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; SER-1782 AND
SER-1798, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[12]
FUNCTION IN MICROVASCULAR HYPERPERMEABILITY DURING SEVERE BURNS, AND
DISRUPTION PHENOTYPE.
PubMed=17577141; DOI=10.1097/SHK.0b013e31804d415f;
Reynoso R., Perrin R.M., Breslin J.W., Daines D.A., Watson K.D.,
Watterson D.M., Wu M.H., Yuan S.;
"A role for long chain myosin light chain kinase (MLCK-210) in
microvascular hyperpermeability during severe burns.";
Shock 28:589-595(2007).
[13]
FUNCTION IN SMOOTH MUSCLE CONTRACTION.
PubMed=18586037; DOI=10.1053/j.gastro.2008.05.032;
He W.-Q., Peng Y.-J., Zhang W.-C., Lv N., Tang J., Chen C.,
Zhang C.-H., Gao S., Chen H.-Q., Zhi G., Feil R., Kamm K.E.,
Stull J.T., Gao X., Zhu M.-S.;
"Myosin light chain kinase is central to smooth muscle contraction and
required for gastrointestinal motility in mice.";
Gastroenterology 135:610-620(2008).
[14]
FUNCTION AS PTK2B/PYK2 KINASE, AND INTERACTION WITH PTK2B/PYK2.
PubMed=18587400; DOI=10.1038/ni.1628;
Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B.;
"Nonmuscle myosin light-chain kinase mediates neutrophil
transmigration in sepsis-induced lung inflammation by activating beta2
integrins.";
Nat. Immunol. 9:880-886(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-355; SER-935;
SER-1460; SER-1781; SER-1782; SER-1795; SER-1798; THR-1800 AND
SER-1801, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
DEGLUTAMYLATION.
PubMed=21074048; DOI=10.1016/j.cell.2010.10.014;
Rogowski K., van Dijk J., Magiera M.M., Bosc C., Deloulme J.C.,
Bosson A., Peris L., Gold N.D., Lacroix B., Grau M.B., Bec N.,
Larroque C., Desagher S., Holzer M., Andrieux A., Moutin M.J.,
Janke C.;
"A family of protein-deglutamylating enzymes associated with
neurodegeneration.";
Cell 143:564-578(2010).
[17]
FUNCTION IN TONIC AIRWAY SMOOTH MUSCLE CONTRACTION.
PubMed=20018858; DOI=10.1074/jbc.M109.062836;
Zhang W.-C., Peng Y.-J., Zhang G.-S., He W.-Q., Qiao Y.-N.,
Dong Y.-Y., Gao Y.-Q., Chen C., Zhang C.-H., Li W., Shen H.-H.,
Ning W., Kamm K.E., Stull J.T., Gao X., Zhu M.-S.;
"Myosin light chain kinase is necessary for tonic airway smooth muscle
contraction.";
J. Biol. Chem. 285:5522-5531(2010).
[18]
FUNCTION IN TIGHT JUNCTION REGULATION.
PubMed=20404178; DOI=10.1073/pnas.0908869107;
Yu D., Marchiando A.M., Weber C.R., Raleigh D.R., Wang Y., Shen L.,
Turner J.R.;
"MLCK-dependent exchange and actin binding region-dependent anchoring
of ZO-1 regulate tight junction barrier function.";
Proc. Natl. Acad. Sci. U.S.A. 107:8237-8241(2010).
-!- FUNCTION: Calcium/calmodulin-dependent myosin light chain kinase
implicated in smooth muscle contraction via phosphorylation of
myosin light chains (MLC). Also regulates actin-myosin interaction
through a non-kinase activity. Phosphorylates PTK2B/PYK2 and
myosin light-chains. Involved in the inflammatory response (e.g.
