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Protein

Coxsackievirus and adenovirus receptor homolog

Gene

Cxadr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • cell adhesion molecule binding Source: UniProtKB
  • cell adhesive protein binding involved in AV node cell-bundle of His cell communication Source: BHF-UCL
  • connexin binding Source: UniProtKB
  • identical protein binding Source: MGI
  • integrin binding Source: MGI
  • PDZ domain binding Source: UniProtKB
  • receptor binding Source: MGI

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • AV node cell-bundle of His cell adhesion involved in cell communication Source: BHF-UCL
  • AV node cell to bundle of His cell communication Source: UniProtKB
  • cardiac muscle fiber development Source: MGI
  • cell-cell junction organization Source: MGI
  • defense response to virus Source: MGI
  • epithelial structure maintenance Source: UniProtKB
  • gamma-delta T cell activation Source: UniProtKB
  • germ cell migration Source: UniProtKB
  • heart development Source: MGI
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  • homotypic cell-cell adhesion Source: UniProtKB
  • mitochondrion organization Source: MGI
  • negative regulation of cardiac muscle cell proliferation Source: MGI
  • neutrophil chemotaxis Source: UniProtKB
  • positive regulation of epithelial cell proliferation involved in wound healing Source: UniProtKB
  • regulation of AV node cell action potential Source: BHF-UCL
  • single organismal cell-cell adhesion Source: UniProtKB
  • transepithelial transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Coxsackievirus and adenovirus receptor homolog
Short name:
CAR
Short name:
mCAR
Gene namesi
Name:Cxadr
Synonyms:Car
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1201679. Cxadr.

Subcellular locationi

Isoform 1 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 237218ExtracellularSequence analysisAdd
BLAST
Transmembranei238 – 25821HelicalSequence analysisAdd
BLAST
Topological domaini259 – 365107CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • acrosomal vesicle Source: MGI
  • adherens junction Source: UniProtKB
  • apicolateral plasma membrane Source: UniProtKB
  • basolateral plasma membrane Source: UniProtKB
  • bicellular tight junction Source: UniProtKB
  • cell body Source: UniProtKB
  • cell-cell junction Source: MGI
  • cell junction Source: MGI
  • cytoplasm Source: UniProtKB
  • extracellular space Source: MGI
  • filopodium Source: UniProtKB
  • growth cone Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • intercalated disc Source: UniProtKB
  • membrane raft Source: UniProtKB
  • neuromuscular junction Source: MGI
  • neuron projection Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 365346Coxsackievirus and adenovirus receptor homologPRO_0000014740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 120Combined sources2 Publications
Glycosylationi106 – 1061N-linked (GlcNAc...)1 Publication
Disulfide bondi146 ↔ 223Combined sources2 Publications
Disulfide bondi162 ↔ 212Combined sources2 Publications
Lipidationi259 – 2591S-palmitoyl cysteineBy similarity
Lipidationi260 – 2601S-palmitoyl cysteineBy similarity
Modified residuei297 – 2971PhosphoserineCombined sources
Modified residuei304 – 3041PhosphoserineCombined sources
Modified residuei306 – 3061PhosphoserineCombined sources
Modified residuei323 – 3231PhosphoserineCombined sources
Modified residuei332 – 3321PhosphoserineBy similarity
Modified residuei363 – 3631PhosphoserineCombined sources

Post-translational modificationi

Palmitoylated on Cys-259 and/or Cys-260; required for proper localization to the plasma membrane.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiP97792.
MaxQBiP97792.
PaxDbiP97792.
PRIDEiP97792.

PTM databases

iPTMnetiP97792.
PhosphoSiteiP97792.
SwissPalmiP97792.

Expressioni

Tissue specificityi

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.4 Publications

Developmental stagei

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.2 Publications

Gene expression databases

BgeeiP97792.
CleanExiMM_CXADR.
GenevisibleiP97792. MM.

