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Cell adhesion molecule 3 (Brain immunoglobulin receptor) (Immunoglobulin superfamily member 4B) (IgSF4B) (Nectin-like protein 1) (NECL-1) (Synaptic cell adhesion molecule 3) (SynCAM3) (TSLC1-like protein 1) (TSLL1)

 CADM3_HUMAN             Reviewed;         398 AA.
Q8N126; Q8IZQ9; Q9NVJ5; Q9UJP1;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
23-MAY-2018, entry version 146.
RecName: Full=Cell adhesion molecule 3;
AltName: Full=Brain immunoglobulin receptor;
AltName: Full=Immunoglobulin superfamily member 4B;
Short=IgSF4B;
AltName: Full=Nectin-like protein 1;
Short=NECL-1;
AltName: Full=Synaptic cell adhesion molecule 3;
Short=SynCAM3;
AltName: Full=TSLC1-like protein 1;
Short=TSLL1;
Flags: Precursor;
Name=CADM3; Synonyms=IGSF4B, NECL1, SYNCAM3, TSLL1;
ORFNames=UNQ225/PRO258;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
INDUCTION.
PubMed=11536053; DOI=10.1038/sj.onc.1204696;
Fukuhara H., Kuramochi M., Nobukuni T., Fukami T., Saino M.,
Maruyama T., Nomura S., Sekiya T., Murakami Y.;
"Isolation of the TSLL1 and TSLL2 genes, members of the tumor
suppressor TSLC1 gene family encoding transmembrane proteins.";
Oncogene 20:5401-5407(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=15893517; DOI=10.1016/j.bbamem.2005.01.013;
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.;
"Nectin-like molecule 1 is a protein 4.1N associated protein and
recruits protein 4.1N from cytoplasm to the plasma membrane.";
Biochim. Biophys. Acta 1669:142-154(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Cunningham S.A., Tran T.M., Arrate M.P.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-280 (ISOFORM 3).
Keryanov S.A., Gardner K.L.;
"Alternatively splicing forms of the human nectin V gene.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 25-39.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-398.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-290, AND LACK OF
GLYCOSYLATION AT ASN-25.
PubMed=18420026; DOI=10.1016/j.bbamem.2008.03.013;
Gao J., Chen T., Hu G., Gong Y., Qiang B., Yuan J., Peng X.;
"Nectin-like molecule 1 is a glycoprotein with a single N-
glycosylation site at N290KS which influences its adhesion activity.";
Biochim. Biophys. Acta 1778:1429-1435(2008).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-135, SUBUNIT, AND
DISULFIDE BOND.
PubMed=16467305; DOI=10.1074/jbc.M513459200;
Dong X., Xu F., Gong Y., Gao J., Lin P., Chen T., Peng Y., Qiang B.,
Yuan J., Peng X., Rao Z.;
"Crystal structure of the V domain of human Nectin-like molecule-
1/Syncam3/Tsll1/Igsf4b, a neural tissue-specific immunoglobulin-like
cell-cell adhesion molecule.";
J. Biol. Chem. 281:10610-10617(2006).
-!- FUNCTION: Involved in the cell-cell adhesion. Has both calcium-
independent homophilic cell-cell adhesion activity and calcium-
independent heterophilic cell-cell adhesion activity with IGSF4,
NECTIN1 and NECTIN3. Interaction with EPB41L1 may regulate
structure or function of cell-cell junctions (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Homodimer. Can form trans-heterodimers with NECTIN3.
Interacts with EPB41L1, DLG3, MPP6 and CASK (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q99N28}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q99N28}. Cell junction
{ECO:0000250|UniProtKB:Q99N28}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8N126-1; Sequence=Displayed;
Name=2;
IsoId=Q8N126-2; Sequence=VSP_017221;
Name=3;
IsoId=Q8N126-3; Sequence=VSP_022008;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed mainly in adult and
fetal brain. Isoform 2 is highly expressed in adult brain and
weakly expressed in placenta. In brain, Isoform 2 is highly
expressed in cerebellum. {ECO:0000269|PubMed:11536053,
ECO:0000269|PubMed:15893517, ECO:0000269|PubMed:18420026}.
