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Cobalt/magnesium transport protein CorA

 CORA_THEMA              Reviewed;         351 AA.
Q9WZ31;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 119.
RecName: Full=Cobalt/magnesium transport protein CorA {ECO:0000305};
Name=corA; OrderedLocusNames=TM_0561;
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099).
Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
NCBI_TaxID=243274;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
PubMed=10360571; DOI=10.1038/20601;
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
"Evidence for lateral gene transfer between Archaea and Bacteria from
genome sequence of Thermotoga maritima.";
Nature 399:323-329(1999).
[2]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF ASP-89; ASP-253; LEU-280; MET-291; LEU-294; PRO-303; GLY-312;
MET-313 AND ASN-314.
PubMed=18276588; DOI=10.1074/jbc.M707889200;
Payandeh J., Li C., Ramjeesingh M., Poduch E., Bear C.E., Pai E.F.;
"Probing structure-function relationships and gating mechanisms in the
CorA Mg2+ transport system.";
J. Biol. Chem. 283:11721-11733(2008).
[3]
FUNCTION IN COBALT TRANSPORT, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=21454699; DOI=10.1074/jbc.M111.222166;
Xia Y., Lundbaeck A.K., Sahaf N., Nordlund G., Brzezinski P.,
Eshaghi S.;
"Co2+ selectivity of Thermotoga maritima CorA and its inability to
regulate Mg2+ homeostasis present a new class of CorA proteins.";
J. Biol. Chem. 286:16525-16532(2011).
[4]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF ILE-310;
TYR-311; GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND
TYR-327.
PubMed=22722933; DOI=10.1074/jbc.M112.371484;
Palombo I., Daley D.O., Rapp M.;
"The periplasmic loop provides stability to the open state of the CorA
magnesium channel.";
J. Biol. Chem. 287:27547-27555(2012).
[5]
FUNCTION, MUTAGENESIS OF ASN-288, AND SUBCELLULAR LOCATION.
PubMed=23091000; DOI=10.1073/pnas.1210076109;
Guskov A., Nordin N., Reynaud A., Engman H., Lundback A.K., Jong A.J.,
Cornvik T., Phua T., Eshaghi S.;
"Structural insights into the mechanisms of Mg2+ uptake, transport,
and gating by CorA.";
Proc. Natl. Acad. Sci. U.S.A. 109:18459-18464(2012).
[6]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF TYR-311;
GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327.
PubMed=23781956; DOI=10.1021/bi4007397;
Palombo I., Daley D.O., Rapp M.;
"Why is the GMN motif conserved in the CorA/Mrs2/Alr1 superfamily of
magnesium transport proteins?";
Biochemistry 52:4842-4847(2013).
[7] {ECO:0000244|PDB:2HN2}
X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION,
TOPOLOGY, MOTIF, DOMAIN, AND MUTAGENESIS OF ASP-253.
PubMed=16902408; DOI=10.1038/sj.emboj.7601269;
Payandeh J., Pai E.F.;
"A structural basis for Mg2+ homeostasis and the CorA translocation
cycle.";
EMBO J. 25:3762-3773(2006).
[8]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT,
TOPOLOGY, DOMAIN, AND MOTIF.
PubMed=16598263; DOI=10.1038/nature04642;
Lunin V.V., Dobrovetsky E., Khutoreskaya G., Zhang R., Joachimiak A.,
Doyle D.A., Bochkarev A., Maguire M.E., Edwards A.M., Koth C.M.;
"Crystal structure of the CorA Mg2+ transporter.";
Nature 440:833-837(2006).
[9]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT,
TOPOLOGY, DOMAIN, AND MOTIF.
PubMed=16857941; DOI=10.1126/science.1127121;
Eshaghi S., Niegowski D., Kohl A., Molina D.M., Lesley S.A.,
Nordlund P.;
"Crystal structure of a divalent metal ion transporter CorA at 2.9
Angstrom resolution.";
Science 313:354-357(2006).
[10] {ECO:0000244|PDB:4EEB, ECO:0000244|PDB:4EED}
X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN
COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
TOPOLOGY, AND DOMAIN.