apoptosis, vascular permeability, leukocyte diapedesis), cell
motility and morphology, airway hyperreactivity and other
activities relevant to asthma. Required for tonic airway smooth
muscle contraction that is necessary for physiological and
asthmatic airway resistance. Necessary for gastrointestinal
motility. Implicated in the regulation of endothelial as well as
vascular permeability, probably via the regulation of cytoskeletal
rearrangements. In the nervous system it has been shown to control
the growth initiation of astrocytic processes in culture and to
participate in transmitter release at synapses formed between
cultured sympathetic ganglion cells. Critical participant in
signaling sequences that result in fibroblast apoptosis. Plays a
role in the regulation of epithelial cell survival. Required for
epithelial wound healing, especially during actomyosin ring
contraction during purse-string wound closure. Mediates RhoA-
dependent membrane blebbing. Triggers TRPC5 channel activity in a
calcium-dependent signaling, by inducing its subcellular
localization at the plasma membrane. Promotes cell migration
(including tumor cells) and tumor metastasis. PTK2B/PYK2
activation by phosphorylation mediates ITGB2 activation and is
thus essential to trigger neutrophil transmigration during acute
lung injury (ALI). May regulate optic nerve head astrocyte
migration. Probably involved in mitotic cytoskeletal regulation.
Regulates tight junction probably by modulating ZO-1 exchange in
the perijunctional actomyosin ring. Mediates burn-induced
microvascular barrier injury; triggers endothelial contraction in
the development of microvascular hyperpermeability by
phosphorylating MLC. Essential for intestinal barrier dysfunction.
Mediates Giardia spp.-mediated reduced epithelial barrier function
during giardiasis intestinal infection via reorganization of
cytoskeletal F-actin and tight junctional ZO-1. Necessary for
hypotonicity-induced Ca(2+) entry and subsequent activation of
volume-sensitive organic osmolyte/anion channels (VSOAC) in
cervical cancer cells. {ECO:0000269|PubMed:11832329,
ECO:0000269|PubMed:12360480, ECO:0000269|PubMed:16055522,
ECO:0000269|PubMed:16184195, ECO:0000269|PubMed:17577141,
ECO:0000269|PubMed:18586037, ECO:0000269|PubMed:18587400,
ECO:0000269|PubMed:20018858, ECO:0000269|PubMed:20404178}.
-!- CATALYTIC ACTIVITY: ATP + [myosin light-chain] = ADP + [myosin
light-chain] phosphate. {ECO:0000269|PubMed:11832329}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- SUBUNIT: All isoforms including Telokin bind calmodulin. Interacts
with CTTN; this interaction is reduced during thrombin-induced
endothelial cell (EC) contraction but is promoted by the barrier-
protective agonist sphingosine 1-phosphate (S1P) within
lamellipodia. A complex made of ABL1, CTTN and MYLK regulates
cortical actin-based cytoskeletal rearrangement critical to
sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC)
barrier enhancement. Binds to NAA10/ARD1 (By similarity).
Interacts with SVIL and PTK2B/PYK2. {ECO:0000250,
ECO:0000269|PubMed:17925381, ECO:0000269|PubMed:18587400}.
-!- INTERACTION:
Q9JMG9:Patz1; NbExp=3; IntAct=EBI-647412, EBI-647451;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11832329}.
Cell projection, lamellipodium {ECO:0000250}. Cleavage furrow
{ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Note=Localized to stress fibers during interphase and to the
cleavage furrow during mitosis (By similarity). Tagged isoform 1
colocalizes with stress fibers. Tagged Smooth muscle isoform is
found throughout the cytoplasm with higher levels near the plasma
membrane. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing, Alternative initiation; Named isoforms=4;
Name=1 {ECO:0000269|PubMed:11832329}; Synonyms=Non muscle isozyme
{ECO:0000269|PubMed:11832329};
IsoId=Q6PDN3-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:16141072};
IsoId=Q6PDN3-2; Sequence=VSP_052002, VSP_052003;
Note=Produced by alternative promoter usage and alternative
splicing. No experimental confirmation available.;
Name=3; Synonyms=Smooth muscle isozyme;
IsoId=Q6PDN3-3; Sequence=VSP_018847;
Note=Produced by alternative initiation at Met-911 of isoform
1.;
Name=4; Synonyms=Telokin;
IsoId=Q6PDN3-4; Sequence=VSP_018848;
Note=Produced by alternative initiation at Met-1783 of isoform
1.;
-!- TISSUE SPECIFICITY: Smooth muscle isoform expressed in all tissues
with highest levels in bladder, uterus, vas deferens, colon,
ileum, and tracheae. Isoform 1 expressed in lung, bladder, and vas
deferens. Telokin expressed in smooth muscle cells of uterus, vas
deferens, bladder, colon, kidney, ureter, ovary and trachea.