Interactioni

Subunit structurei

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).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ActbP607106EBI-7429264,EBI-353957

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • cell adhesion molecule binding Source: UniProtKB
  • cell adhesive protein binding involved in AV node cell-bundle of His cell communication Source: BHF-UCL
  • connexin binding Source: UniProtKB
  • identical protein binding Source: MGI
  • integrin binding Source: MGI
  • PDZ domain binding Source: UniProtKB
  • receptor binding Source: MGI

Protein-protein interaction databases

BioGridi198986. 1 interaction.
DIPiDIP-41457N.
IntActiP97792. 2 interactions.
MINTiMINT-253068.
STRINGi10090.ENSMUSP00000023572.

Structurei

Secondary structure

1
365
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 327Combined sources
Beta strandi37 – 393Combined sources
Beta strandi54 – 6512Combined sources
Beta strandi68 – 758Combined sources
Beta strandi78 – 803Combined sources
Helixi85 – 873Combined sources
Turni88 – 903Combined sources
Beta strandi91 – 944Combined sources
Helixi98 – 1003Combined sources
Beta strandi105 – 1073Combined sources
Helixi112 – 1143Combined sources
Beta strandi116 – 1249Combined sources
Beta strandi127 – 13812Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi158 – 1636Combined sources
Beta strandi172 – 1776Combined sources
Helixi186 – 1916Combined sources
Beta strandi194 – 1996Combined sources
Helixi204 – 2063Combined sources
Beta strandi208 – 2158Combined sources
Beta strandi220 – 2278Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JZ7X-ray2.19A20-233[»]
3MJ7X-ray2.80B18-236[»]
ProteinModelPortaliP97792.
SMRiP97792. Positions 25-233.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP97792.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 136117Ig-like C2-type 1Add
BLAST
Domaini141 – 22888Ig-like C2-type 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi360 – 3656PDZ-bindingBy similarity

Domaini

The Ig-like C2-type 1 domain mediates homodimerization and interaction with JAML.1 Publication
The PDZ-binding motif mediates interaction with MPDZ and BAIAP1.By similarity

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IGDG. Eukaryota.
ENOG4110WP1. LUCA.
GeneTreeiENSGT00760000119145.
HOGENOMiHOG000111222.
HOVERGENiHBG105787.
InParanoidiP97792.
KOiK06788.
OMAiVGNKKIQ.
OrthoDBiEOG7MH0Z1.
PhylomeDBiP97792.
TreeFamiTF330875.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P97792-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARLLCFVLL CGIADFTSGL SITTPEQRIE KAKGETAYLP CKFTLSPEDQ
60 70 80 90 100
GPLDIEWLIS PSDNQIVDQV IILYSGDKIY DNYYPDLKGR VHFTSNDVKS
110 120 130 140 150
GDASINVTNL QLSDIGTYQC KVKKAPGVAN KKFLLTVLVK PSGTRCFVDG
160 170 180 190 200
SEEIGNDFKL KCEPKEGSLP LQFEWQKLSD SQTMPTPWLA EMTSPVISVK
210 220 230 240 250
NASSEYSGTY SCTVQNRVGS DQCMLRLDVV PPSNRAGTIA GAVIGTLLAL
260 270 280 290 300
VLIGAILFCC HRKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS
310 320 330 340 350
SLGSMSPSNM EGYSKTQYNQ VPSEDFERAP QSPTLAPAKV AAPNLSRMGA
360
VPVMIPAQSK DGSIV
Length:365
Mass (Da):39,948
Last modified:May 1, 1997 - v1
Checksum:i5445B4B52A34B2A2
GO
Isoform 2 (identifier: P97792-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     340-365: VAAPNLSRMGAVPVMIPAQSKDGSIV → FKYAYKTDGITVV

Show »
Length:352
Mass (Da):38,843
Checksum:i2BD8CBD25D8CE123
GO
Isoform 3 (identifier: P97792-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     139-164: VKPSGTRCFVDGSEEIGNDFKLKCEP → GKSSFLLSTGVEWGGGAELQGGREGG
     165-365: Missing.

Show »
Length:164
Mass (Da):17,781
Checksum:i9DEFCBD456240C73
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei139 – 16426VKPSG…LKCEP → GKSSFLLSTGVEWGGGAELQ GGREGG in isoform 3. 1 PublicationVSP_014827Add
BLAST
Alternative sequencei165 – 365201Missing in isoform 3. 1 PublicationVSP_014828Add
BLAST
Alternative sequencei340 – 36526VAAPN…DGSIV → FKYAYKTDGITVV in isoform 2. 3 PublicationsVSP_014829Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90715 mRNA. Translation: AAC53148.1.
Y10320 mRNA. Translation: CAA71368.1.
Y11929 mRNA. Translation: CAA72679.1.
AK004908 mRNA. Translation: BAB23660.2.
AK145569 mRNA. Translation: BAE26518.1.
BC004680 mRNA. Translation: AAH04680.1.
BC016457 mRNA. Translation: AAH16457.1.
CCDSiCCDS28276.1. [P97792-1]
CCDS37379.1. [P97792-2]
RefSeqiNP_001020363.1. NM_001025192.3. [P97792-1]
NP_001263192.1. NM_001276263.1. [P97792-3]
NP_034118.1. NM_009988.4. [P97792-2]
XP_006522946.1. XM_006522883.2. [P97792-1]
XP_006522947.1. XM_006522884.2. [P97792-2]
UniGeneiMm.66222.

Genome annotation databases

EnsembliENSMUST00000023572; ENSMUSP00000023572; ENSMUSG00000022865. [P97792-1]
ENSMUST00000114229; ENSMUSP00000109867; ENSMUSG00000022865. [P97792-2]
GeneIDi13052.
KEGGimmu:13052.
UCSCiuc007zsm.2. mouse. [P97792-3]
uc007zsn.2. mouse. [P97792-1]
uc007zso.2. mouse. [P97792-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90715 mRNA. Translation: AAC53148.1.
Y10320 mRNA. Translation: CAA71368.1.
Y11929 mRNA. Translation: CAA72679.1.
AK004908 mRNA. Translation: BAB23660.2.
AK145569 mRNA. Translation: BAE26518.1.
BC004680 mRNA. Translation: AAH04680.1.
BC016457 mRNA. Translation: AAH16457.1.
CCDSiCCDS28276.1. [P97792-1]
CCDS37379.1. [P97792-2]
RefSeqiNP_001020363.1. NM_001025192.3. [P97792-1]
NP_001263192.1. NM_001276263.1. [P97792-3]
NP_034118.1. NM_009988.4. [P97792-2]
XP_006522946.1. XM_006522883.2. [P97792-1]
XP_006522947.1. XM_006522884.2. [P97792-2]
UniGeneiMm.66222.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JZ7X-ray2.19A20-233[»]
3MJ7X-ray2.80B18-236[»]
ProteinModelPortaliP97792.
SMRiP97792. Positions 25-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198986. 1 interaction.
DIPiDIP-41457N.
IntActiP97792. 2 interactions.
MINTiMINT-253068.
STRINGi10090.ENSMUSP00000023572.

PTM databases

iPTMnetiP97792.
PhosphoSiteiP97792.
SwissPalmiP97792.

Proteomic databases

EPDiP97792.
MaxQBiP97792.
PaxDbiP97792.
PRIDEiP97792.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023572; ENSMUSP00000023572; ENSMUSG00000022865. [P97792-1]
ENSMUST00000114229; ENSMUSP00000109867; ENSMUSG00000022865. [P97792-2]
GeneIDi13052.
KEGGimmu:13052.
UCSCiuc007zsm.2. mouse. [P97792-3]
uc007zsn.2. mouse. [P97792-1]
uc007zso.2. mouse. [P97792-2]

Organism-specific databases

CTDi1525.
MGIiMGI:1201679. Cxadr.

