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Anoctamin-5 (Gnathodiaphyseal dysplasia 1 protein) (Transmembrane protein 16E)

 ANO5_HUMAN              Reviewed;         913 AA.
Q75V66;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
20-JUN-2018, entry version 123.
RecName: Full=Anoctamin-5;
AltName: Full=Gnathodiaphyseal dysplasia 1 protein;
AltName: Full=Transmembrane protein 16E;
Name=ANO5; Synonyms=GDD1, TMEM16E;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
AND VARIANTS GDD GLY-356 AND ARG-356.
TISSUE=Skeletal muscle;
PubMed=15124103; DOI=10.1086/421527;
Tsutsumi S., Kamata N., Vokes T.J., Maruoka Y., Nakakuki K.,
Enomoto S., Omura K., Amagasa T., Nagayama M., Saito-Ohara F.,
Inazawa J., Moritani M., Yamaoka T., Inoue H., Itakura M.;
"The novel gene encoding a putative transmembrane protein is mutated
in gnathodiaphyseal dysplasia (GDD).";
Am. J. Hum. Genet. 74:1255-1261(2004).
[2]
TISSUE SPECIFICITY.
PubMed=15067359;
Katoh M., Katoh M.;
"Identification and characterization of TMEM16E and TMEM16F genes in
silico.";
Int. J. Oncol. 24:1345-1349(2004).
[3]
ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY, AND
SUBCELLULAR LOCATION.
PubMed=20056604; DOI=10.1074/jbc.M109.065367;
Schreiber R., Uliyakina I., Kongsuphol P., Warth R., Mirza M.,
Martins J.R., Kunzelmann K.;
"Expression and function of epithelial anoctamins.";
J. Biol. Chem. 285:7838-7845(2010).
[4]
REVIEW.
PubMed=21642943; DOI=10.1038/aps.2011.48;
Duran C., Hartzell H.C.;
"Physiological roles and diseases of Tmem16/Anoctamin proteins: are
they all chloride channels?";
Acta Pharmacol. Sin. 32:685-692(2011).
[5]
REVIEW.
PubMed=21607626; DOI=10.1007/s00424-011-0975-9;
Kunzelmann K., Tian Y., Martins J.R., Faria D., Kongsuphol P.,
Ousingsawat J., Thevenod F., Roussa E., Rock J., Schreiber R.;
"Anoctamins.";
Pflugers Arch. 462:195-208(2011).
[6]
ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY, AND
SUBCELLULAR LOCATION.
PubMed=22075693; DOI=10.1152/ajpcell.00140.2011;
Duran C., Qu Z., Osunkoya A.O., Cui Y., Hartzell H.C.;
"ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular
proteins.";
Am. J. Physiol. 302:C482-C493(2012).
[7]
REVIEW.
PubMed=22302790; DOI=10.1113/expphysiol.2011.058214;
Winpenny J.P., Gray M.A.;
"The anoctamin (TMEM16) gene family: calcium-activated chloride
channels come of age.";
Exp. Physiol. 97:175-176(2012).
[8]
SUBCELLULAR LOCATION.
PubMed=22946059; DOI=10.1242/jcs.109553;
Tian Y., Schreiber R., Kunzelmann K.;
"Anoctamins are a family of Ca2+ activated Cl- channels.";
J. Cell Sci. 125:4991-4998(2012).
[9]
VARIANT LGMD2L VAL-231, AND VARIANT MMD3 CYS-758.
PubMed=20096397; DOI=10.1016/j.ajhg.2009.12.013;
Bolduc V., Marlow G., Boycott K.M., Saleki K., Inoue H., Kroon J.,
Itakura M., Robitaille Y., Parent L., Baas F., Mizuta K., Kamata N.,
Richard I., Linssen W.H., Mahjneh I., de Visser M., Bashir R.,
Brais B.;
"Recessive mutations in the putative calcium-activated chloride
channel Anoctamin 5 cause proximal LGMD2L and distal MMD3 muscular
dystrophies.";
Am. J. Hum. Genet. 86:213-221(2010).
[10]
VARIANT LGMD2L TRP-58, AND VARIANT MMD3 CYS-655.
PubMed=22499103; DOI=10.1002/mus.23281;
Schessl J., Kress W., Schoser B.;
"Novel ANO5 mutations causing hyper-CK-emia, limb girdle muscular
weakness and Miyoshi type of muscular dystrophy.";
Muscle Nerve 45:740-742(2012).
[11]
VARIANT GDD ILE-513, AND FUNCTION.
