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Dystonin (Bullous pemphigoid antigen 1) (BPA) (Dystonia musculorum protein) (Hemidesmosomal plaque protein) (Microtubule actin cross-linking factor 2)

 DYST_MOUSE              Reviewed;        7393 AA.
Q91ZU6; E9PXE5; E9QL23; Q1KP04; Q3I6J6; Q60824; Q60845; Q8K5D4;
Q91ZU7; Q91ZU8; Q9WU50; S4R1U5;
30-APR-2003, integrated into UniProtKB/Swiss-Prot.
03-SEP-2014, sequence version 2.
25-OCT-2017, entry version 154.
RecName: Full=Dystonin;
AltName: Full=Bullous pemphigoid antigen 1;
Short=BPA;
AltName: Full=Dystonia musculorum protein;
AltName: Full=Hemidesmosomal plaque protein;
AltName: Full=Microtubule actin cross-linking factor 2;
Name=Dst; Synonyms=Bpag1, Macf2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:AAK83384.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 5), TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
STRAIN=BALB/cJ; TISSUE=Epithelium, Muscle, and Neuron;
PubMed=11514586; DOI=10.1083/jcb.200012098;
Leung C.L., Zheng M., Prater S.M., Liem R.K.H.;
"The BPAG1 locus: alternative splicing produces multiple isoforms with
distinct cytoskeletal linker domains, including predominant isoforms
in neurons and muscles.";
J. Cell Biol. 154:691-697(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-511 (ISOFORM 2), PARTIAL NUCLEOTIDE
SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Brain;
PubMed=7670468; DOI=10.1038/ng0795-301;
Brown A., Bernier G., Mathieu M., Rossant J., Kothary R.;
"The mouse dystonia musculorum gene is a neural isoform of bullous
pemphigoid antigen 1.";
Nat. Genet. 10:301-306(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-304 (ISOFORM 6), ALTERNATIVE SPLICING
(ISOFORMS 2 AND 6), AND SUBCELLULAR LOCATION (ISOFORMS 2 AND 6).
STRAIN=C3H/HeJ;
PubMed=16289082; DOI=10.1016/j.yexcr.2005.10.002;
Young K.G., Pinheiro B., Kothary R.;
"A Bpag1 isoform involved in cytoskeletal organization surrounding the
nucleus.";
Exp. Cell Res. 312:121-134(2006).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-270 (ISOFORM 7), ALTERNATIVE SPLICING
(ISOFORMS 1; 6 AND 7), FUNCTION OF ISOFORMS 1; 6 AND 7,
PALMITOYLATION, MYRISTOYLATION, MUTAGENESIS, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
STRAIN=C57BL/6 X CBA;
PubMed=16797530; DOI=10.1016/j.yexcr.2006.04.025;
Jefferson J.J., Leung C.L., Liem R.K.;
"Dissecting the sequence specific functions of alternative N-terminal
isoforms of mouse bullous pemphigoid antigen 1.";
Exp. Cell Res. 312:2712-2725(2006).
[6]
PROTEIN SEQUENCE OF 580-584; 1043-1047 AND 1053-1057, AND X-RAY
CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 580-803.
PubMed=17161423; DOI=10.1016/j.jmb.2006.11.036;
Jefferson J.J., Ciatto C., Shapiro L., Liem R.K.;
"Structural analysis of the plakin domain of bullous pemphigoid
antigen1 (BPAG1) suggests that plakins are members of the spectrin
superfamily.";
J. Mol. Biol. 366:244-257(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6697-7393 (ISOFORM 3), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6874-7393 (ISOFORM 4).
STRAIN=C57BL/6J; TISSUE=Fetal skin, and Fetal spinal cord;
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).
[8]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, AND
INTERACTION WITH PRPH.
STRAIN=BALB/cJ;
PubMed=9971739; DOI=10.1083/jcb.144.3.435;
Leung C.L., Sun D., Liem R.K.;
"The intermediate filament protein peripherin is the specific
interaction partner of mouse BPAG1-n (dystonin) in neurons.";
J. Cell Biol. 144:435-446(1999).
[9]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
STRAIN=Swiss Webster / NIH;
Kubo Y., Ohba M., Iwashita S.;
"Molecular network in NGF-mediated neural differentiation.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[10]
ALTERNATIVE SPLICING (ISOFORM 5), DISRUPTION PHENOTYPE, SUBCELLULAR
LOCATION (ISOFORM 5), AND TISSUE SPECIFICITY.
PubMed=7736575; DOI=10.1016/0092-8674(95)90333-X;
Guo L., Degenstein L., Dowling J., Yu Q.C., Wollmann R., Perman B.,
Fuchs E.;
"Gene targeting of BPAG1: abnormalities in mechanical strength and
cell migration in stratified epithelia and neurologic degeneration.";
Cell 81:233-243(1995).
[11]
ALTERNATIVE SPLICING (ISOFORMS 5 AND 6), SUBCELLULAR LOCATION
(ISOFORMS 5 AND 6), AND TISSUE SPECIFICITY.
PubMed=8752219; DOI=10.1016/S0092-8674(00)80138-5;
Yang Y., Dowling J., Yu Q.C., Kouklis P., Cleveland D.W., Fuchs E.;
"An essential cytoskeletal linker protein connecting actin
microfilaments to intermediate filaments.";
Cell 86:655-665(1996).
[12]
DISRUPTION PHENOTYPE.
PubMed=10428034; DOI=10.1016/S0092-8674(00)81017-X;
Yang Y., Bauer C., Strasser G., Wollman R., Julien J.P., Fuchs E.;
"Integrators of the cytoskeleton that stabilize microtubules.";
Cell 98:229-238(1999).
[13]
INTERACTION WITH DES, AND DISRUPTION PHENOTYPE.
PubMed=10357897; DOI=10.1006/dbio.1999.9263;
Dalpe G., Mathieu M., Comtois A., Zhu E., Wasiak S., De Repentigny Y.,
Leclerc N., Kothary R.;
"Dystonin-deficient mice exhibit an intrinsic muscle weakness and an
instability of skeletal muscle cytoarchitecture.";
Dev. Biol. 210:367-380(1999).
[14]
FUNCTION, DISRUPTION PHENOTYPE, ALTERNATIVE SPLICING (ISOFORM 1),
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY (ISOFORM 1).