PubMed=23112165; DOI=10.1073/pnas.1209018109;
Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.;
"Structural asymmetry in the magnesium channel CorA points to
sequential allosteric regulation.";
Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012).
[11] {ECO:0000244|PDB:4I0U}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, TOPOLOGY, DOMAIN, AND MUTAGENESIS OF ASP-89; ASN-288;
THR-295; THR-299 AND THR-305.
PubMed=23425532; DOI=10.1042/BJ20121745;
Nordin N., Guskov A., Phua T., Sahaf N., Xia Y., Lu S., Eshaghi H.,
Eshaghi S.;
"Exploring the structure and function of Thermotoga maritima CorA
reveals the mechanism of gating and ion selectivity in Co2+/Mg2+
transport.";
Biochem. J. 451:365-374(2013).
[12]
STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF APOPROTEIN AND IN
COMPLEX WITH MAGNESIUM, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
DOMAIN.
PubMed=26871634; DOI=10.1016/j.cell.2015.12.055;
Matthies D., Dalmas O., Borgnia M.J., Dominik P.K., Merk A., Rao P.,
Reddy B.G., Islam S., Bartesaghi A., Perozo E., Subramaniam S.;
"Cryo-EM Structures of the magnesium channel CorA reveal symmetry
break upon gating.";
Cell 164:747-756(2016).
-!- FUNCTION: Mediates influx of magnesium ions (PubMed:18276588,
PubMed:22722933, PubMed:23781956, PubMed:23112165). Mediates
Co(2+) uptake (PubMed:21454699, PubMed:23091000, PubMed:23425532).
Has high selectivity for Co(2+) (PubMed:21454699,
PubMed:23425532). Alternates between open and closed states.
Activated by low cytoplasmic Mg(2+) levels. Inactive when
cytoplasmic Mg(2+) levels are high (PubMed:23112165,
PubMed:23425532, PubMed:26871634). {ECO:0000269|PubMed:18276588,
ECO:0000269|PubMed:21454699, ECO:0000269|PubMed:22722933,
ECO:0000269|PubMed:23091000, ECO:0000269|PubMed:23112165,
ECO:0000269|PubMed:23425532, ECO:0000269|PubMed:23781956,
ECO:0000305|PubMed:26871634}.
-!- ACTIVITY REGULATION: Inhibited by cobalt hexaammine.
{ECO:0000269|PubMed:18276588}.
-!- SUBUNIT: Homopentamer (PubMed:22722933, PubMed:23781956,
PubMed:16902408, PubMed:16598263, PubMed:16857941,
PubMed:23112165, PubMed:23425532, PubMed:26871634). In the absence
of Mg(2+), interactions between subunits are weakened, and dimers,
trimers and tetramers can be observed in vitro (PubMed:22722933,
PubMed:26871634). {ECO:0000269|PubMed:16598263,
ECO:0000269|PubMed:16857941, ECO:0000269|PubMed:16902408,
ECO:0000269|PubMed:22722933, ECO:0000269|PubMed:23112165,
ECO:0000269|PubMed:23425532, ECO:0000269|PubMed:23781956,
ECO:0000269|PubMed:26871634}.
-!- INTERACTION:
Self; NbExp=19; IntAct=EBI-15578365, EBI-15578365;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:23112165, ECO:0000305|PubMed:16598263,
ECO:0000305|PubMed:16857941, ECO:0000305|PubMed:16902408,
ECO:0000305|PubMed:18276588, ECO:0000305|PubMed:21454699,
ECO:0000305|PubMed:22722933, ECO:0000305|PubMed:23091000,
ECO:0000305|PubMed:23425532, ECO:0000305|PubMed:23781956,
ECO:0000305|PubMed:26871634}; Multi-pass membrane protein
{ECO:0000269|PubMed:16598263, ECO:0000269|PubMed:16857941,
ECO:0000269|PubMed:16902408, ECO:0000269|PubMed:23112165,
ECO:0000269|PubMed:23425532, ECO:0000269|PubMed:26871634,
ECO:0000305|PubMed:23091000}.
