CXAR_PONAB
ID CXAR_PONAB Reviewed; 365 AA.
AC Q5R764;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Coxsackievirus and adenovirus receptor homolog;
DE Short=CAR;
DE Flags: Precursor;
GN Name=CXADR; Synonyms=CAR;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the epithelial apical junction complex that may
CC function as a homophilic cell adhesion molecule and is essential for
CC tight junction integrity. Also involved in transepithelial migration of
CC leukocytes through adhesive interactions with JAML a transmembrane
CC protein of the plasma membrane of leukocytes. The interaction between
CC both receptors also mediates the activation of gamma-delta T-cells, a
CC subpopulation of T-cells residing in epithelia and involved in tissue
CC homeostasis and repair. Upon epithelial CXADR-binding, JAML induces
CC downstream cell signaling events in gamma-delta T-cells through PI3-
CC kinase and MAP kinases. It results in proliferation and production of
CC cytokines and growth factors by T-cells that in turn stimulate
CC epithelial tissues repair (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. May form homodimer. Interacts with LNX, MAGI1, DLG4,
CC PRKCABP, TJP1 and CTNNB1. Interacts with MPDZ; recruits MPDZ to
CC intercellular contact sites. Interacts with JAML (homodimeric form) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P78310};
CC Single-pass type I membrane protein {ECO:0000255}. Basolateral cell
CC membrane {ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane
CC protein {ECO:0000255}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:P78310}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:P78310}. Note=In epithelial cells localizes to
CC the apical junction complex composed of tight and adherens junctions.
CC In airway epithelial cells localized to basolateral membrane but not to
CC apical surface. {ECO:0000250|UniProtKB:P78310}.
CC -!- DOMAIN: The Ig-like C2-type 1 domain mediates homodimerization and
CC interaction with JAML. {ECO:0000250}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with MPDZ and MAGI1.
CC {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Palmitoylated on Cys-259 and/or Cys-260; required for proper
CC localization to the plasma membrane. {ECO:0000250}.
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DR EMBL; CR860254; CAH92396.1; -; mRNA.
DR RefSeq; NP_001127547.1; NM_001134075.1.
DR AlphaFoldDB; Q5R764; -.
DR BMRB; Q5R764; -.
DR SMR; Q5R764; -.
DR STRING; 9601.ENSPPYP00000012617; -.
DR GeneID; 100174624; -.
DR KEGG; pon:100174624; -.
DR CTD; 1525; -.
DR eggNOG; ENOG502QSG0; Eukaryota.
DR InParanoid; Q5R764; -.
DR OrthoDB; 896005at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0071253; F:connexin binding; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0086067; P:AV node cell to bundle of His cell communication; ISS:UniProtKB.
DR GO; GO:0055013; P:cardiac muscle cell development; ISS:UniProtKB.
DR GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
DR GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0046629; P:gamma-delta T cell activation; ISS:UniProtKB.
DR GO; GO:0008354; P:germ cell migration; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Tight junction;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..365
FT /note="Coxsackievirus and adenovirus receptor homolog"
FT /id="PRO_0000014741"
FT TOPO_DOM 20..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..134
FT /note="Ig-like C2-type 1"
FT DOMAIN 141..228
FT /note="Ig-like C2-type 2"
FT REGION 269..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 360..365
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 269..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97792"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97792"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78310"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78310"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78310"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97792"
FT LIPID 259
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 260
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 146..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 162..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ 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
