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Q8R5M8 (CADM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell adhesion molecule 1
Alternative name(s):
Immunoglobulin superfamily member 4
Short name=IgSF4
Nectin-like protein 2
Short name=NECL-2
Spermatogenic immunoglobulin superfamily
Short name=SgIgSF
Synaptic cell adhesion molecule
Short name=SynCAM
Tumor suppressor in lung cancer 1
Short name=TSLC-1
Gene names
Name:Cadm1
Synonyms:Igsf4, Necl2, Ra175, Syncam, SynCam1, Tslc1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates homophilic cell-cell adhesion in a Ca2+-independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and PVRL3 in a Ca2+-independent manner. Acts as a tumor suppressor in non-small-cell lung cancer (NSCLC) cells. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. May contribute to the less invasive phenotypes of lepidic growth tumor cells. In mast cells, may mediate attachment to and promote communication with nerves. CADM1, together with MITF, is essential for development and survival of mast cells in vivo. May act as a synaptic cell adhesion molecule that drives synapse assembly. May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa. Ref.2 Ref.3 Ref.4 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16 UniProtKB Q9BY67

Subunit structure

Homodimer. Interacts with CRTAM and EPB41L3/DAL1. The interaction with EPB41L3/DAL1 may act to anchor CADM1 to the actin cytoskeleton. Interacts via its C-terminus with the PDZ domain of MPP3 and the PDZ domain of MPP6. Ref.4 Ref.10 Ref.12 UniProtKB Q9BY67

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cell junction › synapse. Note: Associates with perinuclear and plasma membranes in vivo. Localized to the basolateral plasma membrane of epithelial cells in gall bladder. Ref.4 Ref.20 UniProtKB Q9BY67

Tissue specificity

Expressed in brain, lung, kidney, testis, heart, spleen and liver, but not expressed in skeletal muscle. In brain, enriched in the synaptic plasma membrane. Expressed dominantly in epithelial cells but not expressed in fibroblast cells (at protein level). Ref.1 Ref.2 Ref.4 Ref.8

Developmental stage

Expressed in spermatogenic cells during early spermatogenesis. Expression increases in intermediate spermatogonia through to zygotene spermatocytes but becomes diminished in the steps from early pachytene spermatocytes through to round spermatids. After meiosis, expression reappears in spermatids and is present in elongating spermatids until spermiation. Not detected in Sertoli cells. Ref.8

Domain

The cytoplasmic domain appears to play a critical role in proapoptosis and tumor suppressor activity in NSCLC By similarity. UniProtKB Q9BY67

Post-translational modification

N-glycosylated. Ref.8 Ref.20

Glycosylation at Asn-70 and Asn-104 promotes adhesive binding and synapse induction By similarity.

Disruption phenotype

Male mice are infertile, due to a defect at the spermatid stage of spermatogenesis, and show oligoasthenoteratozoospermia with almost no mature motile spermatozoa in the epididymis. Heterozygous males and females and homozygous null females are fertile and have no overt developmental defects. Ref.14 Ref.15 Ref.16

Sequence similarities

Belongs to the nectin family.

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Sequence caution

The sequence AAC67243.1 differs from that shown. Reason: Frameshift at position 65.

Ontologies

Keywords
   Biological processApoptosis
Cell adhesion
Differentiation
Immunity
Spermatogenesis
   Cellular componentCell junction
Cell membrane
Membrane
Synapse
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

bone development

Inferred from mutant phenotype PubMed 22876197. Source: MGI

brain development

Inferred from electronic annotation. Source: Compara

calcium-independent cell-cell adhesion

Inferred from direct assay Ref.2. Source: MGI

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cell recognition

Inferred from direct assay Ref.10. Source: UniProtKB

detection of stimulus

Inferred from direct assay Ref.10. Source: UniProtKB

heterophilic cell-cell adhesion

Inferred from direct assay Ref.4. Source: UniProtKB

homophilic cell adhesion

Inferred from direct assay Ref.4. Source: UniProtKB

liver development

Inferred from electronic annotation. Source: Compara

positive regulation of cytokine secretion

Inferred from electronic annotation. Source: Compara

spermatogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

susceptibility to natural killer cell mediated cytotoxicity

Inferred from direct assay Ref.10. Source: UniProtKB

synapse assembly

Inferred from direct assay Ref.2. Source: MGI

unidimensional cell growth

Inferred from mutant phenotype PubMed 18055550. Source: MGI

   Cellular_componentaxon

Inferred from direct assay Ref.11. Source: MGI

basolateral plasma membrane

Inferred from direct assay Ref.4. Source: UniProtKB

cell-cell junction

Inferred from direct assay Ref.4. Source: UniProtKB

dendrite

Inferred from direct assay Ref.11. Source: MGI

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

synaptic vesicle

Inferred from direct assay Ref.2. Source: MGI

   Molecular_functionprotein homodimerization activity

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ITGB4P161443EBI-5651941,EBI-948678From a different organism.

