P97792 (CXAR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coxsackievirus and adenovirus receptor homolog
Short name=CAR
Short name=mCAR

Gene names

Name:	Cxadr
Synonyms:	Car

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.3 Ref.6 In vitro, acts as a receptor for group B coxsackieviruses and subgroup C of adenoviruses (AD2 and AD5). Ref.2 Ref.3 Ref.6
Subunit structure	Monomer. Probably homodimer formed by 2 molecules on adjacent cells. Interacts with LNX, MPDZ, BAIAP1, DLG4, PRKCABP, TJP1 and CTNNB1 By similarity.
Subcellular location	Isoform 1: Cell membrane; Single-pass type I membrane protein By similarity. Cell junction › adherens junction By similarity. Cell junction › tight junction By similarity. Basolateral cell membrane; Single-pass type I membrane protein By similarity. Note: Localized at the intercellular contacts. 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 By similarity. Ref.6 Ref.8 Isoform 2: Cell membrane; Single-pass type I membrane protein By similarity. Cell junction › adherens junction By similarity. Cell junction › tight junction By similarity. Basolateral cell membrane; Single-pass type I membrane protein By similarity. Note: Localized at the intercellular contacts. 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 By similarity. Ref.6 Ref.8 Isoform 3: Secreted By similarity Ref.6 Ref.8.
Tissue specificity	Expressed in liver, kidney, heart, lung, and brain. In skeletal muscle is found at the neuromuscular junction. In cardiac muscle, isoform 1 and isoform 2 are found at intercalated disks. Ref.1 Ref.6 Ref.7 Ref.8
Developmental stage	Expression starts in the embryonic ectoderm in the uterus on E6.5. Then it is strongly expressed in the neuroepithelium of the neural tube, the developing brain and the spinal cord from E8.5 to postnatal day 7 (P7), in the cranial motor nerves from E9.5 to E11.5, and in the optic nerve from E13.5 to P7. Expression increases until perinatal period and decreases postnatally. Expressed in the immature neuroepithelium including progenitor cells it still occurs in a few proliferating cells of the hippocampal dentate gyrus, the subventricular zone of the lateral ventricles, and the rostral migratory stream over P21. Also expressed in heart, kidney and liver of newborn mice. Ref.6 Ref.7
Domain	The Ig-like C2-type 1 domain mediates homodimerization and interaction with AMICA1/JAML. The PDZ-binding motif mediates interaction with MPDZ and BAIAP1 By similarity.
Post-translational modification	Palmitoylated on Cys-259 and/or Cys-260; required for proper localization to the plasma membrane By similarity.
Sequence similarities	Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Membrane Secreted Tight junction
Coding sequence diversity	Alternative splicing
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	AV node cell to bundle of His cell communication Inferred from mutant phenotype PubMed 18636119. Source: UniProtKB actin cytoskeleton reorganization Inferred from sequence or structural similarity. Source: UniProtKB cardiac muscle fiber development Inferred from mutant phenotype PubMed 16079292. Source: MGI cell-cell junction organization Inferred from mutant phenotype PubMed 16543498. Source: MGI defense response to virus Inferred from electronic annotation. Source: Compara epithelial structure maintenance Inferred from sequence or structural similarity. Source: UniProtKB germ cell migration Inferred from expression pattern PubMed 17690169. Source: UniProtKB heterophilic cell-cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB homotypic cell-cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion organization Inferred from mutant phenotype PubMed 16079292. Source: MGI negative regulation of cardiac muscle cell proliferation Inferred from mutant phenotype PubMed 16543498. Source: MGI neutrophil chemotaxis Inferred from sequence or structural similarity. Source: UniProtKB transepithelial transport Inferred from electronic annotation. Source: Compara
Cellular_component	acrosomal vesicle Inferred from direct assay PubMed 16410001. Source: MGI adherens junction Inferred from sequence or structural similarity. Source: UniProtKB apicolateral plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB basolateral plasma membrane Inferred from direct assay PubMed 11316797PubMed 11316797. Source: UniProtKB cell body Inferred from direct assay Ref.6. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: Compara filopodium Inferred from direct assay Ref.6. Source: UniProtKB growth cone Inferred from direct assay Ref.6. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intercalated disc Inferred from direct assay PubMed 18636119. Source: UniProtKB membrane raft Inferred from sequence or structural similarity. Source: UniProtKB neuromuscular junction Inferred from electronic annotation. Source: Compara nucleus Inferred from sequence or structural similarity. Source: UniProtKB protein complex Inferred from electronic annotation. Source: Compara tight junction Inferred from direct assay PubMed 17690169PubMed 21269662. Source: UniProtKB
Molecular_function	PDZ domain binding Inferred from sequence or structural similarity. Source: UniProtKB cell adhesion molecule binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P97792-1)

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.

