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Myosin-17 (Myosin XI K) (AtXIK)

 MYO17_ARATH             Reviewed;        1531 AA.
F4K5J1; E9N630; F4K5J2; K9KY88; Q0WQJ2;
26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
26-JUN-2013, sequence version 2.
23-MAY-2018, entry version 61.
RecName: Full=Myosin-17;
AltName: Full=Myosin XI K;
Short=AtXIK;
Name=XI-K; Synonyms=XIK; OrderedLocusNames=At5g20490;
ORFNames=F7C8.80;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
PubMed=21233331; DOI=10.1104/pp.110.170720;
Peremyslov V.V., Mockler T.C., Filichkin S.A., Fox S.E., Jaiswal P.,
Makarova K.S., Koonin E.V., Dolja V.V.;
"Expression, splicing, and evolution of the myosin gene family in
plants.";
Plant Physiol. 155:1191-1204(2011).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Park E., Nebenfuehr A.;
"Transport of secretory vesicle by myosin XIK is necessary for
maintenance of optimal tip growth in root hairs of Arabidopsis
thaliana.";
Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1270-1531.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
GENE FAMILY.
PubMed=10984423;
Hodge T., Cope M.J.;
"A myosin family tree.";
J. Cell Sci. 113:3353-3354(2000).
[7]
GENE FAMILY.
PubMed=11516337; DOI=10.1186/gb-2001-2-7-research0024;
Reddy A.S., Day I.S.;
"Analysis of the myosins encoded in the recently completed Arabidopsis
thaliana genome sequence.";
Genome Biol. 2:RESEARCH0024.1-RESEARCH0024.17(2001).
[8]
SUBCELLULAR LOCATION.
PubMed=17288617; DOI=10.1186/1471-2229-7-6;
Reisen D., Hanson M.R.;
"Association of six YFP-myosin XI-tail fusions with mobile plant cell
organelles.";
BMC Plant Biol. 7:6-6(2007).
[9]
DOMAIN, AND SUBCELLULAR LOCATION.
PubMed=17500056; DOI=10.1074/jbc.M700645200;
Li J.F., Nebenfuehr A.;
"Organelle targeting of myosin XI is mediated by two globular tail
subdomains with separate cargo binding sites.";
J. Biol. Chem. 282:20593-20602(2007).
[10]
TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17458634; DOI=10.1007/s00709-006-0233-8;
Ojangu E.L., Jaerve K., Paves H., Truve E.;
"Arabidopsis thaliana myosin XIK is involved in root hair as well as
trichome morphogenesis on stems and leaves.";
Protoplasma 230:193-202(2007).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18503043; DOI=10.1093/jxb/ern114;
Sparkes I.A., Teanby N.A., Hawes C.;
"Truncated myosin XI tail fusions inhibit peroxisome, Golgi, and
mitochondrial movement in tobacco leaf epidermal cells: a genetic tool
for the next generation.";
J. Exp. Bot. 59:2499-2512(2008).
[12]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=18178669; DOI=10.1104/pp.107.113654;
Peremyslov V.V., Prokhnevsky A.I., Avisar D., Dolja V.V.;
"Two class XI myosins function in organelle trafficking and root hair
development in Arabidopsis.";
Plant Physiol. 146:1109-1116(2008).
[13]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19060218; DOI=10.1073/pnas.0810730105;
Prokhnevsky A.I., Peremyslov V.V., Dolja V.V.;
"Overlapping functions of the four class XI myosins in Arabidopsis
growth, root hair elongation, and organelle motility.";
Proc. Natl. Acad. Sci. U.S.A. 105:19744-19749(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1517, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[15]
FUNCTION.
PubMed=19369591; DOI=10.1104/pp.109.136853;
Avisar D., Abu-Abied M., Belausov E., Sadot E., Hawes C.,
Sparkes I.A.;
"A comparative study of the involvement of 17 Arabidopsis myosin
family members on the motility of Golgi and other organelles.";
Plant Physiol. 150:700-709(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1517, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[17]
FUNCTION.
