Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P78310

- CXAR_HUMAN

UniProt

P78310 - CXAR_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Coxsackievirus and adenovirus receptor

Gene

CXADR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Component of the epithelial apical junction complex that may function as an homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with AMICA1/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, AMICA1 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.5 Publications

GO - Molecular functioni

  1. beta-catenin binding Source: UniProtKB
  2. cell adhesion molecule binding Source: UniProtKB
  3. connexin binding Source: UniProtKB
  4. identical protein binding Source: UniProtKB
  5. integrin binding Source: UniProtKB
  6. PDZ domain binding Source: UniProtKB
  7. receptor binding Source: UniProtKB
  8. virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. AV node cell to bundle of His cell communication Source: UniProtKB
  3. blood coagulation Source: Reactome
  4. cardiac muscle fiber development Source: UniProtKB
  5. cell-cell junction organization Source: UniProtKB
  6. defense response to virus Source: UniProtKB
  7. epithelial structure maintenance Source: UniProtKB
  8. gamma-delta T cell activation Source: UniProtKB
  9. germ cell migration Source: UniProtKB
  10. heart development Source: UniProtKB
  11. heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  12. homotypic cell-cell adhesion Source: UniProtKB
  13. leukocyte migration Source: Reactome
  14. mitochondrion organization Source: UniProtKB
  15. neutrophil chemotaxis Source: UniProtKB
  16. regulation of immune response Source: Reactome
  17. transepithelial transport Source: UniProtKB
  18. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Cell adhesion, Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_12051. Cell surface interactions at the vascular wall.

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Coxsackievirus and adenovirus receptor
Short name:
CAR
Short name:
hCAR
Alternative name(s):
CVB3-binding protein
Coxsackievirus B-adenovirus receptor
HCVADR
Gene namesi
Name:CXADR
Synonyms:CAR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:2559. CXADR.

Subcellular locationi

Isoform 1 : Cell membrane; Single-pass type I membrane protein. Cell junctiontight junction. Cell junctionadherens junction. Basolateral cell membrane; Single-pass type I membrane protein
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.
Isoform 2 : Cell membrane; Single-pass type I membrane protein. Cell junctiontight junction. Cell junctionadherens junction. Basolateral cell membrane; Single-pass membrane protein
Note: In epithelial cells localizes to the apical junction complex composced of tight and adherens junctions. In airway epithelial cells localized to basolateral membrane but not to apical surface.

Topology

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

GO - Cellular componenti

  1. acrosomal vesicle Source: UniProtKB
  2. adherens junction Source: UniProtKB
  3. apicolateral plasma membrane Source: UniProtKB
  4. basolateral plasma membrane Source: UniProtKB
  5. cell body Source: UniProtKB
  6. cell-cell junction Source: UniProtKB
  7. cell junction Source: HPA
  8. extracellular region Source: UniProtKB-KW
  9. extracellular space Source: UniProtKB
  10. filopodium Source: UniProtKB
  11. growth cone Source: UniProtKB
  12. integral component of plasma membrane Source: UniProtKB
  13. intercalated disc Source: UniProtKB
  14. membrane raft Source: UniProtKB
  15. neuromuscular junction Source: UniProtKB
  16. neuron projection Source: UniProtKB
  17. nucleus Source: HPA
  18. plasma membrane Source: UniProtKB
  19. protein complex Source: UniProtKB
  20. tight junction Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi70 – 723VII → AID: Abolishes binding to adenovirus type 5. 1 Publication
Mutagenesisi259 – 2602CC → AA: Loss of palmitoylation and altered localization. 1 Publication
Mutagenesisi318 – 3181Y → A: Affects basolateral localization in airway epithelial cells. 1 Publication
Mutagenesisi345 – 3484LSRM → AAAA: Affects basolateral localization in airway epithelial cells. 1 Publication

Organism-specific databases

PharmGKBiPA27055.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 365346Coxsackievirus and adenovirus receptorPRO_0000014739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 120
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi162 ↔ 212PROSITE-ProRule annotation
Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
Lipidationi259 – 2591S-palmitoyl cysteine1 Publication
Lipidationi260 – 2601S-palmitoyl cysteine1 Publication
Modified residuei306 – 3061Phosphoserine1 Publication
Modified residuei323 – 3231PhosphoserineBy similarity
Modified residuei332 – 3321Phosphoserine1 Publication

Post-translational modificationi

N-glycosylated.By similarity
Palmitoylated on Cys-259 and/or Cys-260; required for proper localization to the plasma membrane.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP78310.
PaxDbiP78310.
PRIDEiP78310.