Isoform 2 (identifier: P97792-2)

The sequence of this isoform differs from the canonical sequence as follows:
     340-365: VAAPNLSRMGAVPVMIPAQSKDGSIV → FKYAYKTDGITVV

Isoform 3 (identifier: P97792-3)

The sequence of this isoform differs from the canonical sequence as follows:
     139-164: VKPSGTRCFVDGSEEIGNDFKLKCEP → GKSSFLLSTGVEWGGGAELQGGREGG
     165-365: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Potential

Chain

20 – 365

346

Coxsackievirus and adenovirus receptor homolog

PRO_0000014740

Regions

Topological domain

20 – 237

218

Extracellular Potential

Transmembrane

238 – 258

21

Helical; Potential

Topological domain

259 – 365

107

Cytoplasmic Potential

Domain

20 – 136

117

Ig-like C2-type 1

Domain

141 – 228

88

Ig-like C2-type 2

Motif

360 – 365

6

PDZ-binding By similarity

Amino acid modifications

Modified residue

293

1

Phosphoserine Ref.10

Modified residue

300

1

Phosphoserine Ref.10

Modified residue

306

1

Phosphoserine By similarity

Modified residue

323

1

Phosphoserine Ref.9

Modified residue

332

1

Phosphoserine By similarity

Lipidation

259

1

S-palmitoyl cysteine By similarity

Lipidation

260

1

S-palmitoyl cysteine By similarity

Glycosylation

106

1

N-linked (GlcNAc...) Ref.12

Disulfide bond

41 ↔ 120

Ref.11 Ref.12

Disulfide bond

146 ↔ 223

Ref.11 Ref.12

Disulfide bond

162 ↔ 212

Ref.11 Ref.12

Natural variations

Alternative sequence

139 – 164

26

VKPSG…LKCEP → GKSSFLLSTGVEWGGGAELQ GGREGG in isoform 3.

VSP_014827

Alternative sequence

165 – 365

201

Missing in isoform 3.

VSP_014828

Alternative sequence

340 – 365

26

VAAPN…DGSIV → FKYAYKTDGITVV in isoform 2.

VSP_014829

Secondary structure

1

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365

Helix Strand Turn

Details...