-!- INDUCTION: Markedly in glioma cell lines and prostate cancer cell
lines. {ECO:0000269|PubMed:11536053}.
-!- DOMAIN: The cytoplasmic region mediates interaction with EPB41L1,
DLG3, MPP6 and CASK. {ECO:0000250}.
-!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA91756.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF363367; AAM60749.1; -; mRNA.
EMBL; AF062733; AAD17540.2; -; mRNA.
EMBL; AY046418; AAL02143.1; -; mRNA.
EMBL; AY358332; AAQ88698.1; -; mRNA.
EMBL; AL035403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF529206; AAN75603.1; -; mRNA.
EMBL; AK001560; BAA91756.1; ALT_INIT; mRNA.
CCDS; CCDS1182.1; -. [Q8N126-2]
CCDS; CCDS44251.1; -. [Q8N126-1]
RefSeq; NP_001120645.1; NM_001127173.2. [Q8N126-1]
RefSeq; NP_001333439.1; NM_001346510.1. [Q8N126-3]
RefSeq; NP_067012.1; NM_021189.4. [Q8N126-2]
UniGene; Hs.365689; -.
PDB; 1Z9M; X-ray; 2.40 A; A/B=25-135.
PDBsum; 1Z9M; -.
ProteinModelPortal; Q8N126; -.
SMR; Q8N126; -.
iPTMnet; Q8N126; -.
PhosphoSitePlus; Q8N126; -.
BioMuta; CADM3; -.
DMDM; 74759761; -.
EPD; Q8N126; -.
MaxQB; Q8N126; -.
PeptideAtlas; Q8N126; -.
PRIDE; Q8N126; -.
DNASU; 57863; -.
Ensembl; ENST00000368124; ENSP00000357106; ENSG00000162706. [Q8N126-2]
Ensembl; ENST00000368125; ENSP00000357107; ENSG00000162706. [Q8N126-1]
GeneID; 57863; -.
KEGG; hsa:57863; -.
UCSC; uc001ftk.3; human. [Q8N126-1]
CTD; 57863; -.
DisGeNET; 57863; -.
EuPathDB; HostDB:ENSG00000162706.12; -.
GeneCards; CADM3; -.
HGNC; HGNC:17601; CADM3.
HPA; CAB025746; -.
HPA; HPA002981; -.
MIM; 609743; gene.
neXtProt; NX_Q8N126; -.
OpenTargets; ENSG00000162706; -.
PharmGKB; PA162380906; -.
GeneTree; ENSGT00900000140811; -.
HOGENOM; HOG000036057; -.
HOVERGEN; HBG057086; -.
InParanoid; Q8N126; -.
KO; K06780; -.
OMA; AAQLTWR; -.
OrthoDB; EOG091G0BHE; -.
PhylomeDB; Q8N126; -.
TreeFam; TF326804; -.
Reactome; R-HSA-418990; Adherens junctions interactions.
Reactome; R-HSA-420597; Nectin/Necl trans heterodimerization.
ChiTaRS; CADM3; human.
EvolutionaryTrace; Q8N126; -.
GeneWiki; CADM3; -.
GenomeRNAi; 57863; -.
PRO; PR:Q8N126; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162706; -.
CleanEx; HS_CADM3; -.
ExpressionAtlas; Q8N126; baseline and differential.
Genevisible; Q8N126; HS.
GO; GO:0005913; C:cell-cell adherens junction; IBA:GO_Central.
GO; GO:0005911; C:cell-cell junction; ISS:HGNC.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0034332; P:adherens junction organization; TAS:Reactome.
GO; GO:0008037; P:cell recognition; IBA:GO_Central.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:HGNC.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:HGNC.
GO; GO:0008104; P:protein localization; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR003585; Neurexin-like.
Pfam; PF08205; C2-set_2; 1.