PubMed=20581304; DOI=10.1105/tpc.110.076315;
Peremyslov V.V., Prokhnevsky A.I., Dolja V.V.;
"Class XI myosins are required for development, cell expansion, and F-
Actin organization in Arabidopsis.";
Plant Cell 22:1883-1897(2010).
[18]
DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20351265; DOI=10.1073/pnas.0911482107;
Ueda H., Yokota E., Kutsuna N., Shimada T., Tamura K., Shimmen T.,
Hasezawa S., Dolja V.V., Hara-Nishimura I.;
"Myosin-dependent endoplasmic reticulum motility and F-actin
organization in plant cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:6894-6899(2010).
[19]
FUNCTION.
PubMed=22672737; DOI=10.1186/1471-2229-12-81;
Ojangu E.L., Tanner K., Pata P., Jaerve K., Holweg C.L., Truve E.,
Paves H.;
"Myosins XI-K, XI-1, and XI-2 are required for development of pavement
cells, trichomes, and stigmatic papillae in Arabidopsis.";
BMC Plant Biol. 12:81-81(2012).
[20]
SUBCELLULAR LOCATION.
PubMed=22969781; DOI=10.3389/fpls.2012.00184;
Peremyslov V.V., Klocko A.L., Fowler J.E., Dolja V.V.;
"Arabidopsis Myosin XI-K localizes to the motile endomembrane vesicles
associated with F-actin.";
Front. Plant Sci. 3:184-184(2012).
[21]
FUNCTION.
PubMed=21914656; DOI=10.1093/jxb/err265;
Avisar D., Abu-Abied M., Belausov E., Sadot E.;
"Myosin XIK is a major player in cytoplasm dynamics and is regulated
by two amino acids in its tail.";
J. Exp. Bot. 63:241-249(2012).
[22]
INTERACTION WITH MYOB1; MYOB2 AND MYOB3.
PubMed=23995081; DOI=10.1105/tpc.113.113704;
Peremyslov V.V., Morgun E.A., Kurth E.G., Makarova K.S., Koonin E.V.,
Dolja V.V.;
"Identification of myosin XI receptors in Arabidopsis defines a
distinct class of transport vesicles.";
Plant Cell 25:3022-3038(2013).
[23]
INTERACTION WITH PHOX1 AND PHOX2.
PubMed=28096376; DOI=10.1073/pnas.1620577114;
Kurth E.G., Peremyslov V.V., Turner H.L., Makarova K.S., Iranzo J.,
Mekhedov S.L., Koonin E.V., Dolja V.V.;
"Myosin-driven transport network in plants.";
Proc. Natl. Acad. Sci. U.S.A. 114:E1385-E1394(2017).
-!- FUNCTION: Myosin heavy chain that is required for the cell cycle-
regulated transport of various organelles and proteins for their
segregation. Functions by binding with its tail domain to receptor
proteins on organelles and exerting force with its N-terminal
motor domain against actin filaments, thereby transporting its
cargo along polarized actin cables. Involved in the tip growth of
root hair cells and in the elongation of trichome stalk and
branches. Plays a major role in trafficking of Golgi stacks,
mitochondria and peroxisomes during root hair development. Acts as
the primary contributor to ER streaming with a major role in the
movement of Golgi bodies. Required for development of pavement
cells, trichomes, and stigmatic papillae.
{ECO:0000269|PubMed:17458634, ECO:0000269|PubMed:18178669,
ECO:0000269|PubMed:18503043, ECO:0000269|PubMed:19060218,
ECO:0000269|PubMed:19369591, ECO:0000269|PubMed:20351265,
ECO:0000269|PubMed:20581304, ECO:0000269|PubMed:21914656,
ECO:0000269|PubMed:22672737}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with MYOB1, MYOB2
and MYOB3 (PubMed:23995081). Interacts with PHOX1 and PHOX2
(PubMed:28096376). {ECO:0000250|UniProtKB:Q39160,
ECO:0000269|PubMed:23995081, ECO:0000269|PubMed:28096376}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17288617,
ECO:0000269|PubMed:17500056, ECO:0000269|PubMed:18503043,
ECO:0000269|PubMed:20351265, ECO:0000269|PubMed:22969781}.