PubMed=14581450; DOI=10.1083/jcb.200306075;
Liu J.J., Ding J., Kowal A.S., Nardine T., Allen E., Delcroix J.D.,
Wu C., Mobley W., Fuchs E., Yang Y.;
"BPAG1n4 is essential for retrograde axonal transport in sensory
neurons.";
J. Cell Biol. 163:223-229(2003).
[15]
ALTERNATIVE SPLICING (ISOFORMS 2; 5 AND 6), HOMODIMERIZATION,
MUTAGENESIS OF ARG-1385 AND ARG-1386, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=14576348; DOI=10.1242/jcs.00764;
Young K.G., Pool M., Kothary R.;
"Bpag1 localization to actin filaments and to the nucleus is regulated
by its N-terminus.";
J. Cell Sci. 116:4543-4555(2003).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[17]
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).
[18]
FUNCTION, INTERACTION WITH TMEM108 (ISOFORM 1), DISRUPTION PHENOTYPE,
AND SUBCELLULAR LOCATION.
PubMed=17287360; DOI=10.1073/pnas.0602222104;
Liu J.J., Ding J., Wu C., Bhagavatula P., Cui B., Chu S., Mobley W.C.,
Yang Y.;
"Retrolinkin, a membrane protein, plays an important role in
retrograde axonal transport.";
Proc. Natl. Acad. Sci. U.S.A. 104:2223-2228(2007).
[19]
ALTERNATIVE SPLICING (ISOFORM 6), INTERACTION WITH SYNE3, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=18638474; DOI=10.1016/j.yexcr.2008.06.021;
Young K.G., Kothary R.;
"Dystonin/Bpag1 is a necessary endoplasmic reticulum/nuclear envelope
protein in sensory neurons.";
Exp. Cell Res. 314:2750-2761(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-237; SER-1381;
SER-2211; SER-4680; SER-5488; SER-7333; SER-7336 AND SER-7348,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-208 (ISOFORM
7), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
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).
[21]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH PLEC,
SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
PubMed=19932097; DOI=10.1016/j.yexcr.2009.11.010;
Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F.,
Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G.,
Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L.,
Borradori L.;
"BPAG1 isoform-b: complex distribution pattern in striated and heart
muscle and association with plectin and alpha-actinin.";
Exp. Cell Res. 316:297-313(2010).
[22]
ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION OF ISOFORM 2, SUBCELLULAR
LOCATION (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=20209123; DOI=10.1371/journal.pone.0009465;
Boyer J.G., Bhanot K., Kothary R., Boudreau-Lariviere C.;
"Hearts of dystonia musculorum mice display normal morphological and
histological features but show signs of cardiac stress.";
PLoS ONE 5:E9465-E9465(2010).
-!- FUNCTION: Cytoskeletal linker protein. Acts as an integrator of
intermediate filaments, actin and microtubule cytoskeleton
networks. Required for anchoring either intermediate filaments to
the actin cytoskeleton in neural and muscle cells or keratin-
containing intermediate filaments to hemidesmosomes in epithelial
cells. The proteins may self-aggregate to form filaments or a two-
dimensional mesh. Regulates the organization and stability of the
microtubule network of sensory neurons to allow axonal transport.
Mediates docking of the dynein/dynactin motor complex to vesicle
cargos for retrograde axonal transport through its interaction
with TMEM108 and DCTN1. {ECO:0000269|PubMed:17287360}.
-!- FUNCTION: Isoform 5: plays a structural role in the assembly of
hemidesmosomes of epithelial cells; anchors keratin-containing
intermediate filaments to the inner plaque of hemidesmosomes.
Required for the regulation of keratinocyte polarity and motility;
mediates integrin ITGB4 regulation of RAC1 activity.
-!- FUNCTION: Isoform 6: required for bundling actin filaments around
the nucleus.
-!- SUBUNIT: Homodimer. Interacts with MAPRE1; probably required for
targeting to the growing microtubule plus ends. Isoform 2
interacts (via N-terminus) with ACTN2. Isoform 2 interacts (via N-
terminus) with PLEC (via N-terminus). Isoform 5 interacts (via N-
terminus) with COL17A1 (via cytoplasmic region). Isoform 5
interacts (via N-terminus) with ITGB4 isoform beta-4a (via
cytoplasmic region). Isoform 5 interacts (via N-terminus) with
ERBIN (via C-terminus). Isoform 5 associates (via C-terminal) with
KRT5-KRT14 (via rod region) intermediate filaments of keratins (By
similarity). Isoform 2 and isoform 6 can homodimerize (via N-
terminus). Isoform 2 interacts (via N-terminus) with PLEC (via N-
terminus). Interacts with the neuronal intermediate filament
protein, PRPH. Interacts with DES. Interacts with SYNE3. Isoform 1
interacts with TMEM108 (PubMed:17287360).
{ECO:0000250|UniProtKB:Q03001, ECO:0000269|PubMed:10357897,
ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:18638474,
ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:9971739}.
-!- INTERACTION:
P21807:Prph (xeno); NbExp=3; IntAct=EBI-446159, EBI-446227;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
axon {ECO:0000269|PubMed:17287360}. Note=Associates with axonal
microtubules at the growing distal tip and intermediate filaments,
but not with actin cytoskeleton, in sensory neurons (By
similarity). Associates with intermediate filaments, actin and
microtubule cytoskeletons. Localizes to actin stress fibers and to
actin-rich ruffling at the cortex of cells. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:19932097}. Note=Colocalizes both cortical and
cytoplasmic actin filaments (PubMed:19932097). Localizes to
vesicule-like structures associated with microtubules
(PubMed:14581450, PubMed:17287360). {ECO:0000269|PubMed:14581450,
ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:19932097}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane, sarcolemma.
Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril,
sarcomere, H zone. Cytoplasm, cytoskeleton. Note=Localizes to
microtubules and actin microfilaments throughout the cytoplasm and
at focal contact attachments at the plasma membrane.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm, cytoskeleton. Cell
junction, hemidesmosome. Note=Colocalizes with the epidermal KRT5-
KRT14 intermediate filaments network of keratins. Colocalizes with
ITGB4 at the leading edge of migrating keratinocytes (By
similarity). Localizes to actin and intermediate filaments
cytoskeletons. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 6: Nucleus. Nucleus envelope.
Membrane; Single-pass membrane protein. Endoplasmic reticulum
membrane; Single-pass membrane protein. Cytoplasm, cytoskeleton.
Note=Associates with actin cytoskeleton in sensory neurons (By
similarity). Localizes to actin and intermediate filaments
cytoskeletons. Localizes to central actin stress fibers around the
nucleus and is excluded form focal contact sites in myoblast
cells. Translocates to the nucleus. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 7: Cytoplasm, cytoskeleton.