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.3 (identifier: Q8R5M8-1)

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 Ref.1 Ref.2 Ref.5 Ref.7 (identifier: Q8R5M8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     364-374: Missing.
Isoform 3 Ref.7 (identifier: Q8R5M8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     336-363: Missing.
Isoform 4 Ref.4 Ref.7 (identifier: Q8R5M8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     336-374: Missing.
Isoform 5 Ref.6 Ref.7 (identifier: Q8R5M8-5)

The sequence of this isoform differs from the canonical sequence as follows:
     335-336: DP → GT
     337-456: Missing.
Isoform 6 Ref.3 (identifier: Q8R5M8-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-150: Missing.
     355-365: Missing.
Isoform 7 Ref.3 (identifier: Q8R5M8-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-150: Missing.
     336-352: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4747 Potential
Chain48 – 456409Cell adhesion molecule 1
PRO_0000291969

Regions

Topological domain48 – 388341Extracellular Potential
Transmembrane389 – 40921Helical; Potential
Topological domain410 – 45647Cytoplasmic Potential
Domain48 – 14295Ig-like V-type
Domain147 – 24195Ig-like C2-type 1
Domain246 – 33287Ig-like C2-type 2

Amino acid modifications

Modified residue4481Phosphoserine Ref.17
Glycosylation701N-linked (GlcNAc...) Ref.19 Ref.20
Glycosylation1041N-linked (GlcNAc...) Ref.18 Ref.19 Ref.20
Glycosylation1161N-linked (GlcNAc...) Ref.18 Ref.19
Glycosylation1681N-linked (GlcNAc...) Ref.19
Glycosylation3041N-linked (GlcNAc...) Ref.19
Glycosylation3071N-linked (GlcNAc...) Ref.19
Glycosylation3111N-linked (GlcNAc...) Ref.19
Disulfide bond67 ↔ 127 By similarity
Disulfide bond169 ↔ 223 By similarity
Disulfide bond270 ↔ 316 By similarity

Natural variations

Alternative sequence1 – 150150Missing in isoform 6 and isoform 7. Ref.6 Ref.7
VSP_052463
Alternative sequence335 – 3362DP → GT in isoform 5. Ref.5
VSP_052464
Alternative sequence336 – 37439Missing in isoform 4. Ref.4 Ref.7
VSP_052465
Alternative sequence336 – 36328Missing in isoform 3. Ref.3
VSP_052466
Alternative sequence336 – 35217Missing in isoform 7. Ref.7
VSP_052467
Alternative sequence337 – 456120Missing in isoform 5. Ref.5
VSP_052468
Alternative sequence355 – 36511Missing in isoform 6. Ref.6
VSP_052469
Alternative sequence364 – 37411Missing in isoform 2. Ref.1 Ref.2 Ref.5 Ref.7
VSP_052470

Experimental info

Sequence conflict81S → C in AAN01614. Ref.2
Sequence conflict81S → C in BAD30018. Ref.7
Sequence conflict2661F → L in BAA87914. Ref.3
Sequence conflict2661F → L in BAA87915. Ref.3
Sequence conflict3151R → P in BAA87914. Ref.3
Sequence conflict3151R → P in BAA87915. Ref.3
Sequence conflict3301M → I in BAA87914. Ref.3
Sequence conflict3301M → I in BAA87915. Ref.3
Sequence conflict3561T → S in AAN01614. Ref.2
Sequence conflict3561T → S in BAD30018. Ref.7
Sequence conflict4291D → N in BAB83501. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: 3226E86C04161C7F

FASTA45649,788
        10         20         30         40         50         60 
MASAVLPSGS QCAAAAAVAA AAAPPGLRLR LLLLLLSAAA LIPTGDGQNL FTKDVTVIEG 

        70         80         90        100        110        120 
EVATISCQVN KSDDSVIQLL NPNRQTIYFR DFRPLKDSRF QLLNFSSSEL KVSLTNVSIS 

       130        140        150        160        170        180 
DEGRYFCQLY TDPPQESYTT ITVLVPPRNL MIDIQKDTAV EGEEIEVNCT AMASKPATTI 

       190        200        210        220        230        240 
RWFKGNKELK GKSEVEEWSD MYTVTSQLML KVHKEDDGVP VICQVEHPAV TGNLQTQRYL 

       250        260        270        280        290        300 
EVQYKPQVHI QMTYPLQGLT REGDAFELTC EAIGKPQPVM VTWVRVDDEM PQHAVLSGPN 

       310        320        330        340        350        360 
LFINNLNKTD NGTYRCEASN IVGKAHSDYM LYVYDPPTTI PPPTTTTTTT TTTTTTILTI 

       370        380        390        400        410        420 
ITDTTATTEP AVHDSRAGEE GTIGAVDHAV IGGVVAVVVF AMLCLLIILG RYFARHKGTY 

       430        440        450 
FTHEAKGADD AADADTAIIN AEGGQNNSEE KKEYFI

« Hide

Isoform 2 [UniParc].

