Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00517
Entry Name
UniProt Accession
Theoretical PI
6.94
Molecular Weight
39948.61
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Coxsackievirus and adenovirus receptor homolog
Protein Synonyms/Alias
CAR; rCAR;
Gene Name
Cxadr
Gene Synonyms/Alias
Car;
Created Date
19-JUL-2005
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
6
Canonical
**MALLLCFVLLCGV
[1]
S-Palmitoylation
259
Canonical
LIGAILFCCHKKRRE
[1]
S-Palmitoylation
260
Canonical
IGAILFCCHKKRREE
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Predicted from GPS-Lipid
Functional Description
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 (By similarity).
Sequence Annotation
Topological domain: 20 238 Extracellular.
Transmembrane: 239 259 Helical.
Topological domain: 260 365 Cytoplasmic.
Domain: 20 136 Ig-like C2-type 1.
Domain: 141 228 Ig-like C2-type 2.
Motif: 360 365 PDZ-binding.
Modified residue: 306 306 Phosphoserine.
Modified residue: 323 323 Phosphoserine.
Modified residue: 332 332 Phosphoserine.
Protein Length
365 AA.
Protein Sequence
(Canonical)
MALLLCFVLL CGVADFTSSL SITTPEQRIE KAKGETAYLP CKFTLEPEDQ GPLDIEWLIS  60
PSDNQKVDQV IILYSGDKIY DNYYPDLKGR VHFTSNDVKS GDASINVTNL QLSDIGTYQC  120
KVKKAPGVAN RKFLLTVLVK PSGTRCFVDG SGEIGNDFKL KCEPKEGSLP LQYEWQKLSD  180
SQKMPTPWLA EMTSPVISVK NASSEYSGTY SCTVQNRVGS DQCMLRLDVV PPSNRAGTIA  240
GAVIGTLLAL VLIGAILFCC HKKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS  300
SLGSMSPSNM EGYSKTQYNQ VPSEDFERAP QSPTLAPAKV AAPNLSRMGA VPVMIPAQSK  360
DGSIV                                                              365
FASTA
(Canonical)
>LipidDB-10116-00517|Q9R066
MALLLCFVLLCGVADFTSSLSITTPEQRIEKAKGETAYLPCKFTLEPEDQGPLDIEWLIS
PSDNQKVDQVIILYSGDKIYDNYYPDLKGRVHFTSNDVKSGDASINVTNLQLSDIGTYQC
KVKKAPGVANRKFLLTVLVKPSGTRCFVDGSGEIGNDFKLKCEPKEGSLPLQYEWQKLSD
SQKMPTPWLAEMTSPVISVKNASSEYSGTYSCTVQNRVGSDQCMLRLDVVPPSNRAGTIA
GAVIGTLLALVLIGAILFCCHKKRREEKYEKEVHHDIREDVPPPKSRTSTARSYIGSNHS
SLGSMSPSNMEGYSKTQYNQVPSEDFERAPQSPTLAPAKVAAPNLSRMGAVPVMIPAQSK
DGSIV
Gene Ontology
GO:0001669; C:acrosomal vesicle; ISS:UniProtKB
GO:0005912; C:adherens junction; ISS:UniProtKB
GO:0016327; C:apicolateral plasma membrane; ISS:UniProtKB
GO:0044297; C:cell body; ISS:UniProtKB
GO:0005737; C:cytoplasm; ISS:UniProtKB
GO:0030175; C:filopodium; ISS:UniProtKB
GO:0030426; C:growth cone; ISS:UniProtKB
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0014704; C:intercalated disc; IEA:Ensembl
GO:0045121; C:membrane raft; ISS:UniProtKB
GO:0043005; C:neuron projection; IDA:UniProtKB
GO:0005634; C:nucleus; ISS:UniProtKB
GO:0005886; C:plasma membrane; ISS:UniProtKB
GO:0005923; C:tight junction; IDA:UniProtKB
GO:0008013; F:beta-catenin binding; ISS:UniProtKB
GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB
GO:0071253; F:connexin binding; ISS:UniProtKB
GO:0030165; F:PDZ domain binding; ISS:UniProtKB
GO:0001618; F:virus receptor activity; TAS:RGD
GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB
GO:0086067; P:AV node cell to bundle of His cell communication; ISS:UniProtKB
GO:0048739; P:cardiac muscle fiber development; ISS:UniProtKB
GO:0045216; P:cell-cell junction organization; ISS:UniProtKB
GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB
GO:0046629; P:gamma-delta T cell activation; ISS:UniProtKB
GO:0008354; P:germ cell migration; ISS:UniProtKB
GO:0007507; P:heart development; ISS:UniProtKB
GO:0007157; P:heterophilic cell-cell adhesion; ISS:UniProtKB
GO:0034109; P:homotypic cell-cell adhesion; ISS:UniProtKB
GO:0007005; P:mitochondrion organization; ISS:UniProtKB
GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl
GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB
GO:0009615; P:response to virus; TAS:GOC
Interpro
InterPro; IPR007110; Ig-like_dom
InterPro; IPR013783; Ig-like_fold
InterPro; IPR003599; Ig_sub
InterPro; IPR003598; Ig_sub2
InterPro; IPR013106; Ig_V-set
Pfam
Pfam; PF07686; V-set;
SMART
SMART; SM00409; IG;
SMART; SM00408; IGc2;
PROSITE
PROSITE; PS50835; IG_LIKE;
PRINTS