-!- DOMAIN: The central ion permeation pathway is formed by the first
transmembrane domain from each of the five subunits. Mg(2+)
binding strengthens interactions between subunits and leads to the
formation of a symmetrical homopentamer surrounding a closed ion
permeation pathway (PubMed:23091000, PubMed:16902408,
PubMed:16598263, PubMed:16857941, PubMed:23112165,
PubMed:23425532, PubMed:26871634). Co(2+) binding also induces a
conformation change (PubMed:21454699). Low Mg(2+) concentrations
trigger both a conformation change within each subunit and a
loosening of the interactions between subunits. This results in an
open ion conduction pathway. In addition, this results in a less
symmetrical shape of the whole complex (PubMed:23112165,
PubMed:26871634). {ECO:0000269|PubMed:16598263,
ECO:0000269|PubMed:16857941, ECO:0000269|PubMed:16902408,
ECO:0000269|PubMed:21454699, ECO:0000269|PubMed:23112165,
ECO:0000269|PubMed:23425532, ECO:0000269|PubMed:26871634,
ECO:0000305|PubMed:23091000}.
-!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC
1.A.35) family. {ECO:0000305}.
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EMBL; AE000512; AAD35646.1; -; Genomic_DNA.
PIR; H72360; H72360.
RefSeq; NP_228371.1; NC_000853.1.
RefSeq; WP_004081315.1; NZ_CP011107.1.
PDB; 2BBH; X-ray; 1.85 A; A=1-266.
PDB; 2BBJ; X-ray; 3.90 A; A/B/D/E/F=1-351.
PDB; 2HN2; X-ray; 3.70 A; A/B/C/D/E=1-351.
PDB; 2IUB; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=1-351.
PDB; 3JCF; X-ray; 3.80 A; A/B/C/D/E=1-351.
PDB; 3JCG; X-ray; 7.06 A; A/B/C/D/E=1-351.
PDB; 3JCH; X-ray; 7.06 A; A/B/C/D/E=1-351.
PDB; 4EEB; X-ray; 3.80 A; A/B/C/D/E=26-351.
PDB; 4EED; X-ray; 3.92 A; A/B/C/D/E=26-351.
PDB; 4I0U; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=1-351.
PDB; 5JRW; X-ray; 3.30 A; A/B/C/D/E=2-351.
PDB; 5JTG; X-ray; 3.05 A; A/B/C/D/E=2-351.
PDBsum; 2BBH; -.
PDBsum; 2BBJ; -.
PDBsum; 2HN2; -.
PDBsum; 2IUB; -.
PDBsum; 3JCF; -.
PDBsum; 3JCG; -.
PDBsum; 3JCH; -.
PDBsum; 4EEB; -.
PDBsum; 4EED; -.
PDBsum; 4I0U; -.
PDBsum; 5JRW; -.
PDBsum; 5JTG; -.
ProteinModelPortal; Q9WZ31; -.
SMR; Q9WZ31; -.
DIP; DIP-59006N; -.
STRING; 243274.TM0561; -.
TCDB; 1.A.35.3.2; the cora metal ion transporter (mit) family.
EnsemblBacteria; AAD35646; AAD35646; TM_0561.
GeneID; 897621; -.
KEGG; tma:TM0561; -.
eggNOG; ENOG4105D7N; Bacteria.
eggNOG; COG0598; LUCA.
InParanoid; Q9WZ31; -.
KO; K03284; -.
OMA; FRDIYDH; -.
BRENDA; 3.6.3.2; 6331.
EvolutionaryTrace; Q9WZ31; -.
Proteomes; UP000008183; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0006824; P:cobalt ion transport; IMP:UniProtKB.
GO; GO:1903830; P:magnesium ion transmembrane transport; IMP:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
InterPro; IPR004488; Mg/Co-transport_prot_CorA.
InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
Pfam; PF01544; CorA; 1.
TIGRFAMs; TIGR00383; corA; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Cobalt; Coiled coil;
Complete proteome; Ion transport; Magnesium; Membrane; Metal-binding;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 351 Cobalt/magnesium transport protein CorA.
/FTId=PRO_0000239049.
TOPO_DOM 1 292 Cytoplasmic. {ECO:0000305}.