Note=Colocalizes with peroxisome, cytoplasmic vesicles,
endomembrane vesicles, endoplasmic reticulum and/or organelles.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=F4K5J1-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed ubiquitously.
{ECO:0000269|PubMed:17458634}.
-!- DOMAIN: IQ domain mediates interaction with calmodulin.
{ECO:0000250}.
-!- DOMAIN: The tail domain is a globular cargo-binding domain.
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Impaired growth of root hair cells, twisted
shape of stem trichomes, and irregular size, branch positioning,
and branch expansion of leaf trichomes. Affected organization of
the ER network and orientation of the actin filament bundles.
{ECO:0000269|PubMed:17458634, ECO:0000269|PubMed:18178669,
ECO:0000269|PubMed:19060218, ECO:0000269|PubMed:20351265}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. Plant myosin class XI subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AER51968.1; Type=Frameshift; Positions=403, 412; Evidence={ECO:0000305};
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EMBL; AF296833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002688; AED92852.2; -; Genomic_DNA.
EMBL; HQ427882; ADV74830.1; -; mRNA.
EMBL; JN229265; AER51968.1; ALT_FRAME; mRNA.
EMBL; AK228703; BAF00607.1; -; mRNA.
RefSeq; NP_001318612.1; NM_001343671.1. [F4K5J1-1]
UniGene; At.43864; -.
SMR; F4K5J1; -.
BioGrid; 17447; 6.
STRING; 3702.AT5G20490.1; -.
iPTMnet; F4K5J1; -.
PaxDb; F4K5J1; -.
PRIDE; F4K5J1; -.
EnsemblPlants; AT5G20490.2; AT5G20490.2; AT5G20490. [F4K5J1-1]
GeneID; 832171; -.
Gramene; AT5G20490.2; AT5G20490.2; AT5G20490. [F4K5J1-1]
KEGG; ath:AT5G20490; -.
Araport; AT5G20490; -.
TAIR; locus:2149932; AT5G20490.
eggNOG; KOG0160; Eukaryota.
eggNOG; COG5022; LUCA.
HOGENOM; HOG000029608; -.
InParanoid; F4K5J1; -.
OrthoDB; EOG093600DR; -.
PRO; PR:F4K5J1; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; F4K5J1; baseline and differential.
Genevisible; F4K5J1; AT.
GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0035619; C:root hair tip; IDA:TAIR.
GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
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:0008017; F:microtubule binding; IEA:InterPro.
GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
GO; GO:0003774; F:motor activity; ISS:TAIR.
GO; GO:0007015; P:actin filament organization; IEA:InterPro.
GO; GO:0030048; P:actin filament-based movement; TAS:TAIR.
GO; GO:0051645; P:Golgi localization; IMP:TAIR.
GO; GO:0048467; P:gynoecium development; IGI:TAIR.
GO; GO:0090436; P:leaf pavement cell development; IGI:TAIR.
GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
GO; GO:0051646; P:mitochondrion localization; IMP:TAIR.
GO; GO:0060151; P:peroxisome localization; IMP:TAIR.
GO; GO:0048768; P:root hair cell tip growth; IMP:TAIR.
GO; GO:0048767; P:root hair elongation; IMP:TAIR.
GO; GO:0010091; P:trichome branching; IMP:TAIR.
GO; GO:0010090; P:trichome morphogenesis; IMP:TAIR.
CDD; cd15475; MyosinXI_CBD; 1.
CDD; cd01384; MYSc_Myo11; 1.
Gene3D; 3.40.850.10; -; 3.
InterPro; IPR002710; Dilute_dom.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR004009; Myosin_N.
InterPro; IPR037975; MyosinXI_CBD.
InterPro; IPR036018; MYSc_Myo11.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF01843; DIL; 1.
Pfam; PF00612; IQ; 4.
Pfam; PF00063; Myosin_head; 1.
Pfam; PF02736; Myosin_N; 1.
PRINTS; PR00193; MYOSINHEAVY.
SMART; SM01132; DIL; 1.
SMART; SM00015; IQ; 5.
SMART; SM00242; MYSc; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51126; DILUTE; 1.
PROSITE; PS50096; IQ; 5.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
PROSITE; PS51844; SH3_LIKE; 1.
1: Evidence at protein level;
Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
Coiled coil; Complete proteome; Cytoplasm; Motor protein; Myosin;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 1531 Myosin-17.
/FTId=PRO_0000422872.
DOMAIN 8 57 Myosin N-terminal SH3-like.
{ECO:0000255|PROSITE-ProRule:PRU01190}.
DOMAIN 62 732 Myosin motor. {ECO:0000255|PROSITE-
ProRule:PRU00782}.
DOMAIN 758 787 IQ 1. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 783 812 IQ 2. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 806 835 IQ 3. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 831 860 IQ 4. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 854 883 IQ 5. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1159 1470 Dilute. {ECO:0000255|PROSITE-
ProRule:PRU00503}.
NP_BIND 156 163 ATP. {ECO:0000255}.
NP_BIND 209 217 ATP. {ECO:0000255}.
REGION 495 529 Actin-binding. {ECO:0000255}.
REGION 531 554 Actin-binding. {ECO:0000255}.
REGION 589 613 Actin-binding. {ECO:0000255}.
REGION 613 635 Actin-binding. {ECO:0000250}.
COILED 884 1056 {ECO:0000255}.
MOD_RES 1517 1517 Phosphoserine.
{ECO:0000244|PubMed:19245862,
ECO:0000244|PubMed:19376835}.
CONFLICT 409 409 F -> V (in Ref. 2; AER51968).
{ECO:0000305}.
SEQUENCE 1531 AA; 173377 MW; D6C90682FB78AC5E CRC64;
MVGPVNIIVG SHVWIEDPGA AWIDGEVVKI NGEEVHAHTT NGKTVVANIA NVFPKDTEAP
PGGVDDMTKL SYLHEPGVLN NLAMRYELNE IYTYTGNILI AVNPFQRLPH LYDTHMMEQY
KGAGFGELSP HVFAIAEVAY RAMINEGKSN SILVSGESGA GKTETTKMLM RYLAYLGGRS
GVEGRTVEQQ VLESNPVLEA FGNAKTLRNN NSSRFGKFVE LQFDNCGRIS GAAVRTYLLE
RSRVCQISDP ERNYHCFYLL CAAPPEEREK FKLGDPKLFH YLNQSKCYKL DGVDDTEEYL
ATRRAMDIVG ISEEEQDAIF RVVAAILHLG NVNFAKGKEI DSSVLKDEKS RYHLDVCAEL
LRCDAKKMED ALIKRVMVTP EEVITRTLDP DSATGSRDAL AKTIYSRLFD WLVDKINNSI
GQDPNSKTII GVLDIYGFES FKINSFEQFC INFTNEKLQQ HFNQHVFKME QEDYTKEEIN
WSYIEFVDNK DVLELIEKKP GGVIALLDEA CMFPKSTHET FAQKLYQTFK NYKRFTKPKL
SRTSFAISHY AGEVTYQADL FLDKNKDYVV AEHQDLLIAS SDTFVAGLFP RLPEETSSKT
KFSSIGSRFK LQLQSLMETL SSTEPHYIRC VKPNNVLKPA IFENVNVIQQ LRCGGVLEAI
RISCAGYPTK RTFYEFLNRF GVLAPEVLEG NYDDKVACKM LLDKIGLKGY ELGKTKVFLR
AGQMAELDAR RAEVLGNAAR RIQRQSRTFI ACKEFRALRG AAIVLQSNCR GKLACNLYEE
MRRQAAAVKI QKIFRRHIAR ESYLRIRHST ITVQTALRGM VARNEFRFRK QMKAATIIQA
RLRSHLTHSY YKQLQKAALS TQCGWRSRVA RKELRTLKMA ARDTGALREA KDKLEKRVEE
LTWRLQLEKR QRTELEEAKT QEYAKQQEAL ETMRLQVEEA NAAVIREREA ARKAIEEAPP
VIKETPVLVE DTEKINSLTS EVEALKASLQ AERQAAENLR KAFSEAEARN SELATELENA
TRKADQLHES VQRLEEKLSN SESEIQVLRQ QALAISPTSR TMATRSKTML LPRTPENGNY
LNGGTKTTPD MTLAVREPES EEKPQKHLNE KQQENQDLLV KCISQNLGYN GDKPVAACVI
YKCLLHWRSF EVERTSVFDR IIQTIATAIE VPDNNEVLAY WLSNSATLLL LLQRTLKATG
AASLTPQRRR TTSASLFGRM SQGLRGSPQS AGLSFLNRQG LTKLDDLRQV EAKYPALLFK
QQLTAFLEKI YGMIRDNLKK EISPLLGLCI QAPRTSRASL VKGRAQANAV AQQALIAHWQ
SIRKSLNSYL NLMKANNAPP FLVRKVFTQI FSFINVQLFN SLLLRRECCS FSNGEYVKAG