Pfam; PF07679; I-set; 1.
SMART; SM00294; 4.1m; 1.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell adhesion;
Cell junction; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 24 {ECO:0000269|PubMed:15340161}.
CHAIN 25 398 Cell adhesion molecule 3.
/FTId=PRO_0000046067.
TOPO_DOM 25 330 Extracellular. {ECO:0000255}.
TRANSMEM 331 351 Helical. {ECO:0000255}.
TOPO_DOM 352 398 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 126 Ig-like V-type.
DOMAIN 130 228 Ig-like C2-type 1.
DOMAIN 233 315 Ig-like C2-type 2.
SITE 25 25 Not glycosylated.
{ECO:0000269|PubMed:18420026}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000250|UniProtKB:Q99N28}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18420026}.
DISULFID 50 110 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:16467305}.
DISULFID 152 209 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 254 299 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 29 29 D -> DGYWQEQDLELGTLAPLDEAISSTVWSSPDMLASQ
(in isoform 2).
{ECO:0000303|PubMed:15893517}.
/FTId=VSP_017221.
VAR_SEQ 185 231 GKTFTVSSSVTFQVTREDDGASIVCSVNHESLKGADRSTSQ
RIEVLY -> D (in isoform 3).
{ECO:0000303|Ref.6}.
/FTId=VSP_022008.
VARIANT 162 162 R -> W (in dbSNP:rs3026987).
/FTId=VAR_059383.
STRAND 38 41 {ECO:0000244|PDB:1Z9M}.
STRAND 46 51 {ECO:0000244|PDB:1Z9M}.
STRAND 60 63 {ECO:0000244|PDB:1Z9M}.
STRAND 69 72 {ECO:0000244|PDB:1Z9M}.
STRAND 83 88 {ECO:0000244|PDB:1Z9M}.
STRAND 90 97 {ECO:0000244|PDB:1Z9M}.
HELIX 102 104 {ECO:0000244|PDB:1Z9M}.
STRAND 106 112 {ECO:0000244|PDB:1Z9M}.
STRAND 114 116 {ECO:0000244|PDB:1Z9M}.
STRAND 118 127 {ECO:0000244|PDB:1Z9M}.
SEQUENCE 398 AA; 43300 MW; 601B2FB5D512DB6C CRC64;
MGAPAASLLL LLLLFACCWA PGGANLSQDD SQPWTSDETV VAGGTVVLKC QVKDHEDSSL
QWSNPAQQTL YFGEKRALRD NRIQLVTSTP HELSISISNV ALADEGEYTC SIFTMPVRTA
KSLVTVLGIP QKPIITGYKS SLREKDTATL NCQSSGSKPA ARLTWRKGDQ ELHGEPTRIQ
EDPNGKTFTV SSSVTFQVTR EDDGASIVCS VNHESLKGAD RSTSQRIEVL YTPTAMIRPD
PPHPREGQKL LLHCEGRGNP VPQQYLWEKE GSVPPLKMTQ ESALIFPFLN KSDSGTYGCT
ATSNMGSYKA YYTLNVNDPS PVPSSSSTYH AIIGGIVAFI VFLLLIMLIF LGHYLIRHKG
TYLTHEAKGS DDAPDADTAI INAEGGQSGG DDKKEYFI


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U0086r CLIA CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,Lnhr,L-selectin,Ly-22,Ly-22,Lymph node homing receptor,Lymphocyte antig 96T
U0086b CLIA Bos taurus,Bovine,CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,L-selectin,Lymph node homing receptor,SELL 96T
E0086m ELISA CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,Lnhr,L-selectin,Ly22,Ly-22,Ly-22,Lymph node homing receptor,Lymphocyte 96T
E0086b ELISA Bos taurus,Bovine,CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,L-selectin,Lymph node homing receptor,SELL 96T
E0086r ELISA CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,Lnhr,L-selectin,Ly-22,Ly-22,Lymph node homing receptor,Lymphocyte anti 96T


 

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