PTM databases

PhosphoSiteiP78310.

Expressioni

Tissue specificityi

Expressed in pancreas, brain, heart, small intestine, testis, prostate and at a lower level in liver and lung. Isoform 5 is ubiquitously expressed. Isoform 3 is expressed in heart, lung and pancreas. In skeletal muscle, isoform 1 is found at the neuromuscular junction and isoform 2 is found in blood vessels. In cardiac muscle, isoform 1 and isoform 2 are found at intercalated disks. In heart expressed in subendothelial layers of the vessel wall but not in the luminal endothelial surface. Expression is elevated in hearts with dilated cardiomyopathy.4 Publications

Gene expression databases

BgeeiP78310.
CleanExiHS_CXADR.
GenevestigatoriP78310.

Organism-specific databases

HPAiCAB005103.
HPA003342.
HPA030411.
HPA030412.

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 AMICA1 (homodimeric form). Secreted isoform 3, isoform 4 and isoform 5 can interact with the extracellular domain of the receptor. Interacts with adenovirus subgroups A, C, D, E and F fiber proteins as well as coxsackievirus B1, B2, B3, B4, B5 and B6 capsid proteins and acts as a receptor for these viruses.12 Publications

Protein-protein interaction databases

BioGridi107905. 13 interactions.
IntActiP78310. 3 interactions.
MINTiMINT-111007.
STRINGi9606.ENSP00000284878.

Structurei

Secondary structure

1
365
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 3212Combined sources
Beta strandi37 – 393Combined sources
Beta strandi42 – 443Combined sources
Beta strandi53 – 619Combined sources
Beta strandi62 – 654Combined sources
Beta strandi68 – 758Combined sources
Beta strandi78 – 803Combined sources
Turni86 – 905Combined sources
Beta strandi91 – 933Combined sources
Helixi98 – 1003Combined sources
Beta strandi105 – 1073Combined sources
Helixi112 – 1143Combined sources
Beta strandi116 – 1249Combined sources
Beta strandi127 – 13812Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi156 – 1638Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi171 – 1788Combined sources
Helixi185 – 1928Combined sources
Beta strandi195 – 2017Combined sources
Beta strandi208 – 2158Combined sources
Beta strandi221 – 2277Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EAJX-ray1.35A/B15-140[»]
1F5WX-ray1.70A/B15-140[»]
1JEWelectron microscopy22.00R21-140[»]
1KACX-ray2.60B22-144[»]
1P69X-ray3.10B22-144[»]
1P6AX-ray2.90B22-144[»]
1RSFNMR-A21-144[»]
2J12X-ray1.50B15-140[»]
2J1KX-ray2.30A/B/G/J/K/O/P/T/V/X/Y/Z15-140[»]
2NPLNMR-X142-235[»]
2W9LX-ray2.91A/B/G/J/K/O/P/T/V/X/Y/Z16-139[»]
2WBWX-ray1.55B15-138[»]
3J6Lelectron microscopy9.00B15-140[»]
3J6Melectron microscopy9.00B22-144[»]
3J6Nelectron microscopy9.00K20-233[»]
3J6Oelectron microscopy9.00S20-236[»]
ProteinModelPortaliP78310.
SMRiP78310. Positions 16-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78310.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 134115Ig-like C2-type 1Add
BLAST
Domaini141 – 22888Ig-like C2-type 2Add
BLAST

Motif

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

Domaini

The Ig-like C2-type 1 domain mediates homodimerization and interaction with AMICA1.
The PDZ-binding motif mediates interaction with MPDZ and BAIAP1.