Cytoplasm, cell cortex. Cell membrane; Lipid-anchor.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
Name=2 {ECO:0000269|PubMed:11514586}; Synonyms=BPAG1-b, BPAG1a1,
dystonin-1;
IsoId=Q91ZU6-1; Sequence=Displayed;
Name=1 {ECO:0000269|PubMed:11514586}; Synonyms=BPAG1-a
{ECO:0000303|PubMed:14581450}, BPAG1a2, BPAG1n4
{ECO:0000303|PubMed:14581450};
IsoId=Q91ZU6-2; Sequence=VSP_041549;
Name=3 {ECO:0000305};
IsoId=Q91ZU6-3; Sequence=VSP_041550, VSP_041551, VSP_041552;
Note=No experimental confirmation available. {ECO:0000305};
Name=4 {ECO:0000305};
IsoId=Q91ZU6-4; Sequence=VSP_041551, VSP_041552;
Note=No experimental confirmation available. {ECO:0000305};
Name=5; Synonyms=BPAG1-e;
IsoId=Q91ZU6-5; Sequence=VSP_055459, VSP_055460, VSP_055461;
Name=6; Synonyms=BPAG1n, BPAG1-n1, BPAG1-n2, BPAG1a2, dystonin-2;
IsoId=Q91ZU6-6; Sequence=VSP_041543, VSP_041546;
Note=Incomplete sequence. Transmembrane protein (helical
transmembrane domain from amino acid 18 to 38). Ref.3 (AAC52231)
sequence differs from that shown due to a frameshift in position
51. Ref.3 (AAC52231) sequence is in conflict in position:
101:E->K. {ECO:0000305};
Name=7; Synonyms=BPAG1a3;
IsoId=Q91ZU6-8; Sequence=VSP_041542, VSP_041544, VSP_041545;
Note=Incomplete sequence. Probably myristoylated on Gly-2.
Probably S-palmitoylated on Cys-5 and Cys-7. Mutagenesis of
Gly-2 to Ala inhibits cortical localization. Mutagenesis of
Cys-5 to Ser inhibits cortical localization. Mutagenesis of
Cys-7 to Ser inhibits cortical localization. Contains a
phosphoserine at position 205. Contains a phosphoserine at
position 208. {ECO:0000244|PubMed:21183079};
-!- TISSUE SPECIFICITY: Isoform 1 and 2 are expressed in striated and
heart muscle cells. Isoform 5 is expressed in the skin. Isoform 6
is expressed in sensory neural cells of the dorsal root ganglion
and with low level in the skin (at protein level). Isoform 1 is
expressed predominantly in the brain and spinal cord with low
levels in the heart (PubMed:14581450). Isoform 2 is predominantly
expressed in muscle and heart and with low levels in the brain.
Isoform 5 is expressed in the skin and with low levels in myoblast
cells. Isoform 6 is expressed in neurons. Isoform 7 is expressed
in lung and with low levels in the brain.
{ECO:0000269|PubMed:11514586, ECO:0000269|PubMed:14576348,
ECO:0000269|PubMed:14581450, ECO:0000269|PubMed:16797530,
ECO:0000269|PubMed:18638474, ECO:0000269|PubMed:19932097,
ECO:0000269|PubMed:20209123, ECO:0000269|PubMed:7670468,
ECO:0000269|PubMed:7736575, ECO:0000269|PubMed:8752219}.
-!- DEVELOPMENTAL STAGE: Isoform 1 is the major form expressed in the
dorsal root ganglia at 14.5 dpc. Isoform 2 is predominantly
expressed in the myocardium, skeletal muscles, bone cartilage and
epithelia of the tongue at 14.5 dpc. Isoform 5 is expressed at
high levels in the epidermis and mucosal epithelia of the
digestive tracts at 14.5 dpc. {ECO:0000269|PubMed:11514586,
ECO:0000269|PubMed:7670468}.
-!- DOMAIN: Its association with epidermal and simple keratins is
dependent on the tertiary structure induced by heterodimerization
of these intermedaite filaments proteins and most likely involves
recognition sites located in the rod domain of these keratins.
-!- DOMAIN: The microtubule tip localization signal (MtLS) motif;
mediates interaction with MAPRE1 and targeting to the growing
microtubule plus ends. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show progressive deterioration in motor
function and sensory neurodegeneration. Exhibit axonal swellings
packed with disorganized intermediate filaments (IFs) and
microtubules. Show poorly defined Z lines and display a reduction
in sarcomere length. Have increased accumulation of vesicles and
severely disrupted retrograde axonal transport. In stratified
epithelia, hemidesmosomes are normal but they lack the inner plate
and have no cytoskeleton attached. {ECO:0000269|PubMed:10357897,
ECO:0000269|PubMed:10428034, ECO:0000269|PubMed:14581450,
ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:7736575}.
-!- SIMILARITY: Belongs to the plakin or cytolinker family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK83382.1; Type=Miscellaneous discrepancy; Note=Many conflicts and frameshifts that might be strain-specific.; Evidence={ECO:0000305};
Sequence=AAK83383.1; Type=Miscellaneous discrepancy; Note=Many conflicts and frameshifts that might be strain-specific.; Evidence={ECO:0000305};
Sequence=AAK83384.1; Type=Miscellaneous discrepancy; Note=Many conflicts and frameshifts that might be strain-specific.; Evidence={ECO:0000305};
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EMBL; AF396877; AAK83382.1; ALT_SEQ; mRNA.
EMBL; AF396878; AAK83383.1; ALT_SEQ; mRNA.
EMBL; AF396879; AAK83384.1; ALT_SEQ; mRNA.
EMBL; AC123072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC127433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U22452; AAC52230.1; -; mRNA.
EMBL; U25158; AAC52231.1; ALT_FRAME; mRNA.
EMBL; DQ023311; AAY46942.1; -; mRNA.
EMBL; DQ463750; ABF00406.1; -; mRNA.
EMBL; AK051626; BAC34695.1; -; mRNA.
EMBL; AK037206; BAC29753.1; -; mRNA.
EMBL; AF115383; AAD22959.1; -; mRNA.
EMBL; AB085694; BAB93448.1; -; mRNA.
CCDS; CCDS35534.1; -. [Q91ZU6-1]
CCDS; CCDS35535.1; -. [Q91ZU6-2]
CCDS; CCDS69875.1; -. [Q91ZU6-5]
PIR; A60776; A60776.
PIR; I49290; I49290.
PIR; I49298; I49298.
RefSeq; NP_034211.2; NM_010081.2. [Q91ZU6-5]
RefSeq; NP_598594.2; NM_133833.3. [Q91ZU6-2]
RefSeq; NP_604443.2; NM_134448.3. [Q91ZU6-1]
UniGene; Mm.336625; -.