PubMed=23047743; DOI=10.1038/ejhg.2012.224;
Marconi C., Brunamonti Binello P., Badiali G., Caci E., Cusano R.,
Garibaldi J., Pippucci T., Merlini A., Marchetti C., Rhoden K.J.,
Galietta L.J., Lalatta F., Balbi P., Seri M.;
"A novel missense mutation in ANO5/TMEM16E is causative for
gnathodiaphyseal dyplasia in a large Italian pedigree.";
Eur. J. Hum. Genet. 21:613-619(2013).
[12]
VARIANTS LGMD2L SER-52; SER-54; TRP-58; ILE-87; GLU-93; CYS-143;
LYS-202; ALA-206; VAL-231; ASN-259; SER-265; LEU-266; SER-267;
LEU-404; 405-GLN--LEU-913 DEL; 421-GLN--LEU-913 DEL; GLY-506;
547-ARG--LEU-913 DEL; GLN-547; ILE-555; SER-578; ILE-618; ASN-701 DEL;
SER-714; CYS-758; PRO-781; LEU-796; SER-804; VAL-830; LYS-833; ARG-839
AND LEU-900.
PubMed=25891276; DOI=10.1016/j.nmd.2015.03.011;
Savarese M., Di Fruscio G., Tasca G., Ruggiero L., Janssens S.,
De Bleecker J., Delpech M., Musumeci O., Toscano A., Angelini C.,
Sacconi S., Santoro L., Ricci E., Claes K., Politano L., Nigro V.;
"Next generation sequencing on patients with LGMD and nonspecific
myopathies: Findings associated with ANO5 mutations.";
Neuromuscul. Disord. 25:533-541(2015).
[13]
VARIANT LGMD2L TRP-58.
PubMed=25864073;
Bohlega S., Monies D.M., Abulaban A.A., Murad H.N., Alhindi H.N.,
Meyer B.F.;
"Clinical and genetic features of anoctaminopathy in Saudi Arabia.";
Neurosciences 20:173-177(2015).
[14]
VARIANT GDD TYR-356.
PubMed=27216912; DOI=10.1038/srep26440;
Andreeva T.V., Tyazhelova T.V., Rykalina V.N., Gusev F.E.,
Goltsov A.Y., Zolotareva O.I., Aliseichik M.P., Borodina T.A.,
Grigorenko A.P., Reshetov D.A., Ginter E.K., Amelina S.S.,
Zinchenko R.A., Rogaev E.I.;
"Whole exome sequencing links dental tumor to an autosomal-dominant
mutation in ANO5 gene associated with gnathodiaphyseal dysplasia and
muscle dystrophies.";
Sci. Rep. 6:26440-26440(2016).
-!- FUNCTION: Does not exhibit calcium-activated chloride channel
(CaCC) activity. {ECO:0000269|PubMed:20056604,
ECO:0000269|PubMed:23047743}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:15124103}; Multi-pass membrane protein
{ECO:0000255}. Cell membrane {ECO:0000269|PubMed:20056604,
ECO:0000269|PubMed:22946059}; Multi-pass membrane protein
{ECO:0000255}. Note=Colocalized with CALR/calreticulin
(PubMed:15124103). Shows an intracellular localization according
to PubMed:22075693. {ECO:0000269|PubMed:15124103,
ECO:0000269|PubMed:22075693}.
-!- TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney,
lung, and skeletal muscle. Weakly expressed in bone marrow, fetal
liver, placenta, spleen, thymus, osteoblasts and periodontal
ligament cells. {ECO:0000269|PubMed:15067359,
ECO:0000269|PubMed:15124103}.
-!- DISEASE: Gnathodiaphyseal dysplasia (GDD) [MIM:166260]: Rare
skeletal syndrome characterized by bone fragility, sclerosis of
tubular bones, and cemento-osseous lesions of the jawbone.
Patients experience frequent bone fractures caused by trivial
accidents in childhood; however the fractures heal normally
without bone deformity. The jaw lesions replace the tooth-bearing
segments of the maxilla and mandible with fibrous connective
tissues, including various amounts of cementum-like calcified
mass, sometimes causing facial deformities. Patients also have a
propensity for jaw infection and often suffer from purulent
osteomyelitis-like symptoms, such as swelling of and pus discharge
from the gums, mobility of the teeth, insufficient healing after
tooth extraction and exposure of the lesions into the oral cavity.