Beta strand

26 – 32

7

Beta strand

37 – 39

3

Beta strand

54 – 65

12

Beta strand

68 – 75

8

Beta strand

78 – 80

3

Helix

85 – 87

3

Turn

88 – 90

3

Beta strand

91 – 94

4

Helix

98 – 100

3

Beta strand

105 – 107

3

Helix

112 – 114

3

Beta strand

116 – 124

9

Beta strand

127 – 138

12

Beta strand

145 – 150

6

Beta strand

158 – 163

6

Beta strand

172 – 177

6

Helix

186 – 191

6

Beta strand

194 – 199

6

Helix

204 – 206

3

Beta strand

208 – 215

8

Beta strand

220 – 227

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 5445B4B52A34B2A2	FASTA	365	39,948
	10 20 30 40 50 60 MARLLCFVLL CGIADFTSGL SITTPEQRIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS 70 80 90 100 110 120 PSDNQIVDQV IILYSGDKIY DNYYPDLKGR VHFTSNDVKS GDASINVTNL QLSDIGTYQC 130 140 150 160 170 180 KVKKAPGVAN KKFLLTVLVK PSGTRCFVDG SEEIGNDFKL KCEPKEGSLP LQFEWQKLSD 190 200 210 220 230 240 SQTMPTPWLA EMTSPVISVK NASSEYSGTY SCTVQNRVGS DQCMLRLDVV PPSNRAGTIA 250 260 270 280 290 300 GAVIGTLLAL VLIGAILFCC HRKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS 310 320 330 340 350 360 SLGSMSPSNM EGYSKTQYNQ VPSEDFERAP QSPTLAPAKV AAPNLSRMGA VPVMIPAQSK DGSIV
	Isoform 2 [UniParc]. Checksum: 2BD8CBD25D8CE123	FASTA	352	38,843
	10 20 30 40 50 60 MARLLCFVLL CGIADFTSGL SITTPEQRIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS 70 80 90 100 110 120 PSDNQIVDQV IILYSGDKIY DNYYPDLKGR VHFTSNDVKS GDASINVTNL QLSDIGTYQC 130 140 150 160 170 180 KVKKAPGVAN KKFLLTVLVK PSGTRCFVDG SEEIGNDFKL KCEPKEGSLP LQFEWQKLSD 190 200 210 220 230 240 SQTMPTPWLA EMTSPVISVK NASSEYSGTY SCTVQNRVGS DQCMLRLDVV PPSNRAGTIA 250 260 270 280 290 300 GAVIGTLLAL VLIGAILFCC HRKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS 310 320 330 340 350 SLGSMSPSNM EGYSKTQYNQ VPSEDFERAP QSPTLAPAKF KYAYKTDGIT VV
	Isoform 3 [UniParc]. Checksum: 9DEFCBD456240C73	FASTA	164	17,781
	10 20 30 40 50 60 MARLLCFVLL CGIADFTSGL SITTPEQRIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS 70 80 90 100 110 120 PSDNQIVDQV IILYSGDKIY DNYYPDLKGR VHFTSNDVKS GDASINVTNL QLSDIGTYQC 130 140 150 160 KVKKAPGVAN KKFLLTVLGK SSFLLSTGVE WGGGAELQGG REGG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 2), TISSUE SPECIFICITY. Strain: C3H/Mai.
[2]	"Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5." Bergelson J.M., Cunningham J.A., Droguett G., Kurt-Jones E., Krithivas A., Hong J.S., Horwitz M.S., Crowell R.L., Finberg R.W. Science 275:1320-1323(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS A VIRUS RECEPTOR. Strain: C57BL/6J. Tissue: Colon and Liver.
[3]	"The murine CAR homolog is a receptor for coxsackie B viruses and adenoviruses." Bergelson J.M., Krithivas A., Celi L., Droguett G., Horwitz M.S., Wickham T., Crowell R.L., Finberg R.W. J. Virol. 72:415-419(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION AS A VIRUS RECEPTOR. Strain: C57BL/6J. Tissue: Liver.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Liver.
[5]	"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] (ISOFORMS 2 AND 3). Strain: FVB/N. Tissue: Mammary gland.
[6]	"The coxsackievirus-adenovirus receptor protein as a cell adhesion molecule in the developing mouse brain." Honda T., Saitoh H., Masuko M., Katagiri-Abe T., Tominaga K., Kozakai I., Kobayashi K., Kumanishi T., Watanabe Y.G., Odani S., Kuwano R. Brain Res. Mol. Brain Res. 77:19-28(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, GLYCOSYLATION, FUNCTION.
[7]	"Developmental distribution of coxsackie virus and adenovirus receptor localized in the nervous system." Hotta Y., Honda T., Naito M., Kuwano R. Brain Res. Dev. Brain Res. 143:1-13(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]	"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.
[9]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, MASS SPECTROMETRY. Tissue: Liver.
[10]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-300, MASS SPECTROMETRY. Tissue: Liver.
[11]	"The coxsackievirus-adenovirus receptor reveals complex homophilic and heterophilic interactions on neural cells." Patzke C., Max K.E., Behlke J., Schreiber J., Schmidt H., Dorner A.A., Kroger S., Henning M., Otto A., Heinemann U., Rathjen F.G. J. Neurosci. 30:2897-2910(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 20-233, DISULFIDE BONDS.
[12]	"The molecular interaction of CAR and JAML recruits the central cell signal transducer PI3K." Verdino P., Witherden D.A., Havran W.L., Wilson I.A. Science 329:1210-1214(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-236 IN COMPLEX WITH AMICA1/JAML, DISULFIDE BONDS, GLYCOSYLATION AT ASN-106.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U90715 mRNA. Translation: AAC53148.1.
Y10320 mRNA. Translation: CAA71368.1.
Y11929 mRNA. Translation: CAA72679.1.
AK004908 mRNA. Translation: BAB23660.2.
AK145569 mRNA. Translation: BAE26518.1.
BC004680 mRNA. Translation: AAH04680.1.
BC016457 mRNA. Translation: AAH16457.1.

IPI

IPI00270376.
IPI00271453.
IPI00474948.

RefSeq

NP_001020363.1. NM_001025192.3.
NP_001263192.1. NM_001276263.1.
NP_034118.1. NM_009988.4.

UniGene

Mm.66222.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3JZ7	X-ray	2.19	A	20-233	[»]
3MJ7	X-ray	2.80	B	18-236	[»]

ProteinModelPortal

P97792.

SMR

P97792. Positions 25-233.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41457N.

MINT

MINT-253068.

PTM databases

PhosphoSite

P97792.

Proteomic databases

PaxDb

P97792.

PRIDE

P97792.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000023572; ENSMUSP00000023572; ENSMUSG00000022865.
ENSMUST00000114229; ENSMUSP00000109867; ENSMUSG00000022865.

GeneID

13052.

KEGG

mmu:13052.

UCSC

uc007zsm.1. mouse.
uc007zsn.1. mouse.
uc007zso.1. mouse.

Organism-specific databases

CTD

1525.

MGI

MGI:1201679. Cxadr.

Phylogenomic databases

eggNOG

NOG83644.

GeneTree

ENSGT00680000099635.

HOGENOM

HOG000111222.

HOVERGEN

HBG105787.

InParanoid

P97792.

KO

K06788.

OMA

EDFERAP.

OrthoDB

EOG4894MW.

Gene expression databases

Bgee

P97792.

CleanEx

MM_CXADR.

Genevestigator

P97792.

GermOnline

ENSMUSG00000022865. Mus musculus.

Family and domain databases

Gene3D

2.60.40.10. 2 hits.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]

Pfam

PF07686. V-set. 1 hit.
[Graphical view]

SMART

SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CXADR. mouse.

EvolutionaryTrace

P97792.

NextBio

282970.

SOURCE

Search...

Entry information

Entry name

CXAR_MOUSE

Accession

Primary (citable) accession number: P97792
Secondary accession number(s): O09052 , Q3ULD0, Q91W66, Q99KG0, Q9DBJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1997
Last modified:	April 3, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program