{ECO:0000269|PubMed:11121372, ECO:0000269|PubMed:11832329}.
-!- DEVELOPMENTAL STAGE: Isoform 1 ubiquitously expressed in E14.5
embryos with highest levels in some areas of the developing brain,
the lower gastrointestinal tract as well as certain blood vessels.
Primary cultures of endothelial cells lose high level expression
of Smooth muscle isoform with increasing number of passages.
Telokin expressed in embryonic gut from E11.5 with highest level
in E15.5. Also expressed in developing bronchi from E13.5. High
levels in E15.5 bladder, ureter, urethra and rectum. Telokin
expression is induced in reproductive tract during postnatal
development. {ECO:0000269|PubMed:11121372,
ECO:0000269|PubMed:11832329}.
-!- PTM: Can probably be down-regulated by phosphorylation. Tyrosine
phosphorylation by ABL1 increases kinase activity, reverses MLCK-
mediated inhibition of Arp2/3-mediated actin polymerization, and
enhances CTTN-binding. Phosphorylation by SRC at Tyr-452 promotes
CTTN binding (By similarity). {ECO:0000250}.
-!- PTM: The C-terminus is deglutamylated by AGTPBP1/CCP1, AGBL1/CCP4
and AGBL4/CCP6, leading to the formation of Myosin light chain
kinase, smooth muscle, deglutamylated form. The consequences of C-
terminal deglutamylation are unknown (PubMed:21074048).
{ECO:0000269|PubMed:21074048}.
-!- DISRUPTION PHENOTYPE: Mice lacking isoform 1 show a reduced flow-
mediated dilation of small mesenteric arteries but no significant
changes in main cardiovascular function. Increased survival from
burn. Prevention of epithelial MLC phosphorylation, tight junction
disruption, protein leak, and diarrhea following T-cell
activation. {ECO:0000269|PubMed:16055522,
ECO:0000269|PubMed:17577141}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH58610.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAO85807.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY237727; AAO85808.1; -; mRNA.
EMBL; AF314149; AAG34169.1; -; mRNA.
EMBL; AY237726; AAO85807.1; ALT_INIT; mRNA.
EMBL; AK162008; BAE36678.1; -; mRNA.
EMBL; BC034209; AAH34209.1; -; mRNA.
EMBL; BC045197; AAH45197.1; -; mRNA.
EMBL; BC058610; AAH58610.2; ALT_INIT; mRNA.
EMBL; AF335470; AAK53241.1; -; Genomic_DNA.
UniGene; Mm.33360; -.
ProteinModelPortal; Q6PDN3; -.
SMR; Q6PDN3; -.
IntAct; Q6PDN3; 21.
MINT; MINT-1849579; -.
STRING; 10090.ENSMUSP00000023538; -.
iPTMnet; Q6PDN3; -.
PhosphoSitePlus; Q6PDN3; -.
PaxDb; Q6PDN3; -.
PeptideAtlas; Q6PDN3; -.
PRIDE; Q6PDN3; -.
UCSC; uc007zbe.1; mouse. [Q6PDN3-1]
UCSC; uc007zbh.1; mouse. [Q6PDN3-4]
MGI; MGI:894806; Mylk.
eggNOG; KOG0613; Eukaryota.
eggNOG; ENOG410XQFD; LUCA.
HOVERGEN; HBG052551; -.
InParanoid; Q6PDN3; -.
BRENDA; 2.7.11.18; 3474.
ChiTaRS; Mylk; mouse.