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG83644.
GeneTreeiENSGT00760000119145.
HOGENOMiHOG000111222.
HOVERGENiHBG105787.
InParanoidiP78310.
KOiK06788.
OMAiTEYSGTY.
OrthoDBiEOG7MH0Z1.
PhylomeDBiP78310.
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.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P78310-1) [UniParc]FASTAAdd to Basket

Also known as: SIV

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
MALLLCFVLL CGVVDFARSL SITTPEEMIE KAKGETAYLP CKFTLSPEDQ
60 70 80 90 100
GPLDIEWLIS PADNQKVDQV IILYSGDKIY DDYYPDLKGR VHFTSNDLKS
110 120 130 140 150
GDASINVTNL QLSDIGTYQC KVKKAPGVAN KKIHLVVLVK PSGARCYVDG
160 170 180 190 200
SEEIGSDFKI KCEPKEGSLP LQYEWQKLSD SQKMPTSWLA EMTSSVISVK
210 220 230 240 250
NASSEYSGTY SCTVRNRVGS DQCLLRLNVV PPSNKAGLIA GAIIGTLLAL
260 270 280 290 300
ALIGLIIFCC RKKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS
310 320 330 340 350
SLGSMSPSNM EGYSKTQYNQ VPSEDFERTP QSPTLPPAKV AAPNLSRMGA
360
IPVMIPAQSK DGSIV
Length:365
Mass (Da):40,030
Last modified:May 1, 1997 - v1
Checksum:iAB01C6346CB7FE64
GO
Isoform 2 (identifier: P78310-2) [UniParc]FASTAAdd to Basket

Also known as: CAR2, HCAR2, TVV

The sequence of this isoform differs from the canonical sequence as follows:
     340-345: VAAPNL → FKYPY
     346-365: Missing.

Show »
Length:344
Mass (Da):38,124
Checksum:iEEE9C22E96C697AA
GO
Isoform 3 (identifier: P78310-3) [UniParc]FASTAAdd to Basket

Also known as: CAR2/7, Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     71-89: IILYSGDKIYDDYYPDLKG → GRCATSKEPYVHCQKLHRQ
     90-365: Missing.

Show »
Length:89
Mass (Da):9,967
Checksum:i50951EAAC77CAE36
GO
Isoform 4 (identifier: P78310-4) [UniParc]FASTAAdd to Basket

Also known as: CAR3/7

The sequence of this isoform differs from the canonical sequence as follows:
     139-139: V → GKMCHLQRAVRPLPEATSAVIIHPWGPCLLPTWKDIPRLSITKYQVKTLNALLRVRLSHLLR
     140-365: Missing.

Show »
Length:200
Mass (Da):22,370
Checksum:i43FDB19DF6A7FEB8
GO
Isoform 5 (identifier: P78310-5) [UniParc]FASTAAdd to Basket

Also known as: CAR4/7, Beta

The sequence of this isoform differs from the canonical sequence as follows:
     191-191: E → GKMCHLQRAVRPLPEATSAVIIHPWGPCLLPTWKDIPRLSITKYQVKTLNALLRVRLSHLLR
     192-365: Missing.

Show »
Length:252
Mass (Da):28,201
Checksum:i4532559D01AB67E2
GO
Isoform 6 (identifier: P78310-6) [UniParc]FASTAAdd to Basket

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

Note: Gene prediction based on EST data.

Show »
Length:352
Mass (Da):38,938
Checksum:i0D7C56FEBE6BD653
GO
Isoform 7 (identifier: P78310-7) [UniParc]FASTAAdd to Basket

Also known as: CAR 4/6

The sequence of this isoform differs from the canonical sequence as follows:
     191-232: EMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPP → A

Show »
Length:324
Mass (Da):35,570
Checksum:i97915CFCAF43B698
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: P78310-2)
Sequence conflicti343 – 3431P → A in AAD31772. (PubMed:10490761)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti323 – 3231S → R.
Corresponds to variant rs34727960 [ dbSNP | Ensembl ].
VAR_049871