UniGene; Mm.478284; -.
UniGene; Mm.487428; -.
PDB; 2IAK; X-ray; 3.00 A; A=580-803.
PDBsum; 2IAK; -.
ProteinModelPortal; Q91ZU6; -.
SMR; Q91ZU6; -.
BioGrid; 199328; 2.
IntAct; Q91ZU6; 6.
MINT; MINT-1861530; -.
STRING; 10090.ENSMUSP00000095392; -.
ChEMBL; CHEMBL2176789; -.
iPTMnet; Q91ZU6; -.
PhosphoSitePlus; Q91ZU6; -.
REPRODUCTION-2DPAGE; IPI00230689; -.
REPRODUCTION-2DPAGE; IPI00230690; -.
REPRODUCTION-2DPAGE; IPI00284272; -.
PaxDb; Q91ZU6; -.
PeptideAtlas; Q91ZU6; -.
PRIDE; Q91ZU6; -.
Ensembl; ENSMUST00000097785; ENSMUSP00000095392; ENSMUSG00000026131. [Q91ZU6-1]
Ensembl; ENSMUST00000097786; ENSMUSP00000095393; ENSMUSG00000026131. [Q91ZU6-2]
Ensembl; ENSMUST00000183302; ENSMUSP00000138376; ENSMUSG00000026131. [Q91ZU6-5]
GeneID; 13518; -.
KEGG; mmu:13518; -.
UCSC; uc007aoi.2; mouse. [Q91ZU6-1]
UCSC; uc007aoj.2; mouse. [Q91ZU6-2]
UCSC; uc007aok.1; mouse. [Q91ZU6-8]
UCSC; uc007aol.2; mouse. [Q91ZU6-5]
CTD; 667; -.
MGI; MGI:104627; Dst.
eggNOG; KOG0516; Eukaryota.
eggNOG; KOG0517; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00760000119163; -.
HOVERGEN; HBG031127; -.
InParanoid; Q91ZU6; -.
KO; K10382; -.
Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-MMU-446107; Type I hemidesmosome assembly.
ChiTaRS; Dst; mouse.
EvolutionaryTrace; Q91ZU6; -.
PRO; PR:Q91ZU6; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026131; -.
CleanEx; MM_DST; -.
ExpressionAtlas; Q91ZU6; baseline and differential.
Genevisible; Q91ZU6; MM.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0031673; C:H zone; IDA:UniProtKB.
GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
GO; GO:0030018; C:Z disc; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0007409; P:axonogenesis; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
GO; GO:0046907; P:intracellular transport; IDA:UniProtKB.
GO; GO:0008090; P:retrograde axonal transport; IMP:UniProtKB.
CDD; cd00014; CH; 2.
CDD; cd00051; EFh; 1.
Gene3D; 1.10.418.10; -; 2.
Gene3D; 3.30.920.20; -; 1.
Gene3D; 3.90.1290.10; -; 3.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR036872; Calponin-like_dom_sf.
InterPro; IPR001715; CH-domain.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR003108; GAR_dom.
InterPro; IPR036534; GAR_dom_sf.
InterPro; IPR035915; Plakin_repeat_sf.
InterPro; IPR001101; Plectin_repeat.
InterPro; IPR018159; Spectrin/alpha-actinin.
InterPro; IPR002017; Spectrin_repeat.
Pfam; PF00307; CH; 2.
Pfam; PF13499; EF-hand_7; 1.
Pfam; PF02187; GAS2; 1.
Pfam; PF00681; Plectin; 2.
Pfam; PF00435; Spectrin; 18.
SMART; SM00033; CH; 2.
SMART; SM00054; EFh; 2.
SMART; SM00243; GAS2; 1.
SMART; SM00250; PLEC; 9.
SMART; SM00150; SPEC; 33.
SUPFAM; SSF143575; SSF143575; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF75399; SSF75399; 2.
PROSITE; PS00019; ACTININ_1; 1.
PROSITE; PS00020; ACTININ_2; 1.
PROSITE; PS50021; CH; 2.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 2.
PROSITE; PS51460; GAR; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative promoter usage;
Alternative splicing; Calcium; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing;
Endoplasmic reticulum; Intermediate filament; Isopeptide bond;
Lipoprotein; Membrane; Metal-binding; Microtubule; Muscle protein;
Myristate; Nucleus; Palmitate; Phosphoprotein; Reference proteome;
Repeat; SH3 domain; Transmembrane; Ubl conjugation.
CHAIN 1 7393 Dystonin.
/FTId=PRO_0000078141.
DOMAIN 35 138 Calponin-homology (CH) 1.
{ECO:0000255|PROSITE-ProRule:PRU00044,
ECO:0000305}.
DOMAIN 151 255 Calponin-homology (CH) 2.
{ECO:0000255|PROSITE-ProRule:PRU00044,
ECO:0000305}.
REPEAT 701 801 Spectrin 1.
DOMAIN 889 941 SH3. {ECO:0000305}.
REPEAT 1582 1624 Plectin 1.
REPEAT 1657 1701 Plectin 2.
REPEAT 1772 1815 Plectin 3.
REPEAT 1816 1844 Plectin 4.
REPEAT 1848 1889 Plectin 5.
REPEAT 3850 3930 Spectrin 2.
REPEAT 4002 4084 Spectrin 3.
REPEAT 4445 4553 Spectrin 4.
REPEAT 4557 4662 Spectrin 5.
REPEAT 4780 4882 Spectrin 6.
REPEAT 5213 5320 Spectrin 7.
REPEAT 5327 5428 Spectrin 8.
REPEAT 5435 5537 Spectrin 9.
REPEAT 5651 5755 Spectrin 10.
REPEAT 5762 5860 Spectrin 11.
REPEAT 6006 6086 Spectrin 12.
REPEAT 6093 6195 Spectrin 13.
REPEAT 6201 6304 Spectrin 14.
REPEAT 6312 6414 Spectrin 15.
REPEAT 6419 6523 Spectrin 16.
REPEAT 6527 6633 Spectrin 17.
REPEAT 6640 6740 Spectrin 18.
REPEAT 6745 6848 Spectrin 19.
DOMAIN 7019 7054 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 7055 7090 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 7095 7173 GAR. {ECO:0000255|PROSITE-
ProRule:PRU00792}.
CA_BIND 7032 7043 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 7068 7079 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
REGION 35 252 Actin-binding.
MOTIF 1382 1388 Nuclear localization signal; in isoform
6.