PRO; PR:Q6PDN3; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_MYLK; -.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0032154; C:cleavage furrow; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0030027; C:lamellipodium; ISO:MGI.
GO; GO:0001725; C:stress fiber; ISO:MGI.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004687; F:myosin light chain kinase activity; ISO:MGI.
GO; GO:0060414; P:aorta smooth muscle tissue morphogenesis; ISO:MGI.
GO; GO:0032060; P:bleb assembly; ISO:MGI.
GO; GO:0071476; P:cellular hypotonic response; ISO:MGI.
GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI.
GO; GO:0035690; P:cellular response to drug; IDA:MGI.
GO; GO:0035865; P:cellular response to potassium ion; IDA:MGI.
GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0090303; P:positive regulation of wound healing; ISO:MGI.
GO; GO:0006939; P:smooth muscle contraction; IMP:UniProtKB.
GO; GO:0014820; P:tonic smooth muscle contraction; IMP:UniProtKB.
CDD; cd00063; FN3; 1.
CDD; cd14191; STKc_MLCK1; 1.
Gene3D; 2.60.40.10; -; 10.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR015725; MLCK1_kinase_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00041; fn3; 1.
Pfam; PF07679; I-set; 9.
Pfam; PF00069; Pkinase; 1.
SMART; SM00060; FN3; 1.
SMART; SM00409; IG; 9.
SMART; SM00408; IGc2; 9.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF48726; SSF48726; 9.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50853; FN3; 1.
PROSITE; PS50835; IG_LIKE; 9.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Actin-binding; Alternative initiation; Alternative promoter usage;
Alternative splicing; ATP-binding; Calcium; Calmodulin-binding;
Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
Disulfide bond; Immunoglobulin domain; Kinase; Magnesium;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Repeat; Serine/threonine-protein kinase; Transferase.
CHAIN 1 1941 Myosin light chain kinase, smooth muscle.
/FTId=PRO_0000233949.
CHAIN 1 1934 Myosin light chain kinase, smooth muscle,
deglutamylated form.
/FTId=PRO_0000403732.
DOMAIN 33 122 Ig-like C2-type 1. {ECO:0000255}.
DOMAIN 156 244 Ig-like C2-type 2. {ECO:0000255}.
DOMAIN 402 485 Ig-like C2-type 3. {ECO:0000255}.
DOMAIN 502 587 Ig-like C2-type 4. {ECO:0000255}.
DOMAIN 611 699 Ig-like C2-type 5. {ECO:0000255}.
DOMAIN 709 809 Ig-like C2-type 6. {ECO:0000255}.
REPEAT 856 883 1-1. {ECO:0000250|UniProtKB:Q15746}.
REPEAT 884 911 1-2. {ECO:0000250|UniProtKB:Q15746}.
REPEAT 912 939 1-3. {ECO:0000250|UniProtKB:Q15746}.
REPEAT 940 966 1-4. {ECO:0000250|UniProtKB:Q15746}.
REPEAT 967 985 1-5; truncated.
REPEAT 990 1002 2-1. {ECO:0000250|UniProtKB:Q15746}.
REPEAT 1003 1014 2-2. {ECO:0000250|UniProtKB:Q15746}.
REPEAT 1015 1026 2-3. {ECO:0000250|UniProtKB:Q15746}.
REPEAT 1027 1038 2-4. {ECO:0000250|UniProtKB:Q15746}.
REPEAT 1039 1049 2-5. {ECO:0000250|UniProtKB:Q15746}.
DOMAIN 1120 1208 Ig-like C2-type 7. {ECO:0000255}.
DOMAIN 1260 1348 Ig-like C2-type 8. {ECO:0000255}.
DOMAIN 1356 1449 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1486 1741 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 1831 1920 Ig-like C2-type 9. {ECO:0000255}.
NP_BIND 1492 1500 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 856 985 5 X 28 AA approximate tandem repeats.
REGION 911 951 Actin-binding (calcium/calmodulin-
sensitive). {ECO:0000250}.