Phylogenomic databases

eggNOGiENOG410IGDG. Eukaryota.
ENOG4110WP1. LUCA.
GeneTreeiENSGT00760000119145.
HOGENOMiHOG000111222.
HOVERGENiHBG105787.
InParanoidiP97792.
KOiK06788.
OMAiVGNKKIQ.
OrthoDBiEOG7MH0Z1.
PhylomeDBiP97792.
TreeFamiTF330875.

Miscellaneous databases

ChiTaRSiCxadr. mouse.
EvolutionaryTraceiP97792.
NextBioi282970.
PROiP97792.
SOURCEiSearch...

Gene expression databases

BgeeiP97792.
CleanExiMM_CXADR.
GenevisibleiP97792. MM.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "HCAR and MCAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses."
    Tomko R.P., Xu R., Philipson L.
    Proc. Natl. Acad. Sci. U.S.A. 94:3352-3356(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Strain: C3H/Mai.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS A VIRUS RECEPTOR.
    Strain: C57BL/6J.
    Tissue: Colon and Liver.
  3. "The murine CAR homolog is a receptor for coxsackie B viruses and adenoviruses."
    Bergelson J.M., Krithivas A., Celi L., Droguett G., Horwitz M.S., Wickham T., Crowell R.L., Finberg R.W.
    J. Virol. 72:415-419(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION AS A VIRUS RECEPTOR.
    Strain: C57BL/6J.
    Tissue: Liver.
  4. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Liver.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: FVB/N.
    Tissue: Mammary gland.
  6. "The coxsackievirus-adenovirus receptor protein as a cell adhesion molecule in the developing mouse brain."
    Honda T., Saitoh H., Masuko M., Katagiri-Abe T., Tominaga K., Kozakai I., Kobayashi K., Kumanishi T., Watanabe Y.G., Odani S., Kuwano R.
    Brain Res. Mol. Brain Res. 77:19-28(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION, FUNCTION.
  7. "Developmental distribution of coxsackie virus and adenovirus receptor localized in the nervous system."
    Hotta Y., Honda T., Naito M., Kuwano R.
    Brain Res. Dev. Brain Res. 143:1-13(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. "Isoform-specific expression of the Coxsackie and adenovirus receptor (CAR) in neuromuscular junction and cardiac intercalated discs."
    Shaw C.A., Holland P.C., Sinnreich M., Allen C., Sollerbrant K., Karpati G., Nalbantoglu J.
    BMC Cell Biol. 5:42-42(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-304; SER-306; SER-323 AND SER-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung and Pancreas.
  11. "The junctional adhesion molecule JAML is a costimulatory receptor for epithelial gammadelta T cell activation."
    Witherden D.A., Verdino P., Rieder S.E., Garijo O., Mills R.E., Teyton L., Fischer W.H., Wilson I.A., Havran W.L.
    Science 329:1205-1210(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN T-CELL ACTIVATION, INTERACTION WITH CXADR.
  12. "The coxsackievirus-adenovirus receptor reveals complex homophilic and heterophilic interactions on neural cells."
    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.
    J. Neurosci. 30:2897-2910(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 20-233, DISULFIDE BONDS.
  13. "The molecular interaction of CAR and JAML recruits the central cell signal transducer PI3K."
    Verdino P., Witherden D.A., Havran W.L., Wilson I.A.
    Science 329:1210-1214(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-236 IN COMPLEX WITH JAML, DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-106.

Entry informationi

Entry nameiCXAR_MOUSE
AccessioniPrimary (citable) accession number: P97792
Secondary accession number(s): O09052
, Q3ULD0, Q91W66, Q99KG0, Q9DBJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: May 11, 2016
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.