MOTIF 7373 7376 Microtubule tip localization signal.
COMPBIAS 2367 2427 Asp-rich.
MOD_RES 236 236 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1381 1381 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2211 2211 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2862 2862 Phosphoserine.
{ECO:0000250|UniProtKB:Q03001}.
MOD_RES 3894 3894 Phosphoserine.
{ECO:0000250|UniProtKB:Q03001}.
MOD_RES 4680 4680 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 5488 5488 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 7254 7254 Phosphoserine.
{ECO:0000250|UniProtKB:Q03001}.
MOD_RES 7333 7333 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 7336 7336 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 7348 7348 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 5401 5401 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q03001}.
VAR_SEQ 1 381 MAGYLSPAAYMYVEEQEYLQAYEDVLERYKDERDKVQKKTF
TKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLP
REKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNP
KLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLWTQQA
TEGYAGVRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAV
QSNLANLEHAFYVAEKIGVIRLLDPEDVDVSSPDEKSVITY
VSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWI
RHHVVTMSERTFPNNPLELKALYNQYLQFKEKEIPPKEMEK
SKIKRLYKLLEIWIEFGRIKLLQGYHPNDIEKEWGKLIIAM
LEREKALRPEVE -> MQSSSYSYRSSDSVFSNTTSTRTSL
DSNENLLSVHCGPTLINSCISFSNESLDGH (in
isoform 5).
{ECO:0000303|PubMed:11514586}.
/FTId=VSP_055459.
VAR_SEQ 1 137 MAGYLSPAAYMYVEEQEYLQAYEDVLERYKDERDKVQKKTF
TKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLP
REKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNP
KLTLGLIWTIILHF -> MGNVCGCVRAEKEEPYFDPAKSP
LSPEKYSPGRKYFRRKPCQKVVDDTEPVRQSSEREGKKGVS
QPAGGQPAVSSGELPWEDPAASPTKEDAVQLGKRAATEHGD
QKPLPSSVDGYPHRVTVSSAQGRYSEVQVSIPDKIISEEDS
PPYCPETERHLDDVNSKHRTFLRKDNVSLSQTAASSSPILC
VTEKSLKNSALMGNLSRSCHSVLEQDSDERGHPFGVHRLQL
TKRRCHSLSSGVSCVSKDAPRDDGC (in isoform 7).
{ECO:0000303|PubMed:16797530}.
/FTId=VSP_041542.
VAR_SEQ 1 30 MAGYLSPAAYMYVEEQEYLQAYEDVLERYK -> MIAAAFL
VLLRPYSIQCALFLLLLLLGTVATIVFFCCWHRKLQKGRHP
MKSVFSGRSRSRDAALRSHHFRSEGFRASPRHIRRRVAAAA
AARLEEVKPVVEVHHQSEQESSGRKRRIKKNSRVQPEFYHS
VQGASTRRPSSGNASYRCSMSSSADFSDEDDFSQKSGSASP
APGDTLPWNLPKHERSKRKIQGGSVLDPAERAVLRIA (in
isoform 6).
{ECO:0000303|PubMed:16289082}.
/FTId=VSP_041543.
VAR_SEQ 271 272 VK -> KG (in isoform 7).
{ECO:0000303|PubMed:16797530}.
/FTId=VSP_041544.
VAR_SEQ 273 7393 Missing (in isoform 7).
{ECO:0000303|PubMed:16797530}.
/FTId=VSP_041545.
VAR_SEQ 305 7393 Missing (in isoform 6).
{ECO:0000303|PubMed:16289082}.
/FTId=VSP_041546.
VAR_SEQ 1432 1432 K -> MKRSKENSEHGAYSDLLQRQRATMVENSKLTGKISE
LETMVAELKKQKSRVEEELPKVKEAAENELRKQQRNVEDIA
LQKLRAESEAKQYRRELETIVREKEAAERELERVRQLTAEA
EARRAAVEENLRNFRSQLQENTFTRQTLEDHLRRKDSSLSD
LEQQKRALVEELQRKRDHEEELLRLVKQMERDLAFQKQVAE
KQLKEKQKVELEARRKITEIQFSCRESAAVAQARPQREQGR
QKEEELKQQVDELTLANRKAEKEMRELKYELSAVQLEKASS
EEKARLLKDKLDETNNTLKCLKEDLERKDQAQERYSQQLRD
LGRQLNQTTDKAEEVRQEANDLKKIKHTYQLELESLHQEKG
KLQREVDRVTRAHALAERNIQCLNSQVHASRDEKDLSEERR
RLCQRKSDHLKEEFERSHAQLLQNIQAEKENNDKIQKLNKE
LEKSNECAETLKQKVDELTRQNNETKLMMQRIQAESKNIVR
EKQAIQQRCEVLRIQADGFKDQLRNTNEHLHKQTKTEQDFH
RKIKSLEDDLAQSQNLVSEFKQKCDQQSMIIQKTEKEVRSL
SAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHL
KTIEEQMTHRKMILLQEESDKFKRSADEFRKKMEKLMESKV
VTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQL
QCYREKMQQGPPVEANHYQKCRRLEEELLAQRREVENLKQK
MDQQIKEHEHQLLRLQCEIQKKSTTQDHTFASAFDTAGREC
HHPAEISPGNSGHLNLKTRLPLSRWTQEPHQTEGKWPHRAA
EQLPKEVQFRQPGAPLDRESSQPCYSEYFSQTSTELQITFD
DKNPITRLSELETMREQALHPSRPPVTYQDDKLERELVKLL
TPLEIAKNKQCGMHTEVTTLKQEKRLGSSAGGWMLEGCRTS
GGLKGDFLKKSVEPEASPSLDLNQACSVRDEEFQFQGLRHT
VTGRQLVEAKLLDMRTVEQLRLGLKTVEEVQRSLSKFLTKA
TSIAGLYLESSKEKMSFTSAAQKIIIDKMIALAFLEAQAAT
GFIIDPVSGQTYCVEDAVLHGIVDPEFRSRLLEAEKAVLGY
SHASKTLSVFQAMENRMLDRKKGKHILEAQIASGGVIDPVR
GVRVPPEMAVQQGLLNNAVLQFLHEPSSNTRVFPNPNNKQA
LYYSELLQICVFDVDCQCFLLPFGEREISNLNIEKTHKIAV
VDTKTGAELTAFEAFQRNLIDKGIYLELSGQQYQWKEATFF
DSYGHPSHMLTDTKTGLQFNISEAVEQGTLDKALVQKYQEG
LTTLTELADFLLSKVVPKKDLHSPIAGYWLTASGERISLLK
ASRRNLVDRVTALRCLEAQICTGGIIDPLTGKKYRVAEALH
RGLVDEGFAQQLRQCELVITGISHPVSNKMMSVVEAVNANI
ISKEMGMRCLEFQYLTGGLIEPKVFSRLTIEEALHVGIIDV
LIATRLKDQKSYVRDIMCPQTKRKLTYKEALEKADFDFHTG
LKLLEVSEPLGTGISNLYYSSQ (in isoform 5).