{ECO:0000269|PubMed:15124103, ECO:0000269|PubMed:23047743,
ECO:0000269|PubMed:27216912}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Limb-girdle muscular dystrophy 2L (LGMD2L) [MIM:611307]:
An autosomal recessive degenerative myopathy characterized by
proximal weakness, weakness of the hip and shoulder girdles and
prominent asymmetrical quadriceps femoris and biceps brachii
atrophy. {ECO:0000269|PubMed:20096397,
ECO:0000269|PubMed:22499103, ECO:0000269|PubMed:25864073,
ECO:0000269|PubMed:25891276}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Miyoshi muscular dystrophy 3 (MMD3) [MIM:613319]: A late-
onset muscular dystrophy characterized by distal muscle weakness
of the lower limbs, calf muscle discomfort and weakness,
quadriceps atrophy. Muscle weakness and atrophy may be asymmetric.
{ECO:0000269|PubMed:20096397, ECO:0000269|PubMed:22499103}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: The term 'anoctamin' was coined because these
channels are anion selective and have eight (OCT) transmembrane
segments. There is some dissatisfaction in the field with the Ano
nomenclature because it is not certain that all the members of
this family are anion channels or have the 8-transmembrane
topology.
-!- SIMILARITY: Belongs to the anoctamin family. {ECO:0000305}.
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EMBL; AB125267; BAD17859.1; -; mRNA.
CCDS; CCDS31444.1; -.
RefSeq; NP_001136121.1; NM_001142649.1.
RefSeq; NP_998764.1; NM_213599.2.
UniGene; Hs.154329; -.
ProteinModelPortal; Q75V66; -.
BioGrid; 128482; 2.
IntAct; Q75V66; 1.
STRING; 9606.ENSP00000315371; -.
TCDB; 1.A.17.1.21; the calcium-dependent chloride channel (ca-clc) family.
iPTMnet; Q75V66; -.
PhosphoSitePlus; Q75V66; -.
BioMuta; ANO5; -.
DMDM; 74749827; -.
PaxDb; Q75V66; -.
PeptideAtlas; Q75V66; -.
PRIDE; Q75V66; -.
ProteomicsDB; 68653; -.
DNASU; 203859; -.
Ensembl; ENST00000324559; ENSP00000315371; ENSG00000171714.
GeneID; 203859; -.
KEGG; hsa:203859; -.
UCSC; uc001mqi.3; human.
CTD; 203859; -.
DisGeNET; 203859; -.
EuPathDB; HostDB:ENSG00000171714.10; -.
GeneCards; ANO5; -.
GeneReviews; ANO5; -.
HGNC; HGNC:27337; ANO5.
HPA; HPA058857; -.
MalaCards; ANO5; -.
MIM; 166260; phenotype.
MIM; 608662; gene.
MIM; 611307; phenotype.
MIM; 613319; phenotype.
neXtProt; NX_Q75V66; -.
OpenTargets; ENSG00000171714; -.
Orphanet; 206549; Autosomal recessive limb-girdle muscular dystrophy type 2L.
Orphanet; 399096; Distal anoctaminopathy.
Orphanet; 53697; Gnathodiaphyseal dysplasia.
PharmGKB; PA164715641; -.
eggNOG; KOG2514; Eukaryota.
eggNOG; ENOG410XS4S; LUCA.
GeneTree; ENSGT00760000119015; -.
HOGENOM; HOG000006509; -.
HOVERGEN; HBG069519; -.
InParanoid; Q75V66; -.
KO; K19480; -.
OMA; MEIPRTH; -.
OrthoDB; EOG091G01JF; -.
PhylomeDB; Q75V66; -.
TreeFam; TF314265; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
ChiTaRS; ANO5; human.
GenomeRNAi; 203859; -.
PRO; PR:Q75V66; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000171714; -.
CleanEx; HS_ANO5; -.
Genevisible; Q75V66; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; IEA:Ensembl.
GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
InterPro; IPR032394; Anoct_dimer.
InterPro; IPR007632; Anoctamin.
InterPro; IPR031294; Anoctamin-5.
PANTHER; PTHR12308; PTHR12308; 1.
PANTHER; PTHR12308:SF23; PTHR12308:SF23; 1.
Pfam; PF16178; Anoct_dimer; 1.
Pfam; PF04547; Anoctamin; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disease mutation;
Endoplasmic reticulum; Glycoprotein; Limb-girdle muscular dystrophy;
Membrane; Osteogenesis imperfecta; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 913 Anoctamin-5.
/FTId=PRO_0000191755.
TOPO_DOM 1 299 Cytoplasmic. {ECO:0000255}.