Checksum: C5D5A070DAF70E55
Show »

FASTA44548,664
Isoform 3 [UniParc].

Checksum: B10DFF1A2B893573
Show »

FASTA42846,903
Isoform 4 [UniParc].

Checksum: 98500180D37845C2
Show »

FASTA41745,779
Isoform 5 [UniParc].

Checksum: 9EF3D8B8BE5E8F72
Show »

FASTA33637,155
Isoform 6 [UniParc].

Checksum: F557E3FAF8174671
Show »

FASTA29532,459
Isoform 7 [UniParc].

Checksum: FC718DBCCEA8C452
Show »

FASTA28931,922

References

« Hide 'large scale' references
[1]"Identification of the Tslc1 gene, a mouse orthologue of the human tumor suppressor TSLC1 gene."
Fukami T., Satoh H., Fujita E., Maruyama T., Fukuhara H., Kuramochi M., Takamoto S., Momoi T., Murakami Y.
Gene 295:7-12(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
Strain: 129/SvJ.
[2]"SynCAM, a synaptic adhesion molecule that drives synapse assembly."
Biederer T., Sara Y., Mozhayeva M., Atasoy D., Liu X., Kavalali E.T., Sudhof T.C.
Science 297:1525-1531(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
Strain: C57BL/6.
[3]"RA175, which is the mouse ortholog of TSLC1, a tumor suppressor gene in human lung cancer, is a cell adhesion molecule."
Fujita E., Soyama A., Momoi T.
Exp. Cell Res. 287:57-66(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6 AND 7), FUNCTION.
Tissue: Embryonic carcinoma.
[4]"Implications of nectin-like molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and transmembrane protein localization in epithelial cells."
Shingai T., Ikeda W., Kakunaga S., Morimoto K., Takekuni K., Itoh S., Satoh K., Takeuchi M., Imai T., Monden M., Takai Y.
J. Biol. Chem. 278:35421-35427(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH MPP6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Brain.
[5]"Nectin-like molecule 1 is a protein 4.1N associated protein and recruits protein 4.1N from cytoplasm to the plasma membrane."
Zhou Y., Du G., Hu X., Yu S., Liu Y., Xu Y., Huang X., Liu J., Yin B., Fan M., Peng X., Qiang B., Yuan J.
Biochim. Biophys. Acta 1669:142-154(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-456 (ISOFORM 2).
[6]"A secretion form of SgIGSF/TSLC1."
Ito A., Koma Y., Nagano T.
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Strain: C57BL/6.
Tissue: Mast cell.
[7]"Neuron-specific isoforms of RA175/TSLC1/SynCAM."
Fujita E., Aikawa K., Momoi T.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
[8]"Expression and functional characterization of the adhesion molecule spermatogenic immunoglobulin superfamily in the mouse testis."
Wakayama T., Koami H., Ariga H., Kobayashi D., Sai Y., Tsuji A., Yamamoto M., Iseki S.
Biol. Reprod. 68:1755-1763(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION.
[9]"Contribution of the SgIGSF adhesion molecule to survival of cultured mast cells in vivo."
Ito A., Koma Y., Watabe K., Jippo T., Wakayama T., Iseki S., Kitamura Y.
Biochem. Biophys. Res. Commun. 319:200-206(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell responses through the cell-surface receptor CRTAM."
Boles K.S., Barchet W., Diacovo T., Cella M., Colonna M.
Blood 106:779-786(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CADM1.
[11]"Distribution of RA175/TSLC1/SynCAM, a member of the immunoglobulin superfamily, in the developing nervous system."
Fujita E., Urase K., Soyama A., Kouroku Y., Momoi T.
Brain Res. Dev. Brain Res. 154:199-209(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Nectin-like protein 2 defines a subset of T-cell zone dendritic cells and is a ligand for class-I-restricted T-cell-associated molecule."
Galibert L., Diemer G.S., Liu Z., Johnson R.S., Smith J.L., Walzer T., Comeau M.R., Rauch C.T., Wolfson M.F., Sorensen R.A., Van der Vuurst de Vries A.-R., Branstetter D.G., Koelling R.M., Scholler J., Fanslow W.C., Baum P.R., Derry J.M., Yan W.
J. Biol. Chem. 280:21955-21964(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRTAM.
[13]"MITF and SgIGSF: an essential transcription factor and its target adhesion molecule for development and survival of mast cells."
Kitamura Y.
Novartis Found. Symp. 271:4-11(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Oligo-astheno-teratozoospermia in mice lacking RA175/TSLC1/SynCAM/IGSF4A, a cell adhesion molecule in the immunoglobulin superfamily."
Fujita E., Kouroku Y., Ozeki S., Tanabe Y., Toyama Y., Maekawa M., Kojima N., Senoo H., Toshimori K., Momoi T.
Mol. Cell. Biol. 26:718-726(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[15]"Loss of TSLC1 causes male infertility due to a defect at the spermatid stage of spermatogenesis."
van der Weyden L., Arends M.J., Chausiaux O.E., Ellis P.J., Lange U.C., Surani M.A., Affara N., Murakami Y., Adams D.J., Bradley A.
Mol. Cell. Biol. 26:3595-3609(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[16]"Disruption of spermatogenic cell adhesion and male infertility in mice lacking TSLC1/IGSF4, an immunoglobulin superfamily cell adhesion molecule."
Yamada D., Yoshida M., Williams Y.N., Fukami T., Kikuchi S., Masuda M., Maruyama T., Ohta T., Nakae D., Maekawa A., Kitamura T., Murakami Y.
Mol. Cell. Biol. 26:3610-3624(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[17]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, MASS SPECTROMETRY.
Tissue: Macrophage.
[18]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104 AND ASN-116, MASS SPECTROMETRY.
Tissue: Myoblast.
[19]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-104; ASN-116; ASN-168; ASN-304; ASN-307 AND ASN-311, MASS SPECTROMETRY.
[20]"N-glycosylation at the SynCAM (synaptic cell adhesion molecule) immunoglobulin interface modulates synaptic adhesion."
Fogel A.I., Li Y., Giza J., Wang Q., Lam T.T., Modis Y., Biederer T.
J. Biol. Chem. 285:34864-34874(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-70 AND ASN-104, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF434663 mRNA. Translation: AAL86736.1.
AF539424 mRNA. Translation: AAN01614.1.
AB021964 mRNA. Translation: BAA87914.1.
AB021965 mRNA. Translation: BAA87915.1.
AB064265 mRNA. Translation: BAB83501.2.
AY351388 mRNA. Translation: AAQ02381.1.
AF061260 mRNA. Translation: AAC67243.1. Frameshift.
AB092414 mRNA. Translation: BAC66173.1.
AB183399 mRNA. Translation: BAD30018.1.
AB183400 mRNA. Translation: BAD30019.1.
AB183401 mRNA. Translation: BAD30020.1.
AB183402 mRNA. Translation: BAD30021.1.
IPIIPI00322447.
IPI00410985.
IPI00411088.
IPI00461967.
IPI00849429.
IPI00849618.
IPI00849722.
RefSeqNP_001020771.1. NM_001025600.1.
NP_061240.3. NM_018770.3.
NP_997558.2. NM_207675.2.
NP_997559.1. NM_207676.2.
UniGeneMm.234832.