{ECO:0000303|PubMed:11514586}.
/FTId=VSP_055460.
VAR_SEQ 1433 7393 Missing (in isoform 5).
{ECO:0000303|PubMed:11514586}.
/FTId=VSP_055461.
VAR_SEQ 1549 3562 Missing (in isoform 1).
{ECO:0000303|PubMed:11514586}.
/FTId=VSP_041549.
VAR_SEQ 7129 7134 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_041550.
VAR_SEQ 7174 7197 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_041551.
VAR_SEQ 7265 7265 K -> KILHPLTRNYGKPWLANSKMSTPCKAAECPDFPVSS
AE (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_041552.
MUTAGEN 1385 1385 R->A: Prevents isoform 6 from localizing
to the nucleus; when associated with A-
1386. {ECO:0000269|PubMed:14576348}.
MUTAGEN 1386 1386 R->A: Prevents isoform 6 from localizing
to the nucleus; when associated with A-
1385. {ECO:0000269|PubMed:14576348}.
HELIX 590 593 {ECO:0000244|PDB:2IAK}.
STRAND 594 596 {ECO:0000244|PDB:2IAK}.
HELIX 600 604 {ECO:0000244|PDB:2IAK}.
HELIX 608 623 {ECO:0000244|PDB:2IAK}.
HELIX 631 650 {ECO:0000244|PDB:2IAK}.
HELIX 652 661 {ECO:0000244|PDB:2IAK}.
HELIX 662 664 {ECO:0000244|PDB:2IAK}.
TURN 667 669 {ECO:0000244|PDB:2IAK}.
HELIX 670 686 {ECO:0000244|PDB:2IAK}.
TURN 687 689 {ECO:0000244|PDB:2IAK}.
HELIX 690 722 {ECO:0000244|PDB:2IAK}.
HELIX 744 767 {ECO:0000244|PDB:2IAK}.
HELIX 773 793 {ECO:0000244|PDB:2IAK}.
SEQUENCE 7393 AA; 834218 MW; C3CDF88978C33EF1 CRC64;
MAGYLSPAAY MYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM KVRKHVNDLY
EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL DYLKRRQVKL VNIRNDDITD
GNPKLTLGLI WTIILHFQIS DIHVTGESED MSAKERLLLW TQQATEGYAG VRCENFTTCW
RDGKLFNAII HKYRPDLIDM NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE
KSVITYVSSL YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VVTMSERTFP
NNPLELKALY NQYLQFKEKE IPPKEMEKSK IKRLYKLLEI WIEFGRIKLL QGYHPNDIEK
EWGKLIIAML EREKALRPEV ERLDMLQQIA TRVQRDSVSC EDKLILARNA LQSDSKRLES
GVQFQNEAEI AGYILECENL LRQHVIDVQI LIDGKYYQAD QLVQRVAKLR DEIMALRNEC
SSVYSKGRML TTEQTKLMIS GITQSLNSGF AQTLHPSLNS GLTQSLTPSL TSSSVTSGLS
SGMTSRLTPS VTPVYAPGFP SVVAPNFSLG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE
EEVNMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE FESSLKEAKI
SEIQMTAPLK LSYTDKLHRL ESQYAKLLNT SRNQERHLDT LHNFVTRATN ELIWLNEKEE
SEVAYDWSER NSSVARKKSY HAELMRELEQ KEESIKAVQE IAEQLLLENH PARLTIEAYR
AAMQTQWSWI LQLCQCVEQH IQENSAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI
HKLEDLVQES MEKEELLQYR SVVAGLMGRA KTVVQLKPRN PDNPLKTSIP IKAICDYRQI
EITIYKDDEC VLANNSHRAK WKVISPTGNE AMVPSVCFTV PPPNKEAVDF ANRIEQQYQS
VLTLWHESHI NMKSVVSWHY LVNEIDRIRA SNVASIKTML PGEHQQVLSN LQSRLEDFLE
DSQESQIFSG SDISQLEKEV SVCRKYYQEL LKSAEREEQE ESVYNLYISE VRNIRLRLES
CEDRLIRQIR TPLERDDLHE SMLRITEQEK LKKELDRLKD DLGTITNKCE EFFSQAADSP
SVPALRSELS VVIQSLSQIY SMSSTYIEKL KTVNLVLKNT QAAEALVKLY ETKLCEEEAV
IADKNNIENL MSTLKQWRSE VDEKREVFHA LEDELQKAKA ISDEMFKTHK ERDLDFDWHK
EKADQLVERW QSVHVQIDNR LRDLEGIGKS LKHYRDSYHP LDDWIQHIET TQRKIQENQP
ENSKALALQL NQQKMLVSEI EVKQSKMDEC QKYSEQYSAA VKDYELQTMT YRAMVESQQK
SPVKRRRIQS SADLVIQEFM DLRTRYTALV TLMTQYIKFA GDSLKRLEEE EKSLDEEKKQ
HIEKAKELQK WVSNISKTLG DGEKAGKPLF SKQQMSSKEI STKKEQFSEA LQTTQIFLAK
HGDKLTEEER SDLEKQVKTL QEGYNLLFSE SLKQQELQPS GESKVPEKPD KVIAGTINQT
TGEVLSVFQA VLRGLIDYET GIRLLEAQLV ITGLISPELR KCFDLRDAES HGLIDEQVLR
