CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010682
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Coxsackievirus and adenovirus receptor homolog 
Protein Synonyms/Alias
 CAR; mCAR 
Gene Name
 Cxadr 
Gene Synonyms/Alias
 Car 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
271RREEKYEKEVHHDIRubiquitination[1]
315SNMEGYSKTQYNQVPubiquitination[1]
339SPTLAPAKVAAPNLSubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Component of the epithelial apical junction complex that is essential for the tight junction integrity. Proposed to function as a homophilic cell adhesion molecule. Recruits MPDZ to intercellular contact sites. Probably involved in transepithelial migration of polymorphonuclear leukocytes (PMN) through adhesive interactions with AMICA1/JAML located in the plasma membrane of PMN (By similarity). 
Sequence Annotation
 DOMAIN 20 136 Ig-like C2-type 1.
 DOMAIN 141 228 Ig-like C2-type 2.
 MOTIF 360 365 PDZ-binding (By similarity).
 MOD_RES 293 293 Phosphoserine.
 MOD_RES 300 300 Phosphoserine.
 MOD_RES 306 306 Phosphoserine (By similarity).
 MOD_RES 323 323 Phosphoserine.
 MOD_RES 332 332 Phosphoserine (By similarity).
 LIPID 259 259 S-palmitoyl cysteine (By similarity).
 LIPID 260 260 S-palmitoyl cysteine (By similarity).
 CARBOHYD 106 106 N-linked (GlcNAc...).
 DISULFID 41 120
 DISULFID 146 223
 DISULFID 162 212  
Keyword
 3D-structure; Alternative splicing; Cell adhesion; Cell junction; Cell membrane; Complete proteome; Disulfide bond; Glycoprotein; Immunoglobulin domain; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted; Signal; Tight junction; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 365 AA 
Protein Sequence
MARLLCFVLL CGIADFTSGL SITTPEQRIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS 60
PSDNQIVDQV IILYSGDKIY DNYYPDLKGR VHFTSNDVKS GDASINVTNL QLSDIGTYQC 120
KVKKAPGVAN KKFLLTVLVK PSGTRCFVDG SEEIGNDFKL KCEPKEGSLP LQFEWQKLSD 180
SQTMPTPWLA EMTSPVISVK NASSEYSGTY SCTVQNRVGS DQCMLRLDVV PPSNRAGTIA 240
GAVIGTLLAL VLIGAILFCC HRKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS 300
SLGSMSPSNM EGYSKTQYNQ VPSEDFERAP QSPTLAPAKV AAPNLSRMGA VPVMIPAQSK 360
DGSIV 365 
Gene Ontology
 GO:0001669; C:acrosomal vesicle; IDA:MGI.
 GO:0005912; C:adherens junction; ISS:UniProtKB.
 GO:0016327; C:apicolateral plasma membrane; ISS:UniProtKB.
 GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
 GO:0044297; C:cell body; IDA:UniProtKB.
 GO:0005615; C:extracellular space; IEA:Compara.
 GO:0030175; C:filopodium; IDA:UniProtKB.
 GO:0030426; C:growth cone; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0014704; C:intercalated disc; IDA:UniProtKB.
 GO:0045121; C:membrane raft; ISS:UniProtKB.
 GO:0031594; C:neuromuscular junction; IEA:Compara.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0005923; C:tight junction; IDA:UniProtKB.
 GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
 GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
 GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
 GO:0086067; P:AV node cell to bundle of His cell communication; IMP:UniProtKB.
 GO:0048739; P:cardiac muscle fiber development; IMP:MGI.
 GO:0045216; P:cell-cell junction organization; IMP:MGI.
 GO:0051607; P:defense response to virus; IEA:Compara.
 GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
 GO:0008354; P:germ cell migration; IEP:UniProtKB.
 GO:0007157; P:heterophilic cell-cell adhesion; ISS:UniProtKB.
 GO:0034109; P:homotypic cell-cell adhesion; ISS:UniProtKB.
 GO:0007005; P:mitochondrion organization; IMP:MGI.
 GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:MGI.
 GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
 GO:0070633; P:transepithelial transport; IEA:Compara. 
Interpro
 IPR007110; Ig-like_dom.
 IPR013783; Ig-like_fold.
 IPR003599; Ig_sub.
 IPR003598; Ig_sub2.
 IPR013106; Ig_V-set. 
Pfam
 PF07686; V-set 
SMART
 SM00409; IG
 SM00408; IGc2 
PROSITE
 PS50835; IG_LIKE 
PRINTS