TRANSMEM 300 320 Helical. {ECO:0000255}.
TOPO_DOM 321 380 Extracellular. {ECO:0000255}.
TRANSMEM 381 401 Helical. {ECO:0000255}.
TOPO_DOM 402 462 Cytoplasmic. {ECO:0000255}.
TRANSMEM 463 483 Helical. {ECO:0000255}.
TOPO_DOM 484 511 Extracellular. {ECO:0000255}.
TRANSMEM 512 532 Helical. {ECO:0000255}.
TOPO_DOM 533 557 Cytoplasmic. {ECO:0000255}.
TRANSMEM 558 578 Helical. {ECO:0000255}.
TOPO_DOM 579 679 Extracellular. {ECO:0000255}.
TRANSMEM 680 700 Helical. {ECO:0000255}.
TOPO_DOM 701 732 Cytoplasmic. {ECO:0000255}.
TRANSMEM 733 753 Helical. {ECO:0000255}.
TOPO_DOM 754 834 Extracellular. {ECO:0000255}.
TRANSMEM 835 855 Helical. {ECO:0000255}.
TOPO_DOM 856 913 Cytoplasmic. {ECO:0000255}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 380 380 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 768 768 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 778 778 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 791 791 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 52 52 N -> S (in LGMD2L; unknown pathological
significance; dbSNP:rs143777403).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080271.
VARIANT 54 54 F -> S (in LGMD2L; unknown pathological
significance; dbSNP:rs886043577).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080272.
VARIANT 58 58 R -> W (in LGMD2L; unknown pathological
significance; dbSNP:rs201725369).
{ECO:0000269|PubMed:22499103,
ECO:0000269|PubMed:25864073,
ECO:0000269|PubMed:25891276}.
/FTId=VAR_068247.
VARIANT 87 87 V -> I (in LGMD2L; unknown pathological
significance; dbSNP:rs34994927).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080273.
VARIANT 93 93 D -> E (in LGMD2L; unknown pathological
significance).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080274.
VARIANT 143 143 Y -> C (in LGMD2L; unknown pathological
significance).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080275.
VARIANT 202 202 E -> K (in LGMD2L; unknown pathological
significance; dbSNP:rs115750596).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080276.
VARIANT 206 206 T -> A (in LGMD2L; unknown pathological
significance; dbSNP:rs78266558).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080277.
VARIANT 231 231 G -> V (in LGMD2L; unknown pathological
significance; dbSNP:rs137854523).
{ECO:0000269|PubMed:20096397,
ECO:0000269|PubMed:25891276}.
/FTId=VAR_063582.
VARIANT 259 259 K -> N (in LGMD2L; unknown pathological
significance).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080278.
VARIANT 265 265 N -> S (in LGMD2L; unknown pathological
significance; dbSNP:rs377553546).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080279.
VARIANT 266 266 P -> L (in LGMD2L; unknown pathological
significance; dbSNP:rs745908606).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080280.
VARIANT 267 267 T -> S (in LGMD2L; unknown pathological
significance; dbSNP:rs138144479).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080281.
VARIANT 322 322 L -> F (in dbSNP:rs7481951).
/FTId=VAR_052339.
VARIANT 356 356 C -> G (in GDD; dbSNP:rs119103234).
{ECO:0000269|PubMed:15124103}.
/FTId=VAR_023524.
VARIANT 356 356 C -> R (in GDD; dbSNP:rs119103234).
{ECO:0000269|PubMed:15124103}.
/FTId=VAR_023525.
VARIANT 356 356 C -> Y (in GDD).
{ECO:0000269|PubMed:27216912}.
/FTId=VAR_076476.
VARIANT 404 404 R -> L (in LGMD2L; unknown pathological
significance).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080282.
VARIANT 405 913 Missing (in LGMD2L).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080301.
VARIANT 421 913 Missing (in LGMD2L).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080283.
VARIANT 506 506 S -> G (in LGMD2L; unknown pathological
significance; dbSNP:rs141799673).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080284.
VARIANT 513 513 T -> I (in GDD; unknown pathological
significance; dbSNP:rs281865467).
{ECO:0000269|PubMed:23047743}.
/FTId=VAR_076477.
VARIANT 547 913 Missing (in LGMD2L; unknown pathological
significance).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080285.
VARIANT 547 547 R -> Q (in LGMD2L; unknown pathological
significance; dbSNP:rs139618850).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080286.
VARIANT 555 555 S -> I (in LGMD2L; unknown pathological
significance; dbSNP:rs375014127).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080287.