LAELEQWCIE ATDEYAGSAW DELRHIRQAV GFLVIHQKPK KTLDEITREL CPVLSIQQLY
RISTMYWDDK YGTHSVSSDV IANMRVMMTE DSNNAVSSSF LLDDDSSIPF TVEDISKSMQ
QVDVNDIEPP QLIRENSGFG FLLTRKEGST S


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EIAAB26044 BBMI,BBM-I,Brush border myosin I,Homo sapiens,Human,MIHC,MYHL,MYO1A,Myosin I heavy chain,Myosin-Ia
E0755h ELISA kit Homo sapiens,Human,MYH2,MyHC-2a,MyHC-IIa,MYHSA2,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain IIa,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2 96T
U0755h CLIA Homo sapiens,Human,MYH2,MyHC-2a,MyHC-IIa,MYHSA2,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain IIa,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2 96T
E0755h ELISA Homo sapiens,Human,MYH2,MyHC-2a,MyHC-IIa,MYHSA2,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain IIa,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2 96T
E0161m ELISA kit Mouse,Mus musculus,Myh1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
E0161m ELISA Mouse,Mus musculus,Myh1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
E0755b ELISA Bos taurus,Bovine,MYH2,MyHC-2a,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2 96T
E0161b ELISA kit Bos taurus,Bovine,MYH1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
E0755b ELISA kit Bos taurus,Bovine,MYH2,MyHC-2a,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2 96T
E0161b ELISA Bos taurus,Bovine,MYH1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
U0161b CLIA Bos taurus,Bovine,MYH1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
EIAAB25976 MYH4,MyHC-2b,Myosin heavy chain 2b,Myosin heavy chain 4,Myosin heavy chain, skeletal muscle, juvenile,Myosin-4,Oryctolagus cuniculus,Rabbit
U0161m CLIA Mouse,Mus musculus,Myh1,MyHC-2x,Myosin heavy chain 1,Myosin heavy chain 2x,Myosin heavy chain, skeletal muscle, adult 1,Myosin-1 96T
U0755b CLIA Bos taurus,Bovine,MYH2,MyHC-2a,Myosin heavy chain 2,Myosin heavy chain 2a,Myosin heavy chain, skeletal muscle, adult 2,Myosin-2 96T
EIAAB26006 17 kDa myosin light chain,LC17,MLC-3,MYL6,Myosin light chain 3,Myosin light chain A3,Myosin light chain alkali 3,Myosin light polypeptide 6,Pig,Smooth muscle and nonmuscle myosin light chain alkali 6,
EIAAB25977 Homo sapiens,Human,MYH4,MyHC-2b,MyHC-IIb,Myosin heavy chain 2b,Myosin heavy chain 4,Myosin heavy chain IIb,Myosin heavy chain, skeletal muscle, fetal,Myosin-4
EIAAB26046 BBMI,BBM-I,Brush border myosin I,Chicken,Gallus gallus,MIHC,MYHL,MYO1A,Myosin I heavy chain,Myosin-Ia
EIAAB26043 BBMI,Bbmi,BBM-I,Brush border myosin I,MIHC,Myhl,Myo1a,Myosin I heavy chain,Myosin-Ia,Rat,Rattus norvegicus
EIAAB26045 BBMI,Bbmi,BBM-I,Brush border myosin I,MIHC,Mouse,Mus musculus,Myhl,Myo1a,Myosin I heavy chain,Myosin-Ia


 

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