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei71 – 8919IILYS…PDLKG → GRCATSKEPYVHCQKLHRQ in isoform 3. 1 PublicationVSP_014819Add
BLAST
Alternative sequencei90 – 365276Missing in isoform 3. 1 PublicationVSP_014820Add
BLAST
Alternative sequencei139 – 1391V → GKMCHLQRAVRPLPEATSAV IIHPWGPCLLPTWKDIPRLS ITKYQVKTLNALLRVRLSHL LR in isoform 4. 1 PublicationVSP_014821
Alternative sequencei140 – 365226Missing in isoform 4. 1 PublicationVSP_014822Add
BLAST
Alternative sequencei191 – 23242EMTSS…NVVPP → A in isoform 7. 1 PublicationVSP_047729Add
BLAST
Alternative sequencei191 – 1911E → GKMCHLQRAVRPLPEATSAV IIHPWGPCLLPTWKDIPRLS ITKYQVKTLNALLRVRLSHL LR in isoform 5. 1 PublicationVSP_014823
Alternative sequencei192 – 365174Missing in isoform 5. 1 PublicationVSP_014824Add
BLAST
Alternative sequencei340 – 36526VAAPN…DGSIV → FKYPYKTDGITVV in isoform 6. CuratedVSP_047357Add
BLAST
Alternative sequencei340 – 3456VAAPNL → FKYPY in isoform 2. 1 PublicationVSP_014825
Alternative sequencei346 – 36520Missing in isoform 2. 1 PublicationVSP_014826Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90716 mRNA. Translation: AAC51234.1.
Y07593 mRNA. Translation: CAA68868.1.
AF169366
, AF169360, AF169361, AF169362, AF169363, AF169364, AF169365 Genomic DNA. Translation: AAF05908.1.
AF200465 Genomic DNA. Translation: AAF24344.1.
AY072910 mRNA. Translation: AAL68878.1.
AY072911 mRNA. Translation: AAL68879.1.
AY072912 mRNA. Translation: AAL68880.1.
AF242865, AF242862, AF242864 Genomic DNA. Translation: AAG01088.1.
GU474812 mRNA. Translation: ADC84500.1.
CR617256 mRNA. No translation available.
BT019876 mRNA. Translation: AAV38679.1.
AK313526 mRNA. Translation: BAG36305.1.
AP000963 Genomic DNA. No translation available.
AP000967 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX10031.1.
BC003684 mRNA. Translation: AAH03684.1.
BC010536 mRNA. Translation: AAH10536.1.
AF124598 mRNA. Translation: AAD31772.1.
CCDSiCCDS33519.1. [P78310-1]
CCDS56204.1. [P78310-6]
CCDS56205.1. [P78310-5]
CCDS56206.1. [P78310-4]
CCDS56207.1. [P78310-3]
RefSeqiNP_001193992.1. NM_001207063.1. [P78310-5]
NP_001193993.1. NM_001207064.1. [P78310-4]
NP_001193994.1. NM_001207065.1. [P78310-3]
NP_001193995.1. NM_001207066.1. [P78310-6]
NP_001329.1. NM_001338.4. [P78310-1]
UniGeneiHs.627078.

Genome annotation databases

EnsembliENST00000284878; ENSP00000284878; ENSG00000154639. [P78310-1]
ENST00000356275; ENSP00000348620; ENSG00000154639. [P78310-3]
ENST00000400165; ENSP00000383029; ENSG00000154639. [P78310-4]
ENST00000400166; ENSP00000383030; ENSG00000154639. [P78310-5]
ENST00000400169; ENSP00000383033; ENSG00000154639. [P78310-6]
GeneIDi1525.
KEGGihsa:1525.
UCSCiuc002ykh.2. human. [P78310-5]
uc002yki.3. human. [P78310-1]
uc010gld.2. human. [P78310-4]
uc010gle.2. human. [P78310-3]