QLKELNRAKQ LISTASPTSI PVLDSLAQGM VSESMAIRVL EILLSAGPLL VPATGEHLTL
QQAFQQNLIS SALFSKVLER QDTCKDLIDP CTSEKVSLTD MVQRSILQEN TRMWLLPVRP
QEAGRITLKC GRSVSILRAA HEGLIDRETM FRLLGAQLLS GGLIDCNSGQ KMTVEEAVAE
GVIDRDTASS ILTYQVQTGG IVHSNPAKRL TVDEAVQCEL ITSSSALLVL EAQRGYVGLI
WPHSGEIFPT SSSLQQELIT NELASKILNG RQKIAALYIP ESSQVIGLDA AKQLGIIDNN
TASVLKSVTL PDKMPDLGDL EDCKNAKRWL SFCKLQPSTV HDYRQEEGGS DGEEPVTAQS
SEQTKKLFLS YLMVNSYMDA HTGQRLLLYD GDLDEAVGML LESCGTELGA DTSTRESLSV
LTIPDAFPDC ALSEEKHECS AAAAGPDKCH YSHPGHKESL ENAKWDMNEA FCKMGNNDSN
GELPRPENLA DTTVVQKGSE SPSRVRVPKP TSSSTQPEGS VLRPESGSIL KGCKSQSEPV
TKKYPDGANH SHFLTSETSR PCDSNEREDE ENIQKGPSVF DYSPRLSALL SHDELRQSQG
RFSDTSTPQN TGYLCEASTL SPSDQRVLAD QSTREKFQDQ FLGIAAISVS LQGAPCGQKP
VDTECSSSQV HYHSEESMSD ASAESGATRQ TDESEKTGSK VEDNSCTMVP GGGSRNDNTS
DCGPLSHKGA IDAGDYETSL LAGQQSDTAT DSDSDDYFYD TPLFEDEDHD SLILQGDDRD
CLQPEDYDTS LQEENDRTPP PDDIFYDVMK EKENPEFPHG GMDESLGVEN KVCCPQGFPV
GIEKPELYLA GEKEFNSGGS EQLVESVSES ENPPGLWDSE SDSLTEGEII GRKERLGASL
TPDGHWRGDR EECDTSRESQ SDTDGVGSIQ SSESYRPYMS DGSDLDEEDN GGRSSEDSGD
GRGGQGVADE GGEPQYQADP TQLYTAIRKE HGGETQNVSD MIPLDKTHSY SPLETQHGAG
VFQPESAGRG GWDTERSSHP ELTTEADEED EASLSTHMAT KGVSLSNAEG TASEEIRLVQ
GPDSTGILKA EDLENVSPEI SPSSDNIVRS EAELGGGASE DGHLSFTGSD RDQQGPGRGL
VKGRDGQSDK LVDETSIREM GFQKEGVLMS SPEEGGEEER DLEPFPNGSA TESLNMGKSQ
VPPLLTHTEE LSHRGAPHTT TMTTTMTLEG EAKNVQTGLT ESPVLLETLA EIFDTPASKV
TRADLTSAVT ASEMKSQVKE DSLTGGPEKE TGPCTSLGHC DKCIHVDMLE PNEHTPSCAL
VAPPTVKDNL CSVNNAGEKS VRPQEDWPPA AEVRLSDACV EESISEGKAG ILQFTPENSD
STLSRLPHQS VAGWGKSADS VQARLPVSGV RHTSADTLDV GCPQLESSRE KASAEEEPHR
ERALSLKPQE REHHMLGFVE DGRSILKSSL DKVHMNLQEV GDPSAGTGTK ISIQNLIRRA
ILSELPNEVS NVPSHGISPI SNSSEVRAES GGDPFCITSF LHLLKQNQPP QETPGISELA
KVLTQMDCDP EQRGLGSELL PPQLKNAFYK LLFDGYATEK DQAEALGQTS CAVPKMAEEK
PHVCSDLRNK EGHHCPLNPQ AVGEAEVEPF SVHIAALPGG EKLGELCSEP PEHSESTSGS
KERSSDSSSK EKCSNGLQQC LQHTEKMHEY LVLLQDMKPP LDNQASVESS LEALKSQLKQ
LEAFELGLAP IAVFLRKDLK LAEEFLKSFP SDLPRRHHEE LSKSHQRLQN AFSSLSSVSS
ERMKLIKLAI NSEMSKLAVR HEDFLHKLTS YSDWVSEKSR SVKAIQTVNV QDTELVKNSV
KFLKNVLADL SHTKMQLETT AFDVQSFISD YAQDLSPSQS RQLLRLLNTT QKGFLDLQEL
VTTEADRLEA LLQLEQELGH QKVVAERQQE YREKLQGLCD LLTQTENRLI SNQEAFVIGD
GTVELQKYQS KQEELQRDMQ GSTQAMEEIV RNTELFLKES GDELSQADRA LIEQKLNEVK
MKCAQLNLKA EQSRKELDKA VTTALKEETE KVAAVRQLEE SKTKIENLLN WLSNVEEDSE
GVWTKHTQPM EQNGTYLHEG DSKLGAGEED EVNGNLLETD AEGHSEATKG NLNQQYEKVK
AQHGKIMAQH QAVLLATQSA QVLLEKQGHY LSPEEKEKLQ KNTQELKVHY EKVLAECEKK
VKLTHSLQEE LEKFDTDYSE FEHWLQQSEQ ELANLEAGAD DLSGLMDKLT RQKSFSEDVI
SHKGDLRYIT ISGNRVIDAA KSCSKRDSDR IGKDSVETSA THREVQTKLD QVTDRFRSLY
SKCSVLGNNL KDLVDQYQQY EDASCGLLSG LQACEAKASK HLREPIALDP KNLQRQLEET
KALQGQISSQ QVAVEKLKKT AEVLLDAKGS LLPAKNDIQK TLDDIVGRYD DLSKCVNERN
EKLQITLTRS LSVQDALDEM LDWMGSVESS LVKPGQVPLN STALQDLISK DTMLEQDITG
RQSSINAMNE KVKTFIETTD PSTASSLQAK MKDLSARFSE ASQKHKEKLA KMVELKAKVE
QFEKLSDKLQ TFLETQSQAL TEVAMPGKDV PELSQHMQES TAKFLEHRKD LEALHSLLKE
ISSHGLPGDK ALVFEKTNNL SRKFKEMEDT IQEKKDALSS CQEQLSAFQT LAQSLKTWIK
ETTKQVPVVK PSLGTEDLRK SLEETKKLQE KWNLKAPEIH KANNSGVSLC NLLSALISPA
KAIAAAKSGG VILNGEGTDT NTQDFLANKG LTSIKKDMTD ISHSYEDLGL LLKDKIVELN
TKLSKLQKAQ EESSAMMQWL EKMNKTASRW RQTPTPADTE SVKLQVEQNK SFEAELKQNV
NKVQELKDKL SELLEENPEA PEAQSWKQAL AEMDTKWQEL NQLTMDRQQK LEESSNNLTQ