3D structure databases

HSSPHSSP built from PDB template 1Z9M based on UniProtKB Q8IZQ9.
ProteinModelPortalQ8R5M8.
SMRQ8R5M8. Positions 47-348.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8R5M8. 1 interaction.
STRING10090.ENSMUSP00000083073.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteQ8R5M8.

Proteomic databases

PaxDbQ8R5M8.
PRIDEQ8R5M8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034581; ENSMUSP00000034581; ENSMUSG00000032076.
ENSMUST00000085909; ENSMUSP00000083073; ENSMUSG00000032076.
ENSMUST00000114547; ENSMUSP00000110194; ENSMUSG00000032076.
ENSMUST00000114548; ENSMUSP00000110195; ENSMUSG00000032076.
GeneID54725.
KEGGmmu:54725.
UCSCuc009phn.1. mouse.
uc009pho.1. mouse.
uc009php.1. mouse.
uc009phq.1. mouse.
uc009phr.1. mouse.

Organism-specific databases

CTD23705.
MGIMGI:1889272. Cadm1.

Phylogenomic databases

eggNOGNOG69486.
GeneTreeENSGT00610000085800.
HOVERGENHBG057086.
InParanoidQ8R5M8.
KOK06781.

Gene expression databases

ArrayExpressQ8R5M8.
BgeeQ8R5M8.
CleanExMM_CADM1.
GenevestigatorQ8R5M8.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR003585. Neurexin-like.
[Graphical view]
PfamPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00294. 4.1m. 1 hit.
SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio311582.
SOURCESearch...

Entry information

Entry nameCADM1_MOUSE
AccessionPrimary (citable) accession number: Q8R5M8
Secondary accession number(s): Q6F3J3 expand/collapse secondary AC list , Q7TNL1, Q80VG4, Q8K3T6, Q8R4L1, Q9QYL5, Q9QYL6, Q9Z2H8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents