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Coxsackievirus and adenovirus receptor homolog (CAR) (mCAR)

 CXAR_MOUSE              Reviewed;         365 AA.
P97792; O09052; Q3ULD0; Q91W66; Q99KG0; Q9DBJ8;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
27-SEP-2017, entry version 161.
RecName: Full=Coxsackievirus and adenovirus receptor homolog;
Short=CAR;
Short=mCAR;
Flags: Precursor;
Name=Cxadr; Synonyms=Car;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
STRAIN=C3H/Mai;
PubMed=9096397; DOI=10.1073/pnas.94.7.3352;
Tomko R.P., Xu R., Philipson L.;
"HCAR and MCAR: the human and mouse cellular receptors for subgroup C
adenoviruses and group B coxsackieviruses.";
Proc. Natl. Acad. Sci. U.S.A. 94:3352-3356(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A VIRUS
RECEPTOR.
STRAIN=C57BL/6J; TISSUE=Colon, and Liver;
PubMed=9036860; DOI=10.1126/science.275.5304.1320;
Bergelson J.M., Cunningham J.A., Droguett G., Kurt-Jones E.,
Krithivas A., Hong J.S., Horwitz M.S., Crowell R.L., Finberg R.W.;
"Isolation of a common receptor for Coxsackie B viruses and
adenoviruses 2 and 5.";
Science 275:1320-1323(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION AS A VIRUS
RECEPTOR.
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=9420240;
Bergelson J.M., Krithivas A., Celi L., Droguett G., Horwitz M.S.,
Wickham T., Crowell R.L., Finberg R.W.;
"The murine CAR homolog is a receptor for coxsackie B viruses and
adenoviruses.";
J. Virol. 72:415-419(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION, AND FUNCTION.
PubMed=10814828; DOI=10.1016/S0169-328X(00)00036-X;
Honda T., Saitoh H., Masuko M., Katagiri-Abe T., Tominaga K.,
Kozakai I., Kobayashi K., Kumanishi T., Watanabe Y.G., Odani S.,
Kuwano R.;
"The coxsackievirus-adenovirus receptor protein as a cell adhesion
molecule in the developing mouse brain.";
Brain Res. Mol. Brain Res. 77:19-28(2000).
[7]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=12763576; DOI=10.1016/S0165-3806(03)00035-X;
Hotta Y., Honda T., Naito M., Kuwano R.;
"Developmental distribution of coxsackie virus and adenovirus receptor
localized in the nervous system.";
Brain Res. Dev. Brain Res. 143:1-13(2003).
[8]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15533241; DOI=10.1186/1471-2121-5-42;
Shaw C.A., Holland P.C., Sinnreich M., Allen C., Sollerbrant K.,
Karpati G., Nalbantoglu J.;
"Isoform-specific expression of the Coxsackie and adenovirus receptor
(CAR) in neuromuscular junction and cardiac intercalated discs.";
BMC Cell Biol. 5:42-42(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-304; SER-306;
SER-323 AND SER-363, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
Pancreas;
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).
[11]
FUNCTION IN T-CELL ACTIVATION, AND INTERACTION WITH CXADR.
PubMed=20813954; DOI=10.1126/science.1192698;
Witherden D.A., Verdino P., Rieder S.E., Garijo O., Mills R.E.,
Teyton L., Fischer W.H., Wilson I.A., Havran W.L.;
"The junctional adhesion molecule JAML is a costimulatory receptor for
epithelial gammadelta T cell activation.";
Science 329:1205-1210(2010).
[12]
X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 20-233, AND DISULFIDE BONDS.
PubMed=20181587; DOI=10.1523/JNEUROSCI.5725-09.2010;
Patzke C., Max K.E., Behlke J., Schreiber J., Schmidt H., Dorner A.A.,
Kroger S., Henning M., Otto A., Heinemann U., Rathjen F.G.;
"The coxsackievirus-adenovirus receptor reveals complex homophilic and
heterophilic interactions on neural cells.";
J. Neurosci. 30:2897-2910(2010).
[13]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-236 IN COMPLEX WITH JAML,
DOMAIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-106.
PubMed=20813955; DOI=10.1126/science.1187996;
Verdino P., Witherden D.A., Havran W.L., Wilson I.A.;
"The molecular interaction of CAR and JAML recruits the central cell
signal transducer PI3K.";
Science 329:1210-1214(2010).
-!- FUNCTION: Component of the epithelial apical junction complex that
may function as a homophilic cell adhesion molecule and is
essential for tight junction integrity. Also involved in
transepithelial migration of leukocytes through adhesive
interactions with JAML a transmembrane protein of the plasma
membrane of leukocytes. The interaction between both receptors
also mediates the activation of gamma-delta T-cells, a
subpopulation of T-cells residing in epithelia and involved in
tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML
induces downstream cell signaling events in gamma-delta T-cells
through PI3-kinase and MAP kinases. It results in proliferation
and production of cytokines and growth factors by T-cells that in
turn stimulate epithelial tissues repair.
{ECO:0000269|PubMed:10814828, ECO:0000269|PubMed:20813954,
ECO:0000269|PubMed:9036860, ECO:0000269|PubMed:9420240}.
-!- SUBUNIT: Monomer. May form homodimer. Interacts with LNX, BAIAP1,
DLG4, PRKCABP, TJP1 and CTNNB1. Interacts with MPDZ; recruits MPDZ
to intercellular contact sites. Interacts with JAML (homodimeric
form). {ECO:0000269|PubMed:20813954, ECO:0000269|PubMed:20813955}.
-!- INTERACTION:
P60710:Actb; NbExp=6; IntAct=EBI-7429264, EBI-353957;
O70263:Lnx1; NbExp=4; IntAct=EBI-7429264, EBI-7650391;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:15533241}; Single-pass type I membrane protein
{ECO:0000255}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane
protein {ECO:0000255}. Cell junction, tight junction
{ECO:0000250|UniProtKB:P78310}. Cell junction, adherens junction
{ECO:0000250|UniProtKB:P78310}. Note=In epithelial cells localizes
to the apical junction complex composed of tight and adherens
junctions. In airway epithelial cells localized to basolateral
membrane but not to apical surface.
{ECO:0000250|UniProtKB:P78310}.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P97792-1; Sequence=Displayed;
Name=2;
IsoId=P97792-2; Sequence=VSP_014829;
Name=3;
IsoId=P97792-3; Sequence=VSP_014827, VSP_014828;
-!- TISSUE SPECIFICITY: Expressed in liver, kidney, heart, lung, and
brain. In skeletal muscle is found at the neuromuscular junction.
In cardiac muscle, isoform 1 and isoform 2 are found at
intercalated disks. {ECO:0000269|PubMed:10814828,
ECO:0000269|PubMed:12763576, ECO:0000269|PubMed:15533241,
ECO:0000269|PubMed:9096397}.
-!- DEVELOPMENTAL STAGE: Expression starts in the embryonic ectoderm
in the uterus on E6.5. Then it is strongly expressed in the
neuroepithelium of the neural tube, the developing brain and the
spinal cord from E8.5 to postnatal day 7 (P7), in the cranial
motor nerves from E9.5 to E11.5, and in the optic nerve from E13.5
to P7. Expression increases until perinatal period and decreases
postnatally. Expressed in the immature neuroepithelium including
progenitor cells it still occurs in a few proliferating cells of
the hippocampal dentate gyrus, the subventricular zone of the
lateral ventricles, and the rostral migratory stream over P21.
Also expressed in heart, kidney and liver of newborn mice.
{ECO:0000269|PubMed:10814828, ECO:0000269|PubMed:12763576}.
-!- DOMAIN: The Ig-like C2-type 1 domain mediates homodimerization and
interaction with JAML. {ECO:0000269|PubMed:20813955}.
-!- DOMAIN: The PDZ-binding motif mediates interaction with MPDZ and
BAIAP1. {ECO:0000250}.
-!- PTM: Palmitoylated on Cys-259 and/or Cys-260; required for proper
localization to the plasma membrane. {ECO:0000250}.
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EMBL; U90715; AAC53148.1; -; mRNA.
EMBL; Y10320; CAA71368.1; -; mRNA.
EMBL; Y11929; CAA72679.1; -; mRNA.
EMBL; AK004908; BAB23660.2; -; mRNA.
EMBL; AK145569; BAE26518.1; -; mRNA.
EMBL; BC004680; AAH04680.1; -; mRNA.
EMBL; BC016457; AAH16457.1; -; mRNA.
CCDS; CCDS28276.1; -. [P97792-1]
CCDS; CCDS37379.1; -. [P97792-2]
RefSeq; NP_001020363.1; NM_001025192.3. [P97792-1]
RefSeq; NP_001263192.1; NM_001276263.1. [P97792-3]
RefSeq; NP_034118.1; NM_009988.4. [P97792-2]
RefSeq; XP_006522946.1; XM_006522883.3. [P97792-1]
RefSeq; XP_006522947.1; XM_006522884.3. [P97792-2]
UniGene; Mm.66222; -.
PDB; 3JZ7; X-ray; 2.19 A; A=20-233.
PDB; 3MJ7; X-ray; 2.80 A; B=18-236.
PDBsum; 3JZ7; -.
PDBsum; 3MJ7; -.
ProteinModelPortal; P97792; -.
SMR; P97792; -.
BioGrid; 198986; 1.
CORUM; P97792; -.
DIP; DIP-41457N; -.
IntAct; P97792; 2.
MINT; MINT-253068; -.
STRING; 10090.ENSMUSP00000023572; -.
iPTMnet; P97792; -.
PhosphoSitePlus; P97792; -.
SwissPalm; P97792; -.
MaxQB; P97792; -.
PaxDb; P97792; -.
PeptideAtlas; P97792; -.
PRIDE; P97792; -.
Ensembl; ENSMUST00000023572; ENSMUSP00000023572; ENSMUSG00000022865. [P97792-1]
Ensembl; ENSMUST00000114229; ENSMUSP00000109867; ENSMUSG00000022865. [P97792-2]
GeneID; 13052; -.
KEGG; mmu:13052; -.
UCSC; uc007zsm.2; mouse. [P97792-3]
UCSC; uc007zsn.2; mouse. [P97792-1]
UCSC; uc007zso.2; mouse. [P97792-2]
CTD; 1525; -.
MGI; MGI:1201679; Cxadr.
eggNOG; ENOG410IGDG; Eukaryota.
eggNOG; ENOG4110WP1; LUCA.
GeneTree; ENSGT00760000119145; -.
HOGENOM; HOG000111222; -.
HOVERGEN; HBG105787; -.
InParanoid; P97792; -.
KO; K06788; -.
OMA; VGNKKIQ; -.
OrthoDB; EOG091G05PI; -.
PhylomeDB; P97792; -.
TreeFam; TF330875; -.
ChiTaRS; Cxadr; mouse.
EvolutionaryTrace; P97792; -.
PRO; PR:P97792; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022865; -.
CleanEx; MM_CXADR; -.
Genevisible; P97792; MM.
GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
GO; GO:0016327; C:apicolateral plasma membrane; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0044297; C:cell body; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0005913; C:cell-cell adherens junction; ISO:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0030175; C:filopodium; IDA:UniProtKB.
GO; GO:0030426; C:growth cone; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
GO; GO:0086082; F:cell adhesive protein binding involved in AV node cell-bundle of His cell communication; IC:BHF-UCL.
GO; GO:0071253; F:connexin binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0086067; P:AV node cell to bundle of His cell communication; IMP:UniProtKB.
GO; GO:0086072; P:AV node cell-bundle of His cell adhesion involved in cell communication; IMP:BHF-UCL.
GO; GO:0048739; P:cardiac muscle fiber development; IMP:MGI.
GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
GO; GO:0051607; P:defense response to virus; ISO:MGI.
GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
GO; GO:0046629; P:gamma-delta T cell activation; IDA:UniProtKB.
GO; GO:0008354; P:germ cell migration; IEP:UniProtKB.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
GO; GO:0034109; P:homotypic cell-cell adhesion; ISS:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:MGI.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IC:UniProtKB.
GO; GO:0098904; P:regulation of AV node cell action potential; IMP:BHF-UCL.
GO; GO:0016337; P:single organismal cell-cell adhesion; IMP:UniProtKB.
GO; GO:0070633; P:transepithelial transport; ISO:MGI.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR013151; Immunoglobulin.
Pfam; PF00047; ig; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 2.
SMART; SM00408; IGc2; 2.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell junction;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted;
Signal; Tight junction; Transmembrane; Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 365 Coxsackievirus and adenovirus receptor
homolog.
/FTId=PRO_0000014740.
TOPO_DOM 20 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
TOPO_DOM 259 365 Cytoplasmic. {ECO:0000255}.
DOMAIN 20 136 Ig-like C2-type 1.
DOMAIN 141 228 Ig-like C2-type 2.
MOTIF 360 365 PDZ-binding. {ECO:0000250}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000250|UniProtKB:P78310}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
LIPID 259 259 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 260 260 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20813955}.
DISULFID 41 120 {ECO:0000244|PDB:3JZ7,
ECO:0000244|PDB:3MJ7,
ECO:0000269|PubMed:20181587,
ECO:0000269|PubMed:20813955}.
DISULFID 146 223 {ECO:0000244|PDB:3JZ7,
ECO:0000244|PDB:3MJ7,
ECO:0000269|PubMed:20181587,
ECO:0000269|PubMed:20813955}.
DISULFID 162 212 {ECO:0000244|PDB:3JZ7,
ECO:0000244|PDB:3MJ7,
ECO:0000269|PubMed:20181587,
ECO:0000269|PubMed:20813955}.
VAR_SEQ 139 164 VKPSGTRCFVDGSEEIGNDFKLKCEP -> GKSSFLLSTGV
EWGGGAELQGGREGG (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014827.
VAR_SEQ 165 365 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014828.
VAR_SEQ 340 365 VAAPNLSRMGAVPVMIPAQSKDGSIV -> FKYAYKTDGIT
VV (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9096397,
ECO:0000303|PubMed:9420240}.
/FTId=VSP_014829.
STRAND 26 32 {ECO:0000244|PDB:3JZ7}.
STRAND 37 39 {ECO:0000244|PDB:3JZ7}.
STRAND 54 65 {ECO:0000244|PDB:3JZ7}.
STRAND 68 75 {ECO:0000244|PDB:3JZ7}.
STRAND 78 80 {ECO:0000244|PDB:3JZ7}.
HELIX 85 87 {ECO:0000244|PDB:3JZ7}.
TURN 88 90 {ECO:0000244|PDB:3JZ7}.
STRAND 91 94 {ECO:0000244|PDB:3JZ7}.
HELIX 98 100 {ECO:0000244|PDB:3JZ7}.
STRAND 105 107 {ECO:0000244|PDB:3JZ7}.
HELIX 112 114 {ECO:0000244|PDB:3JZ7}.
STRAND 116 124 {ECO:0000244|PDB:3JZ7}.
STRAND 127 138 {ECO:0000244|PDB:3JZ7}.
STRAND 145 150 {ECO:0000244|PDB:3JZ7}.
STRAND 158 163 {ECO:0000244|PDB:3JZ7}.
STRAND 172 177 {ECO:0000244|PDB:3JZ7}.
HELIX 186 191 {ECO:0000244|PDB:3JZ7}.
STRAND 194 199 {ECO:0000244|PDB:3JZ7}.
HELIX 204 206 {ECO:0000244|PDB:3JZ7}.
STRAND 208 215 {ECO:0000244|PDB:3JZ7}.
STRAND 220 227 {ECO:0000244|PDB:3JZ7}.
SEQUENCE 365 AA; 39948 MW; 5445B4B52A34B2A2 CRC64;
MARLLCFVLL CGIADFTSGL SITTPEQRIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS
PSDNQIVDQV IILYSGDKIY DNYYPDLKGR VHFTSNDVKS GDASINVTNL QLSDIGTYQC
KVKKAPGVAN KKFLLTVLVK PSGTRCFVDG SEEIGNDFKL KCEPKEGSLP LQFEWQKLSD
SQTMPTPWLA EMTSPVISVK NASSEYSGTY SCTVQNRVGS DQCMLRLDVV PPSNRAGTIA
GAVIGTLLAL VLIGAILFCC HRKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS
SLGSMSPSNM EGYSKTQYNQ VPSEDFERAP QSPTLAPAKV AAPNLSRMGA VPVMIPAQSK
DGSIV


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