FQTTEAQLKQ WLMEKELMVS VLGPLSIDPN MLNTQKQQVQ ILLQEFDTRK PQYEQLTAAG
QGILSRPGED PSLHGIVNEQ LEAVTQKWDN LTGQLRDRCD WIDQAIVKST QYQSLLRSLS
GTLTELDDKL SSGLTSGALP DAVNQQLEAA QRLKQEIEQQ APKIKEAQEV CEDLSALVKE
EYLKAELSRQ LEGILKSFKD IEQKTENHVQ HLQSACASSH QFQQMSKDFQ AWLDAKKEEQ
RDSPPISAKL DVLESLLNSQ KDFGKTFTEQ SNIYEKTISE GENLLLKTQG AEKAALQLQL
NTMKTDWDRF RKQVKEREEK LKDSLEKALK YREQVETLRP WIDRCQHSLD GVTFSLDPTE
SESSIAELKS LQKEMDHHFG MLELLNNTAN SLLSVCEVDK EAVTEENQSL MEKVNRVTEQ
LQSKTVSLEN MAQKFKEFQE VSRDTQRQLQ DTKEQLEVHH SLGPQAYSNK HLSVLQAQQK
SLQTLKQQVD EAKRLAQDLV VEAADSKGTS DVLLQAETLA EEHSELSQQV DEKCSFLETK
LQGLGHFQNT IREMFSQFTE CDDELDGMAP VGRDAETLRK QKACMQTFLK KLEALMASND
SANRTCKMML ATEETSPDLI GVKRDLEALS KQCNKLLDRA KTREEQVDGA TEKLEEFHRK
LEEFSTLLQK AEEHEESQGP VGTETETINQ QLDVFKVFQK EEIEPLQVKQ QDVNWLGQGL
IQSAAANTCT QGLEHDLDSV NSRWKTLNKK VAQRTSQLQE ALLHCGRFQD ALESLLSWMA
DTEELVANQK PPSAEFKVVK AQIQEQKLLQ RLLEDRKSTV EVIKREGEKI AASAEPADRV
KLTRQLSLLD SRWEALLSRA EARNRQLEGI SVVAQEFHET LEPLNEWLTA VEKKLANSEP
IGTQAPKLEE QISQHKALQE DILLRKQSVD QALLNGLELL KQTTGDEVLI IQDKLEAIKA
RYKDITKLSA DVAKTLEHAL QLAGQLQSMH KELCNWLDKV EVELLSYETQ GLKGEAASQV
QERQKELKNE VRSNKALVDS LNEVSSALLE LVPWRAREGL EKTIAEDNER YRLVSDTITQ
KVEEIDAAIL RSQQFEQAAD AELSWITETQ KKLMSLGDIR LEQDQTSAQL QVQKAFTMDI
LRHKDIIDEL VTSGHKIMTT SSEEEKQSMK KKLDKVLKKY DAVCQINSER HLQLERAQSL
VSQFWETYEE LWPWLTETQR IISQLPAPAL EYETLRRQQE EHRQLRELIA EHKPHIDKMN
KTGPQLLELS PKEGIYIQEK YVAADTLYSQ IKEDVKKRAV VLDEAISQST QFHDKIDQIL
ESLERIAERL RQPPSISAEV EKIKEQIGEN KSVSVDMEKL QPLYETLRQR GEEMIARSEG
TEKDVSARAV QDKLDQMVFI WGSIHTLVEE REAKLLDVME LAEKFWCDHM SLVVTIKDTQ
DFIRDLEDPG IDPSVVKQQQ EAAEAIREEI DGLQEELDMV ITLGSELIAA CGEPDKPIVK
KSIDELNSAW DSLNKAWKDR VDRLEEAMQA AVQYQDGLQG IFDWVDIAGN KLATMSPIGT
DLETVKQQIE ELKQFKSEAY QQQIEMERLN HQAELLLKKV TEEADKHTVQ DPLMELKLIW
DSLDERIVSR QHKLEGALLA LGQFQHALDE LLAWLTHTKG LLSEQKPVGG DPKAIEIELA
KHHVLQNDVL AHQSTVEAVN KAGNDLIESS EGEEASNLQY KLRILNQRWQ DILEKTDQRK
QQLDSALRQA KGFHGEIEDL QQWLTDTERH LLASKPLGGL PETAKEQLNA HMEVCTAFAI
KEETYKSLML RGQQMLARCP RSAETNIDQD ITNLKEKWES VKSKLNEKKT KLEEALHLAM
NFHNSLQDFI NWLTQAEQTL NVASRPSLIL DTILFQIDEH KVFANEVNSH REQIIELDKT
GTHLKYFSQK QDVVLIKNLL ISVQSRWEKV VQRLVERGRS LDEARKRAKQ FHEAWSKLME
WLEESEKSLD SELEIANDPD KIKAQLVQHK EFQKSLGGKH SVYDTTNRTG RSLKEKTSLA
DDNLKLDNML SELRDKWDTI CGKSVERQNK LEEALLFSGQ FTDALQALID WLYRVEPQLA
EDQPVHGDID LVMNLIDNHK VFQKELGKRT SSVQALKRSA RELIEGSRDD SSWVRVQMQE
LSTRWETVCA LSISKQTRLE SALQQAEEFH SVVHTLLEWL AEAEQTLRFH GALPDDEDAL
RTLIEQHKEF MKRLEEKRAE LSKATGMGDA LLAVCHPDSI TTIKHWITII QARFEEVLAW
AKQHQQRLAG ALAGLIAKQE LLETLLAWLQ WAETTLTEKD KEVIPQEIEE VKTLIAEHQT
FMEEMTRKQP DVDKVTKTYK RRATDPPSLQ SHIPVLDKGR AGRKRFPASG FYPSGSQTQI
ETKNPRVNLL VSKWQQVWLL ALERRRKLND ALDRLEELRE FANFDFDIWR KKYMRWMNHK
KSRVMDFFRR IDKDQDGKIT RQEFIDGILS SKFPTSRLEM SAVADIFDRD GDGYIDYYEF
VAALHPNKDA YKPITDADKI EDEVTRQVAK CKCAKRFQVE QIGDNKYRFF LGNQFGDSQQ
LRLVRILRST VMVRVGGGWM ALDEFLVKND PCRVHHHGSK MLRSESNSSI TATQPTLAKG
RTNMELREKF ILADGASQGM AAFRPRGRRS RPSSRGASPN RSTSASSHAC QAASPPVPAA
ASTPKGTPIQ GSKLRLPGYL SGKGFHSGED SALITTAAAR VRTQFAESRK TPSRPGSRAG
SKAGSRASSR RGSDASDFDI SEIQSVCSDV ETVPQTHRPV PRAGSRPSTA KPSKIPTPQR
RSPASKLDKS SKR


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