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P78310

- CXAR_HUMAN

UniProt

P78310 - CXAR_HUMAN

Protein

Coxsackievirus and adenovirus receptor

Gene

CXADR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    8. receptor binding Source: UniProtKB
    9. 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 Source: UniProtKB
    12. homotypic cell-cell adhesion Source: UniProtKB
    13. leukocyte migration Source: Reactome
    14. mitochondrion organization Source: UniProtKB
    15. negative regulation of cardiac muscle cell proliferation Source: Ensembl
    16. neutrophil chemotaxis Source: UniProtKB
    17. regulation of immune response Source: Reactome
    18. single organismal cell-cell adhesion Source: Ensembl
    19. transepithelial transport Source: UniProtKB
    20. viral process Source: UniProtKB-KW

    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.

    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-SubCell
    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

    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.
    Mutagenesisi259 – 2602CC → AA: Loss of palmitoylation and altered localization.
    Mutagenesisi318 – 3181Y → A: Affects basolateral localization in airway epithelial cells. 1 Publication
    Mutagenesisi345 – 3484LSRM → AAAA: Affects basolateral localization in airway epithelial cells.

    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

    ArrayExpressiP78310.
    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. 12 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 – 3212
    Beta strandi37 – 393
    Beta strandi42 – 443
    Beta strandi53 – 619
    Beta strandi62 – 654
    Beta strandi68 – 758
    Beta strandi78 – 803
    Turni86 – 905
    Beta strandi91 – 933
    Helixi98 – 1003
    Beta strandi105 – 1073
    Helixi112 – 1143
    Beta strandi116 – 1249
    Beta strandi127 – 13812
    Beta strandi145 – 1484
    Beta strandi156 – 1638
    Beta strandi166 – 1683
    Beta strandi171 – 1788
    Helixi185 – 1928
    Beta strandi195 – 2017
    Beta strandi208 – 2158
    Beta strandi221 – 2277

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei238 – 25821HelicalSequence AnalysisAdd
    BLAST

    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.
    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

    MALLLCFVLL CGVVDFARSL SITTPEEMIE KAKGETAYLP CKFTLSPEDQ    50
    GPLDIEWLIS PADNQKVDQV IILYSGDKIY DDYYPDLKGR VHFTSNDLKS 100
    GDASINVTNL QLSDIGTYQC KVKKAPGVAN KKIHLVVLVK PSGARCYVDG 150
    SEEIGSDFKI KCEPKEGSLP LQYEWQKLSD SQKMPTSWLA EMTSSVISVK 200
    NASSEYSGTY SCTVRNRVGS DQCLLRLNVV PPSNKAGLIA GAIIGTLLAL 250
    ALIGLIIFCC RKKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS 300
    SLGSMSPSNM EGYSKTQYNQ VPSEDFERTP QSPTLPPAKV AAPNLSRMGA 350
    IPVMIPAQSK DGSIV 365
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 12 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.
    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

    ArrayExpressi P78310.
    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

    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: October 1, 2014
    This is version 154 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