VARIANT 578 578 F -> S (in LGMD2L; unknown pathological
significance; dbSNP:rs137854526).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080288.
VARIANT 618 618 M -> I (in LGMD2L; unknown pathological
significance).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080289.
VARIANT 655 655 W -> C (in MMD3; unknown pathological
significance; dbSNP:rs760137559).
{ECO:0000269|PubMed:22499103}.
/FTId=VAR_068248.
VARIANT 701 701 Missing (in LGMD2L; unknown pathological
significance).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080290.
VARIANT 714 714 T -> S (in LGMD2L; unknown pathological
significance; dbSNP:rs200631556).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080291.
VARIANT 758 758 R -> C (in MMD3 and LGMD2L; unknown
pathological significance;
dbSNP:rs137854529).
{ECO:0000269|PubMed:20096397,
ECO:0000269|PubMed:25891276}.
/FTId=VAR_063583.
VARIANT 781 781 L -> P (in LGMD2L; unknown pathological
significance).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080292.
VARIANT 796 796 S -> L (in LGMD2L; unknown pathological
significance; dbSNP:rs61910685).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080293.
VARIANT 804 804 C -> S (in LGMD2L; unknown pathological
significance).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080294.
VARIANT 830 830 A -> V (in LGMD2L; unknown pathological
significance; dbSNP:rs766853141).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080295.
VARIANT 833 833 M -> K (in LGMD2L; unknown pathological
significance; dbSNP:rs142073798).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080296.
VARIANT 839 839 M -> R (in LGMD2L; unknown pathological
significance).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080297.
VARIANT 882 882 N -> K (in dbSNP:rs34969327).
/FTId=VAR_052340.
VARIANT 900 900 M -> L (in LGMD2L; unknown pathological
significance; dbSNP:rs148293985).
{ECO:0000269|PubMed:25891276}.
/FTId=VAR_080298.
SEQUENCE 913 AA; 107188 MW; 98BC40318678C073 CRC64;
MGDPDLLEVL AEEGEKVNKH IDYSFQMSEQ SLSSRETSFL INEETMPAKR FNLFLRRRLM
FQKNQQSKDS IFFRDGIRQI DFVLSYVDDV KKDAELKAER RKEFETNLRK TGLELEIEDK
RDSEDGRTYF VKIHAPWEVL VTYAEVLGIK MPIKESDIPR PKHTPISYVL GPVRLPLSVK
YPHPEYFTAQ FSRHRQELFL IEDQATFFPS SSRNRIVYYI LSRCPFGIED GKKRFGIERL
LNSNTYSSAY PLHDGQYWKP SEPPNPTNER YTLHQNWARF SYFYKEQPLD LIKNYYGEKI
GIYFVFLGFY TEMLFFAAVV GLACFIYGLL SMEHNTSSTE ICDPEIGGQM IMCPLCDQVC
DYWRLNSTCL ASKFSHLFDN ESTVFFAIFM GIWVTLFLEF WKQRQARLEY EWDLVDFEEE
QQQLQLRPEF EAMCKHRKLN AVTKEMEPYM PLYTRIPWYF LSGATVTLWM SLVVTSMVAV
IVYRLSVFAT FASFMESDAS LKQVKSFLTP QITTSLTGSC LNFIVILILN FFYEKISAWI
TKMEIPRTYQ EYESSLTLKM FLFQFVNFYS SCFYVAFFKG KFVGYPGKYT YLFNEWRSEE
CDPGGCLIEL TTQLTIIMTG KQIFGNIKEA IYPLALNWWR RRKARTNSEK LYSRWEQDHD
LESFGPLGLF YEYLETVTQF GFVTLFVASF PLAPLLALIN NIVEIRVDAW KLTTQYRRTV
ASKAHSIGVW QDILYGMAVL SVATNAFIVA FTSDIIPRLV YYYAYSTNAT QPMTGYVNNS
LSVFLIADFP NHTAPSEKRD FITCRYRDYR YPPDDENKYF HNMQFWHVLA AKMTFIIVME
HVVFLVKFLL AWMIPDVPKD VVERIKREKL MTIKILHDFE LNKLKENLGI NSNEFAKHVM
IEENKAQLAK STL


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EIAAB43187 Homo sapiens,Human,Protein M83,TMEM6,TMEM8,TMEM8A,Transmembrane protein 6,Transmembrane protein 8,Transmembrane protein 8A
EIAAB43035 21 kDa transmembrane-trafficking protein,Integral membrane protein p23,Oryctolagus cuniculus,Rabbit,TMED10,TMP21,Transmembrane emp24 domain-containing protein 10,Transmembrane protein Tmp21