REGION 936 951 Calmodulin-binding. {ECO:0000250}.
REGION 990 1049 5 X 12 AA approximate tandem repeats.
REGION 1048 1482 Actin-binding (calcium/calmodulin-
insensitive). {ECO:0000250}.
REGION 1733 1796 Calmodulin-binding.
{ECO:0000250|UniProtKB:Q15746}.
COMPBIAS 1918 1941 Glu-rich. {ECO:0000255}.
ACT_SITE 1607 1607 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 1515 1515 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 226 226 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q15746}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000250|UniProtKB:Q15746}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 452 452 Phosphotyrosine; by ABL1 and SRC.
{ECO:0000250|UniProtKB:Q15746}.
MOD_RES 780 780 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q15746}.
MOD_RES 935 935 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1460 1460 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1471 1471 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q15746}.
MOD_RES 1597 1597 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q15746}.
MOD_RES 1657 1657 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q15746}.
MOD_RES 1781 1781 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1782 1782 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1794 1794 Phosphoserine.
{ECO:0000250|UniProtKB:Q15746}.
MOD_RES 1795 1795 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1798 1798 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1800 1800 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1801 1801 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
DISULFID 177 228 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 423 475 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 523 571 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 730 793 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 1141 1192 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 1852 1904 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 1782 Missing (in isoform 4).
{ECO:0000303|PubMed:11121372}.
/FTId=VSP_018848.
VAR_SEQ 1 1254 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_052002.
VAR_SEQ 1 910 Missing (in isoform 3).
{ECO:0000303|PubMed:11029314}.
/FTId=VSP_018847.
VAR_SEQ 1255 1256 KA -> MQ (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_052003.
CONFLICT 173 173 W -> G (in Ref. 3 and 6). {ECO:0000305}.
CONFLICT 252 252 S -> A (in Ref. 6; AAK53241).
{ECO:0000305}.
CONFLICT 471 472 RK -> GR (in Ref. 3 and 6).
{ECO:0000305}.
CONFLICT 478 478 S -> T (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 482 482 G -> A (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 666 667 HS -> TP (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 677 677 D -> S (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 749 750 LS -> SP (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 1004 1004 A -> G (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 1038 1038 G -> A (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 1106 1106 A -> R (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 1174 1181 RFSVSIEK -> TFLCLHRE (in Ref. 3;
AAO85807). {ECO:0000305}.
CONFLICT 1210 1210 D -> A (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 1289 1289 I -> T (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 1340 1340 Missing (in Ref. 4; BAE36678).
{ECO:0000305}.
CONFLICT 1409 1409 T -> H (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 1657 1657 Y -> H (in Ref. 5; AAH58610).
{ECO:0000305}.
CONFLICT 1661 1661 G -> R (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 1678 1678 S -> R (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 1706 1706 A -> E (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 1732 1735 CTQC -> STHG (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 1825 1825 E -> K (in Ref. 3; AAO85807).
{ECO:0000305}.
CONFLICT 1888 1888 S -> T (in Ref. 2; AAG34169).
{ECO:0000305}.
CONFLICT 1941 1941 Missing (in Ref. 5; AAH58610).
{ECO:0000305}.