Polymorphism databases

DMDMi6685351.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90716 mRNA. Translation: AAC51234.1 .
Y07593 mRNA. Translation: CAA68868.1 .
AF169366
, AF169360 , AF169361 , AF169362 , AF169363 , AF169364 , AF169365 Genomic DNA. Translation: AAF05908.1 .
AF200465 Genomic DNA. Translation: AAF24344.1 .
AY072910 mRNA. Translation: AAL68878.1 .
AY072911 mRNA. Translation: AAL68879.1 .
AY072912 mRNA. Translation: AAL68880.1 .
AF242865 , AF242862 , AF242864 Genomic DNA. Translation: AAG01088.1 .
GU474812 mRNA. Translation: ADC84500.1 .
CR617256 mRNA. No translation available.
BT019876 mRNA. Translation: AAV38679.1 .
AK313526 mRNA. Translation: BAG36305.1 .
AP000963 Genomic DNA. No translation available.
AP000967 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX10031.1 .
BC003684 mRNA. Translation: AAH03684.1 .
BC010536 mRNA. Translation: AAH10536.1 .
AF124598 mRNA. Translation: AAD31772.1 .
CCDSi CCDS33519.1. [P78310-1 ]
CCDS56204.1. [P78310-6 ]
CCDS56205.1. [P78310-5 ]
CCDS56206.1. [P78310-4 ]
CCDS56207.1. [P78310-3 ]
RefSeqi NP_001193992.1. NM_001207063.1. [P78310-5 ]
NP_001193993.1. NM_001207064.1. [P78310-4 ]
NP_001193994.1. NM_001207065.1. [P78310-3 ]
NP_001193995.1. NM_001207066.1. [P78310-6 ]
NP_001329.1. NM_001338.4. [P78310-1 ]
UniGenei Hs.627078.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EAJ X-ray 1.35 A/B 15-140 [» ]
1F5W X-ray 1.70 A/B 15-140 [» ]
1JEW electron microscopy 22.00 R 21-140 [» ]
1KAC X-ray 2.60 B 22-144 [» ]
1P69 X-ray 3.10 B 22-144 [» ]
1P6A X-ray 2.90 B 22-144 [» ]
1RSF NMR - A 21-144 [» ]
2J12 X-ray 1.50 B 15-140 [» ]
2J1K X-ray 2.30 A/B/G/J/K/O/P/T/V/X/Y/Z 15-140 [» ]
2NPL NMR - X 142-235 [» ]
2W9L X-ray 2.91 A/B/G/J/K/O/P/T/V/X/Y/Z 16-139 [» ]
2WBW X-ray 1.55 B 15-138 [» ]
3J6L electron microscopy 9.00 B 15-140 [» ]
3J6M electron microscopy 9.00 B 22-144 [» ]
3J6N electron microscopy 9.00 K 20-233 [» ]
3J6O electron microscopy 9.00 S 20-236 [» ]
ProteinModelPortali P78310.
SMRi P78310. Positions 16-235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107905. 13 interactions.
IntActi P78310. 3 interactions.
MINTi MINT-111007.
STRINGi 9606.ENSP00000284878.

Protein family/group databases

MEROPSi I43.001.

PTM databases

PhosphoSitei P78310.

Polymorphism databases

DMDMi 6685351.

Proteomic databases

MaxQBi P78310.
PaxDbi P78310.
PRIDEi P78310.

Protocols and materials databases

DNASUi 1525.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000284878 ; ENSP00000284878 ; ENSG00000154639 . [P78310-1 ]
ENST00000356275 ; ENSP00000348620 ; ENSG00000154639 . [P78310-3 ]
ENST00000400165 ; ENSP00000383029 ; ENSG00000154639 . [P78310-4 ]
ENST00000400166 ; ENSP00000383030 ; ENSG00000154639 . [P78310-5 ]
ENST00000400169 ; ENSP00000383033 ; ENSG00000154639 . [P78310-6 ]
GeneIDi 1525.
KEGGi hsa:1525.
UCSCi uc002ykh.2. human. [P78310-5 ]
uc002yki.3. human. [P78310-1 ]
uc010gld.2. human. [P78310-4 ]
uc010gle.2. human. [P78310-3 ]

Organism-specific databases

CTDi 1525.
GeneCardsi GC21P018884.
HGNCi HGNC:2559. CXADR.
HPAi CAB005103.
HPA003342.
HPA030411.
HPA030412.
MIMi 602621. gene.
neXtProti NX_P78310.
PharmGKBi PA27055.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG83644.
GeneTreei ENSGT00760000119145.
HOGENOMi HOG000111222.
HOVERGENi HBG105787.
InParanoidi P78310.
KOi K06788.
OMAi TEYSGTY.
OrthoDBi EOG7MH0Z1.
PhylomeDBi P78310.
TreeFami TF330875.