EIAAB42684 Mouse,Mus musculus,Tmem165,TPA-regulated locus protein,Tparl,Transmembrane protein 165,Transmembrane protein PFT27,Transmembrane protein TPARL
EIAAB43033 21 kDa transmembrane-trafficking protein,Homo sapiens,Human,p23,p24delta,S31I125,S31III125,TMED10,TMP21,Tmp-21-I,Transmembrane emp24 domain-containing protein 10,Transmembrane protein Tmp21
EIAAB40998 HBE120,Homo sapiens,Human,KIAA1944,Mature OL transmembrane protein,Mature oligodendrocytes transmembrane protein,MOLT,TMEM132D,Transmembrane protein 132D
EIAAB42959 Beethoven protein,Bth,Deafness protein,dn,Mouse,Mus musculus,Tmc1,Transmembrane channel-like protein 1,Transmembrane cochlear-expressed protein 1
EIAAB41071 Homo sapiens,Human,TMEM200B,Transmembrane protein 200B,Transmembrane protein TTMA,TTMB,Two transmembrane domain-containing family member B
EIAAB41000 Mature OL transmembrane protein,Mature oligodendrocytes transmembrane protein,Molt,Mouse,Mus musculus,Tmem132d,Transmembrane protein 132D
EIAAB43034 21 kDa transmembrane-trafficking protein,Rat,Rattus norvegicus,Tmed10,Tmp21,Transmembrane emp24 domain-containing protein 10,Transmembrane protein Tmp21
EIAAB43032 21 kDa transmembrane-trafficking protein,Bos taurus,Bovine,TMED10,TMP21,Transmembrane emp24 domain-containing protein 10,Transmembrane protein Tmp21
EIAAB40999 Mature OL transmembrane protein,Mature oligodendrocytes transmembrane protein,Molt,Rat,Rattus norvegicus,Tmem132d,Transmembrane protein 132D
EIAAB43036 21 kDa transmembrane-trafficking protein,Mouse,Mus musculus,Tmed10,Tmp21,Transmembrane emp24 domain-containing protein 10,Transmembrane protein Tmp21
EIAAB42685 Homo sapiens,Human,TMEM165,TPARL,Transmembrane protein 165,Transmembrane protein PT27,Transmembrane protein TPARL
EIAAB12407 Ectodermal dysplasia protein,Ectodysplasin-A,ED1,EDA,EDA protein,EDA2,Homo sapiens,Human
EIAAB41072 Homo sapiens,Human,TMEM200C,Transmembrane protein 200C,Transmembrane protein TTMA,TTMA,Two transmembrane domain-containing family member A
EIAAB43188 M83 protein,Mouse,Mus musculus,Tmem8,Tmem8a,Transmembrane protein 8,Transmembrane protein 8A
EIAAB41003 Fasting-inducible integral membrane protein TM6P1,Rat,Rattus norvegicus,Tm6p1,Tmem150,Tmem150a,Transmembrane protein 150,Transmembrane protein 150A
EIAAB42834 Homo sapiens,Human,IFITMD2,Interferon-induced transmembrane domain-containing protein D2,TMEM233,Transmembrane protein 233
EIAAB42960 C20orf145,Homo sapiens,Human,TMC2,Transmembrane channel-like protein 2,Transmembrane cochlear-expressed protein 2,UNQ907_PRO1928
EIAAB42958 Homo sapiens,Human,TMC1,Transmembrane channel-like protein 1,Transmembrane cochlear-expressed protein 1
EIAAB41017 C6orf137,Homo sapiens,Human,TMEM151B,TMEM193,Transmembrane protein 151B,Transmembrane protein 193
EIAAB41035 C14orf90,Homo sapiens,Human,TMEM179,TMEM179A,Transmembrane protein 179,Transmembrane protein 179A
EIAAB41048 Homo sapiens,Human,PRO1355,TMEM184C,TMEM34,Transmembrane protein 184C,Transmembrane protein 34
EIAAB40979 Mouse,Mus musculus,Tmem120a,Tmpit,Transmembrane protein 120A,Transmembrane protein induced by tumor necrosis factor alpha
EIAAB40978 Rat,Rattus norvegicus,Tmem120a,Tmpit,Transmembrane protein 120A,Transmembrane protein induced by tumor necrosis factor alpha


 

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