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Coxsackievirus and adenovirus receptor homolog (CAR)

 CXAR_PONAB              Reviewed;         365 AA.
Q5R764;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
25-OCT-2017, entry version 88.
RecName: Full=Coxsackievirus and adenovirus receptor homolog;
Short=CAR;
Flags: Precursor;
Name=CXADR; Synonyms=CAR;
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Component of the epithelial apical junction complex that
may function as a homophilic cell adhesion molecule and is
essential for tight junction integrity. Also involved in
transepithelial migration of leukocytes through adhesive
interactions with JAML a transmembrane protein of the plasma
membrane of leukocytes. The interaction between both receptors
also mediates the activation of gamma-delta T-cells, a
subpopulation of T-cells residing in epithelia and involved in
tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML
induces downstream cell signaling events in gamma-delta T-cells
through PI3-kinase and MAP kinases. It results in proliferation
and production of cytokines and growth factors by T-cells that in
turn stimulate epithelial tissues repair (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Monomer. May form homodimer. Interacts with LNX, BAIAP1,
DLG4, PRKCABP, TJP1 and CTNNB1. Interacts with MPDZ; recruits MPDZ
to intercellular contact sites. Interacts with JAML (homodimeric
form) (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane
protein {ECO:0000255}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane
protein {ECO:0000255}. Cell junction, tight junction
{ECO:0000250|UniProtKB:P78310}. Cell junction, adherens junction
{ECO:0000250|UniProtKB:P78310}. Note=In epithelial cells localizes
to the apical junction complex composed of tight and adherens
junctions. In airway epithelial cells localized to basolateral
membrane but not to apical surface.
{ECO:0000250|UniProtKB:P78310}.
-!- DOMAIN: The Ig-like C2-type 1 domain mediates homodimerization and
interaction with JAML. {ECO:0000250}.
-!- DOMAIN: The PDZ-binding motif mediates interaction with MPDZ and
BAIAP1. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: Palmitoylated on Cys-259 and/or Cys-260; required for proper
localization to the plasma membrane. {ECO:0000250}.
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EMBL; CR860254; CAH92396.1; -; mRNA.
RefSeq; NP_001127547.1; NM_001134075.1.
ProteinModelPortal; Q5R764; -.
SMR; Q5R764; -.
STRING; 9601.ENSPPYP00000012617; -.
GeneID; 100174624; -.
KEGG; pon:100174624; -.
CTD; 1525; -.
eggNOG; ENOG410IGDG; Eukaryota.
eggNOG; ENOG4110WP1; LUCA.
HOVERGEN; HBG105787; -.
InParanoid; Q5R764; -.
KO; K06788; -.
Proteomes; UP000001595; Unplaced.
GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
GO; GO:0016327; C:apicolateral plasma membrane; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
GO; GO:0044297; C:cell body; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030175; C:filopodium; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
GO; GO:0071253; F:connexin binding; ISS:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0086067; P:AV node cell to bundle of His cell communication; ISS:UniProtKB.
GO; GO:0048739; P:cardiac muscle fiber development; ISS:UniProtKB.
GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
GO; GO:0046629; P:gamma-delta T cell activation; ISS:UniProtKB.
GO; GO:0008354; P:germ cell migration; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
GO; GO:0034109; P:homotypic cell-cell adhesion; ISS:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR013151; Immunoglobulin.
Pfam; PF00047; ig; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 2.
SMART; SM00408; IGc2; 2.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
2: Evidence at transcript level;
Cell adhesion; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Lipoprotein;
Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
Repeat; Signal; Tight junction; Transmembrane; Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 365 Coxsackievirus and adenovirus receptor
homolog.
/FTId=PRO_0000014741.
TOPO_DOM 20 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
TOPO_DOM 259 365 Cytoplasmic. {ECO:0000255}.
DOMAIN 20 134 Ig-like C2-type 1.
DOMAIN 141 228 Ig-like C2-type 2.
MOTIF 360 365 PDZ-binding. {ECO:0000250}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000250|UniProtKB:P97792}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000250|UniProtKB:P97792}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000250|UniProtKB:P78310}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000250|UniProtKB:P78310}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000250|UniProtKB:P78310}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000250|UniProtKB:P97792}.
LIPID 259 259 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 260 260 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 120 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 146 223 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 162 212 {ECO:0000255|PROSITE-ProRule:PRU00114}.
SEQUENCE 365 AA; 40030 MW; AB01C6346CB7FE64 CRC64;
MALLLCFVLL CGVVDFARSL SITTPEEMIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS
PADNQKVDQV IILYSGDKIY DDYYPDLKGR VHFTSNDLKS GDASINVTNL QLSDIGTYQC
KVKKAPGVAN KKIHLVVLVK PSGARCYVDG SEEIGSDFKI KCEPKEGSLP LQYEWQKLSD
SQKMPTSWLA EMTSSVISVK NASSEYSGTY SCTVRNRVGS DQCLLRLNVV PPSNKAGLIA
GAIIGTLLAL ALIGLIIFCC RKKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS
SLGSMSPSNM EGYSKTQYNQ VPSEDFERTP QSPTLPPAKV AAPNLSRMGA IPVMIPAQSK
DGSIV


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