Enzyme and pathway databases

Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_12051. Cell surface interactions at the vascular wall.

Miscellaneous databases

ChiTaRSi CXADR. human.
EvolutionaryTracei P78310.
GeneWikii Coxsackie_virus_and_adenovirus_receptor.
GenomeRNAii 1525.
NextBioi 35491112.
PROi P78310.
SOURCEi Search...

Gene expression databases

Bgeei P78310.
CleanExi HS_CXADR.
Genevestigatori P78310.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view ]
Pfami PF07686. V-set. 1 hit.
[Graphical view ]
SMARTi SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 2 hits.
[Graphical view ]
ProtoNeti Search...

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 1), FUNCTION AS A VIRUS RECEPTOR, TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Genomic organization and chromosomal localization of the human Coxsackievirus B-adenovirus receptor gene."
    Bowles K.R., Gibson J., Wu J., Shaffer L.G., Towbin J.A., Bowles N.E.
    Hum. Genet. 105:354-359(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor."
    He Y., Chipman P.R., Howitt J., Bator C.M., Whitt M.A., Baker T.S., Kuhn R.J., Anderson C.W., Freimuth P., Rossmann M.G.
    Nat. Struct. Biol. 8:874-878(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Alternatively spliced soluble coxsackie-adenovirus receptors inhibit coxsackievirus infection."
    Doerner A., Xiong D., Couch K., Yajima T., Knowlton K.U.
    J. Biol. Chem. 279:18497-18503(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5), INTERACTION WITH COXSACKIEVIRUS TYPE B3, SUBCELLULAR LOCATION.
  6. "Putative regulatory domains in the human and mouse CAR genes."
    Andersson B., Tomko R.P., Andersson K., Darban H., Oncu D., Mizra M., Sollerbrant K., Sonnhammer E., Philipson L.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "Identification and characterisation of CAR 4/6 as a new splice variant of the Coxsackie adenovirus receptor (CAR)."
    Dietel M.
    Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
  8. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cervix.
  9. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  10. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  11. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. "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] (ISOFORM 1).
    Tissue: Cervix.
  14. "Expression of Coxsackie-adenovirus-receptor and alpha v-integrin does not correlate with adenovector targeting in vivo indicating anatomical vector barriers."
    Fechner H., Haack A., Wang H., Wang X., Eizema K., Pauschinger M., Schoemaker R.G., van Veghel R., Houtsmuller A.B., Schultheiss H.-P., Lamers J.M.J., Poller W.
    Gene Ther. 6:1520-1535(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Tissue: Liver.
  15. "The coxsackievirus-adenovirus receptor protein can function as a cellular attachment protein for adenovirus serotypes from subgroups A, C, D, E, and F."
    Roelvink P.W., Lizonova A., Lee J.G.M., Li Y., Bergelson J.M., Finberg R.W., Brough D.E., Kovesdi I., Wickham T.J.
    J. Virol. 72:7909-7915(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN ADENOVIRUS SUBGROUPS A/C/D/E/F FIBER PROTEINS.
  16. "Expression of the adenovirus receptor and its interaction with the fiber knob."
    Tomko R.P., Johansson C.B., Totrov M., Abagyan R., Frisen J., Philipson L.
    Exp. Cell Res. 255:47-55(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN ADENOVIRUS FIBER PROTEIN, MUTAGENESIS OF 70-VAL--ILE-72.
  17. "The coxsackie-adenovirus receptor (CAR) is used by reference strains and clinical isolates representing all six serotypes of coxsackievirus group B and by swine vesicular disease virus."
    Martino T.A., Petric M., Weingartl H., Bergelson J.M., Opavsky M.A., Richardson C.D., Modlin J.F., Finberg R.W., Kain K.C., Willis N., Gauntt C.J., Liu P.P.
    Virology 271:99-108(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COXSACKIEVIRUS GROUP B CAPSID PROTEINS.
  18. "Identification of alternative splice products encoded by the human coxsackie-adenovirus receptor gene."
    Thoelen I., Magnusson C., Tagerud S., Polacek C., Lindberg M., Van Ranst M.