TRANSMEM 293 313 Helical. {ECO:0000269|PubMed:16598263,
ECO:0000269|PubMed:16857941,
ECO:0000269|PubMed:16902408,
ECO:0000269|PubMed:23112165,
ECO:0000269|PubMed:23425532,
ECO:0000269|PubMed:26871634}.
TOPO_DOM 314 324 Extracellular. {ECO:0000305}.
TRANSMEM 325 345 Helical. {ECO:0000269|PubMed:16598263,
ECO:0000269|PubMed:16857941,
ECO:0000269|PubMed:16902408,
ECO:0000269|PubMed:23112165,
ECO:0000269|PubMed:23425532,
ECO:0000269|PubMed:26871634}.
TOPO_DOM 346 351 Cytoplasmic. {ECO:0000305}.
COILED 178 225 {ECO:0000255}.
MOTIF 312 314 Probable selectivity filter.
{ECO:0000305|PubMed:16598263,
ECO:0000305|PubMed:16857941,
ECO:0000305|PubMed:16902408,
ECO:0000305|PubMed:23781956}.
COMPBIAS 346 349 Poly-Lys.
SITE 288 288 Essential for ion permeation.
{ECO:0000269|PubMed:23091000}.
SITE 294 294 Important for closing the ion permeation
pathway in the closed state.
{ECO:0000269|PubMed:16598263,
ECO:0000269|PubMed:16857941,
ECO:0000269|PubMed:16902408,
ECO:0000269|PubMed:18276588}.
SITE 295 295 Threonine that confers selectivity for
Co(2+) transport.
{ECO:0000269|PubMed:23425532}.
MUTAGEN 89 89 D->F,K: Decreases ion transport.
{ECO:0000269|PubMed:18276588,
ECO:0000269|PubMed:23425532}.
MUTAGEN 253 253 D->K: Increases protein stability.
Decreases ion transport.
{ECO:0000269|PubMed:16902408,
ECO:0000269|PubMed:18276588}.
MUTAGEN 280 280 L->A: Decreases ion transport.
{ECO:0000269|PubMed:18276588}.
MUTAGEN 288 288 N->L: Abolishes Co(2+) uptake.
{ECO:0000269|PubMed:23091000,
ECO:0000269|PubMed:23425532}.
MUTAGEN 291 291 M->A: No effect on ion transport.
{ECO:0000269|PubMed:18276588}.
MUTAGEN 294 294 L->A,V: Increases ion transport by
suppression of an obstruction in the
transmembrane ion permeation pathway.
{ECO:0000269|PubMed:18276588}.
MUTAGEN 295 295 T->L: Strongly reduces Co(2+) uptake.
Abolishes Co(2+) uptake; when associated
with L-299.
{ECO:0000269|PubMed:23425532}.
MUTAGEN 295 295 T->M: Strongly reduces Co(2+) uptake.
{ECO:0000269|PubMed:23425532}.
MUTAGEN 295 295 T->S: No significant decrease of Co(2+)
uptake, but abolishes selectivity for
Co(2+). {ECO:0000269|PubMed:23425532}.
MUTAGEN 299 299 T->L: Reduces Co(2+) uptake. Abolishes
Co(2+) uptake; when associated with L-
295. {ECO:0000269|PubMed:23425532}.
MUTAGEN 299 299 T->M: No effect on Co(2+) uptake.
{ECO:0000269|PubMed:23425532}.
MUTAGEN 299 299 T->S: Abolishes Co(2+) uptake.
{ECO:0000269|PubMed:23425532}.
MUTAGEN 303 303 P->A,G,I: Increases ion transport by
suppression of a kink in the
transmembrane ion permeation pathway.
{ECO:0000269|PubMed:18276588}.
MUTAGEN 305 305 T->L: Abolishes Co(2+) uptake.
{ECO:0000269|PubMed:23425532}.
MUTAGEN 310 310 I->A: Increases ion transport.
{ECO:0000269|PubMed:22722933}.
MUTAGEN 311 311 Y->A: Abolishes pentamerization.
Abolishes ion transport.