SEQUENCE 1941 AA; 212925 MW; 7FF12C60F1BDFFDD CRC64;
MGDVKLFASS HMSKTSHSVD PSKVSSMPLT EAPAFILPPR NLCVKEGATA KFEGRVRGYP
EPQVTWHRKG QAITNGGRFL LDCGVRGTFS LVIHTVREED KGKYTCEASN GSGARQVTVE
LTVEGNSMKK RDQPVLSKAS GFPGETRPSI WGECPPKFAT KLGRAVVKEG QMWRFSCKIT
GRPPPQVTWL KGNVPLQPSA RVSMSEKNGM QILEIRGVTR DDLGVYTCMV VNGSGKASMS
AELSIPGLDN ASRLAVRGTK APSPDIRKEV TNGVSKDPET VAESKNCPSP QRSGSSARAT
NSHLKSPQEP KPKLCEDAPR KVPQSSILQK STSTITLQAL KVQPEARVPA IGSFSPGEDR
KSLAAPQQAT LPTRQSSLGG SVGNKFVTGN IPRESQREST FPRFESQPQS QEVTEGQTVK
FICEVSGIPK PDVGWFLEGI PVRRREGITE VYEDGVSHHL CLLRARTRDS RKYSCTASNS
LGQVSCSWSL LVDRPNLAQT APSFSSVLKD SVVIEGQDFV LRCSVQGTPA PRVTWLLNGQ
PIQFAHSICE AGVAELHIQD ALPEDRGTYT CLAENAMGQV SCSATVTVQE KKGEGEREHR
LSPARSKPIA PIFLQGLSDL KVMDGSQVTM TVQVSGNPPP EVIWLHDGNE IQESEDFHFE
QKGGWHSLCI QEVFPEDTGT YTCEAWNSAG EVRTRAVLTV QEPHDGTQPW FISKPRSVTA
TLGQSVLISC AIAGDPFPTV HWLRDGRALS KDSGHFELLQ NEDVFTLVLK NVQPWHAGQY
EILLKNRVGE CSCQVSLMLH NSPSRAPPRG REPASCEGLC GGGGVGAHGD GDRHGTLRPC
WPARGQGWPE EEDGEDVRGL LKRRVETRLH TEEAIRQQEV GQLDFRDLLG KKVSTKTVSE
DDLKDIPAEQ MDFRANLQRQ VKPKTISEEE RKVHSPQQVD FRSVLAKKGT PKTPVPEKAP
PKAATPDFRS VLGGKKKSPS ENGGNSAEVL NVKAGESPTP AGDAQAIGAL KPVGNAKPAE
TPKPIGNAKP TETLKPVGNT KPAETLKPIA NAQPSGSLKP VTNAQPAEPQ KPVGNAKSAE
TSKPAGKEEV KEVKNDVNCK KGQVGATGNE KRPESQGSAP VFKEKLQDVH VAEGEKLLLQ
CQVISDPPAT VTWSLNGKTL KTTKFIVLAQ EGSRFSVSIE KALPEDRGLY KCVAKNSAGQ
AECSCQVTVD DAQTSENTKA PEMKSRRPKS SLPPVLGTES DATVKKKPAP KTPTKAAMPP
QIIQFPEDQK VRAGEPVELF GKVAGTQPIT CKWMKFRKQI QESEHIKVEN GESGSKLTIL
AARQEHCGCY TLVVENKLGS RQAQVNLTVV DKPDPPAGTP CASDIRSSSL TLSWYGSSYD
GGSAVQSYNV EIWDTEDKVW KELATCRSTS FNVQDLLPDR EYKFRVRAVN VYGTSEPSQE
SELTAVGEKP EEPKDEVEVS DDDEKEPEVD YRTVTVNTEQ KVSDVYDIEE RLGSGKFGQV
FRLVEKKTGK IWAGKFFKAY SAKEKDNIRQ EISIMNCLHH PKLVQCVDAF EEKANIVMVL
EIVSGGELFE RIIDEDFELT ERECIKYMRQ ISEGVEYIHK QGIVHLDLKP ENIMCVNKTG
TRIKLIDFGL ARRLENAGSL KVLFGTPEFV APEVINYEPI GYATDMWSIG VICYILVSGL
SPFMGDNDNE TLANVTSATW DFDDEAFDEI SDDAKDFISN LLKKDMKNRL DCTQCLQHPW
LMKDTKNMEA KKLSKDRMKK YMARRKWQKT GNAVRAIGRL SSMAMISGLS GRKSSTGSPT
SPINAEKLES EDDVSQAFLE AVAEEKPHVK PYFSKTIRDL EVVEGSAARF DCKIEGYPDP
EVVWFKDDQS IRESRHFQID YDEDGNCSLI ISDVCGDDDA KYTCKAVNSL GEATCTAELI
VETMEEGEGE EGGEEEEEEE E


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