    Biochem. Biophys. Res. Commun. 287:216-222(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  19. "Human coxsackie-adenovirus receptor is colocalized with integrins alpha(v)beta(3) and alpha(v)beta(5) on the cardiomyocyte sarcolemma and upregulated in dilated cardiomyopathy: implications for cardiotropic viral infections."
    Noutsias M., Fechner H., de Jonge H., Wang X., Dekkers D., Houtsmuller A.B., Pauschinger M., Bergelson J.M., Warraich R., Yacoub M., Hetzer R., Lamers J.M.J., Schultheiss H.-P., Poller W.
    Circulation 104:275-280(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  20. "Multiple regions within the coxsackievirus and adenovirus receptor cytoplasmic domain are required for basolateral sorting."
    Cohen C.J., Gaetz J., Ohman T., Bergelson J.M.
    J. Biol. Chem. 276:25392-25398(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-318 AND 345-LEU--MET-348.
  21. "The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction."
    Cohen C.J., Shieh J.T.C., Pickles R.J., Okegawa T., Hsieh J.-T., Bergelson J.M.
    Proc. Natl. Acad. Sci. U.S.A. 98:15191-15196(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TJP1, FUNCTION.
  22. "Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape."
    Walters R.W., Freimuth P., Moninger T.O., Ganske I., Zabner J., Welsh M.J.
    Cell 110:789-799(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1, INTERACTION WITH HUMAN ADENOVIRUS FIBER PROTEIN, FUNCTION.
  23. "Fatty acid modification of the coxsackievirus and adenovirus receptor."
    van't Hof W., Crystal R.G.
    J. Virol. 76:6382-6386(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-259 AND CYS-260, SUBCELLULAR LOCATION, MUTAGENESIS OF 259-CYS-CYS-260.
  24. "The Coxsackievirus and adenovirus receptor (CAR) forms a complex with the PDZ domain-containing protein ligand-of-numb protein-X (LNX)."
    Sollerbrant K., Raschperger E., Mirza M., Engstroem U., Philipson L., Ljungdahl P.O., Pettersson R.F.
    J. Biol. Chem. 278:7439-7444(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LNX.
  25. "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 (ISOFORMS 1 AND 2).
  26. "The coxsackievirus and adenovirus receptor interacts with the multi-PDZ domain protein-1 (MUPP-1) within the tight junction."
    Coyne C.B., Voelker T., Pichla S.L., Bergelson J.M.
    J. Biol. Chem. 279:48079-48084(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MPDZ, SUBCELLULAR LOCATION.
  27. "A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth."
    Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L., Zabner J.
    J. Cell Sci. 117:4401-4409(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAIAP1; DLG4 AND PRKCABP.
  28. "Neutrophil migration across tight junctions is mediated by adhesive interactions between epithelial CAR and a JAM-like protein on neutrophils."
    Zen K., Liu Y., McCall I.C., Wu T., Lee W., Babbin B.A., Nusrat A., Parkos C.A.
    Mol. Biol. Cell 16:2694-2703(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AMICA1, DOMAIN, FUNCTION.
  29. "JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis by alpha4beta1 integrin activation."
    Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O., Bourdoulous S.
    J. Cell Biol. 183:1159-1173(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LEUKOCYTE MIGRATION, INTERACTION WITH AMICA1.
  30. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  32. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR."
    Bewley M.C., Springer K., Zhang Y.-B., Freimuth P., Flanagan J.M.
    Science 286:1579-1583(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-144 IN COMPLEX WITH HUMAN ADENOVIRUS 12 FIBER PROTEIN.
  34. "Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution."
    van Raaij M.J., Chouin E., van der Zandt H., Bergelson J.M., Cusack S.
    Structure 8:1147-1155(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 15-140, DOMAIN.
  35. "Solution structure of the coxsackievirus and adenovirus receptor domain 1."
    Jiang S., Jacobs A., Laue T.M., Caffrey M.
    Biochemistry 43:1847-1853(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 21-144.

Entry informationi

Entry nameiCXAR_HUMAN
AccessioniPrimary (citable) accession number: P78310
Secondary accession number(s): B2R8V8
, B7WPI3, D3YHP0, O00694, Q8WWT6, Q8WWT7, Q8WWT8, Q9UKV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: November 26, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3