{ECO:0000269|PubMed:22722933,
ECO:0000269|PubMed:23781956}.
MUTAGEN 311 311 Y->F: No effect on pentamerization. No
effect on ion transport.
{ECO:0000269|PubMed:23781956}.
MUTAGEN 312 312 G->A: No effect on pentamerization.
Abolishes ion transport.
{ECO:0000269|PubMed:18276588,
ECO:0000269|PubMed:22722933}.
MUTAGEN 312 312 G->F: No effect on pentamerization.
Abolishes ion transport.
{ECO:0000269|PubMed:23781956}.
MUTAGEN 313 313 M->A: Abolishes pentamerization.
Abolishes ion transport.
{ECO:0000269|PubMed:18276588,
ECO:0000269|PubMed:22722933}.
MUTAGEN 313 313 M->C,I,L,V: Abolishes pentamerization.
Abolishes ion transport.
{ECO:0000269|PubMed:23781956}.
MUTAGEN 314 314 N->A: Abolishes pentamerization.
Abolishes ion transport.
{ECO:0000269|PubMed:18276588}.
MUTAGEN 314 314 N->D,E,T: Abolishes pentamerization.
Abolishes ion transport.
{ECO:0000269|PubMed:23781956}.
MUTAGEN 314 314 N->Q: No effect on pentamerization.
Abolishes ion transport.
{ECO:0000269|PubMed:23781956}.
MUTAGEN 315 315 F->A: Abolishes pentamerization.
Abolishes ion transport.
{ECO:0000269|PubMed:22722933,
ECO:0000269|PubMed:23781956}.
MUTAGEN 315 315 F->W: No effect on pentamerization.
Increases ion transport.
{ECO:0000269|PubMed:23781956}.
MUTAGEN 318 318 M->A: Impairs pentamerization. Decreases
ion transport.
{ECO:0000269|PubMed:22722933}.
MUTAGEN 318 318 M->I,L,V: No effect on pentamerization.
Decreases ion transport.
{ECO:0000269|PubMed:23781956}.
MUTAGEN 321 321 L->A: Impairs pentamerization. Decreases
ion transport.
{ECO:0000269|PubMed:22722933}.
MUTAGEN 321 321 L->I: No effect on pentamerization.
Decreases ion transport.
{ECO:0000269|PubMed:23781956}.
MUTAGEN 321 321 L->V: No effect on pentamerization. No
effect on ion transport.
{ECO:0000269|PubMed:23781956}.
MUTAGEN 327 327 Y->A: Abolishes pentamerization. Strongly
decreases ion transport.
{ECO:0000269|PubMed:22722933,
ECO:0000269|PubMed:23781956}.
MUTAGEN 327 327 Y->F: No effect on pentamerization.
Increases ion transport.
{ECO:0000269|PubMed:23781956}.
MUTAGEN 327 327 Y->W: Abolishes pentamerization. Mildly
decreases ion transport.
{ECO:0000269|PubMed:23781956}.
STRAND 5 7 {ECO:0000244|PDB:4I0U}.
STRAND 28 35 {ECO:0000244|PDB:2BBH}.
STRAND 38 45 {ECO:0000244|PDB:2BBH}.
HELIX 47 49 {ECO:0000244|PDB:2BBH}.
HELIX 51 55 {ECO:0000244|PDB:2BBH}.
STRAND 60 65 {ECO:0000244|PDB:2BBH}.
HELIX 70 80 {ECO:0000244|PDB:2BBH}.
HELIX 84 91 {ECO:0000244|PDB:2BBH}.
STRAND 98 101 {ECO:0000244|PDB:2BBH}.
STRAND 103 114 {ECO:0000244|PDB:2BBH}.
TURN 117 120 {ECO:0000244|PDB:4I0U}.
STRAND 123 132 {ECO:0000244|PDB:2BBH}.
STRAND 135 143 {ECO:0000244|PDB:2BBH}.
HELIX 148 155 {ECO:0000244|PDB:2BBH}.
HELIX 161 163 {ECO:0000244|PDB:2BBH}.
HELIX 166 197 {ECO:0000244|PDB:2BBH}.
HELIX 208 242 {ECO:0000244|PDB:2BBH}.
HELIX 244 272 {ECO:0000244|PDB:4I0U}.
HELIX 275 310 {ECO:0000244|PDB:4I0U}.
STRAND 311 313 {ECO:0000244|PDB:4I0U}.
HELIX 319 322 {ECO:0000244|PDB:4I0U}.
HELIX 326 344 {ECO:0000244|PDB:4I0U}.
TURN 345 348 {ECO:0000244|PDB:4I0U}.
SEQUENCE 351 AA; 41446 MW; 6A845EC612A4A0BA CRC64;
MEEKRLSAKK GLPPGTLVYT GKYREDFEIE VMNYSIEEFR EFKTTDVESV LPFRDSSTPT
WINITGIHRT DVVQRVGEFF GIHPLVLEDI LNVHQRPKVE FFENYVFIVL KMFTYDKNLH
ELESEQVSLI LTKNCVLMFQ EKIGDVFDPV RERIRYNRGI IRKKRADYLL YSLIDALVDD
YFVLLEKIDD EIDVLEEEVL ERPEKETVQR THQLKRNLVE LRKTIWPLRE VLSSLYRDVP
PLIEKETVPY FRDVYDHTIQ IADTVETFRD IVSGLLDVYL SSVSNKTNEV MKVLTIIATI
FMPLTFIAGI YGMNFEYMPE LRWKWGYPVV LAVMGVIAVI MVVYFKKKKW L


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EIAAB36853 Acsvl3,Fatp3,FATP-3,Fatty acid transport protein 3,Long-chain fatty acid transport protein 3,Mouse,Mus musculus,Slc27a3,Solute carrier family 27 member 3
EIAAB36847 ACSVL5,FATP1,FATP-1,Fatty acid transport protein 1,Homo sapiens,Human,Long-chain fatty acid transport protein 1,SLC27A1,Solute carrier family 27 member 1
EIAAB36856 ACSVL4,FATP4,FATP-4,Fatty acid transport protein 4,Homo sapiens,Human,Long-chain fatty acid transport protein 4,SLC27A4,Solute carrier family 27 member 4
EIAAB38646 B(0,+)-type amino acid transport protein,D2,NAA-TR,Nbat,Neutral and basic amino acid transport protein rBAT,Rat,Rattus norvegicus,Slc3a1
C23710 Cobalt naphthenate (in mineral spirits) 6 percent cobalt content 500 G
C23710 Cobalt naphthenate (in mineral spirits) 6 percent cobalt content
C23740 Cobalt octoate (in Mineral Spirits) 6 percent Cobalt Content 100 G
C23710 Cobalt naphthenate (in mineral spirits) 6 percent cobalt content 100 G
C23710 Cobalt naphthenate (in mineral spirits) 6 percent cobalt content 1000 G
C23740 Cobalt octoate (in Mineral Spirits) 6 percent Cobalt Content 25 G
C23740 Cobalt octoate (in Mineral Spirits) 6 percent Cobalt Content
C23710 Cobalt naphthenate (in mineral spirits) 6 percent cobalt content
C23710 Cobalt naphthenate (in mineral spirits) 6 percent cobalt content
C23740 Cobalt octoate (in Mineral Spirits) 6 percent Cobalt Content
38582-17-1 Cobalt(II) cyclohexanebutyrate min. 14 percent Cobalt(II) cyclohexaneb 1g
C-02912 COBALT NAPHTHENATE (6 percent COBALT ) CAS: 61789-51-3 500 gm
123334-29-2 Cobalt(II) acetylacetonate hydrate Cobalt(II) acetylacetona 1g
09216-75 Cobalt(Ⅱ) 2‐Ethylhexanoate 〔Cobalt(Ⅱ) Octylate〕 CAS: 13586-82-8 500G
94333-37-6 cobalt 1,2,3,6_tetrahydro_2,6_dioxopyrimi cobalt 1,2,3,6_tetrahydr 1g
14666-96-7 cobalt (9Z,12Z)_octadeca_9,12_dienoate cobalt (9Z,12Z)_octade 1g


 

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