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.
 25-MAY-2022, entry version 173.
 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, PALS2 and CASK (By similarity). {ECO:0000250}.
 -!- INTERACTION:
     Q8N126; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-18961338, EBI-2855401;
 -!- 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,
     PALS2 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]
 PDB; 1Z9M; X-ray; 2.40 A; A/B=25-135.
 PDBsum; 1Z9M; -.
 AlphaFoldDB; Q8N126; -.
 SMR; Q8N126; -.
 BioGRID; 121793; 2.
 IntAct; Q8N126; 1.
 STRING; 9606.ENSP00000357106; -.
 GlyGen; Q8N126; 2 sites, 1 O-linked glycan (1 site).
 iPTMnet; Q8N126; -.
 PhosphoSitePlus; Q8N126; -.
 BioMuta; CADM3; -.
 DMDM; 74759761; -.
 EPD; Q8N126; -.
 jPOST; Q8N126; -.
 MassIVE; Q8N126; -.
 MaxQB; Q8N126; -.
 PeptideAtlas; Q8N126; -.
 PRIDE; Q8N126; -.
 ProteomicsDB; 71524; -. [Q8N126-1]
 ProteomicsDB; 71525; -. [Q8N126-2]
 ProteomicsDB; 71526; -. [Q8N126-3]
 Antibodypedia; 669; 363 antibodies from 34 providers.
 DNASU; 57863; -.
 Ensembl; ENST00000368124.8; ENSP00000357106.4; ENSG00000162706.13. [Q8N126-2]
 Ensembl; ENST00000368125.9; ENSP00000357107.4; ENSG00000162706.13.
 GeneID; 57863; -.
 KEGG; hsa:57863; -.
 MANE-Select; ENST00000368125.9; ENSP00000357107.4; NM_001127173.3; NP_001120645.1.
 UCSC; uc001ftk.3; human. [Q8N126-1]
 CTD; 57863; -.
 DisGeNET; 57863; -.
 GeneCards; CADM3; -.
 HGNC; HGNC:17601; CADM3.
 HPA; ENSG00000162706; Tissue enhanced (brain, placenta).
 MIM; 609743; gene.
 neXtProt; NX_Q8N126; -.
 OpenTargets; ENSG00000162706; -.
 PharmGKB; PA162380906; -.
 VEuPathDB; HostDB:ENSG00000162706; -.
 eggNOG; ENOG502QWJ8; Eukaryota.
 GeneTree; ENSGT00940000159779; -.
 HOGENOM; CLU_047574_1_0_1; -.
 InParanoid; Q8N126; -.
 OMA; MTQERAL; -.
 OrthoDB; 716894at2759; -.
 PhylomeDB; Q8N126; -.
 TreeFam; TF326804; -.
 PathwayCommons; Q8N126; -.
 Reactome; R-HSA-418990; Adherens junctions interactions.
 Reactome; R-HSA-420597; Nectin/Necl trans heterodimerization.
 SignaLink; Q8N126; -.
 BioGRID-ORCS; 57863; 9 hits in 1059 CRISPR screens.
 ChiTaRS; CADM3; human.
 EvolutionaryTrace; Q8N126; -.
 GeneWiki; CADM3; -.
 GenomeRNAi; 57863; -.
 Pharos; Q8N126; Tbio.
 PRO; PR:Q8N126; -.
 Proteomes; UP000005640; Chromosome 1.
 RNAct; Q8N126; protein.
 Bgee; ENSG00000162706; Expressed in cerebellar cortex and 196 other tissues.
 ExpressionAtlas; Q8N126; baseline and differential.
 Genevisible; Q8N126; HS.
 GO; GO:0005911; C:cell-cell junction; ISS:HGNC-UCL.
 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
 GO; GO:0005886; C:plasma membrane; TAS:Reactome.
 GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC-UCL.
 GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:HGNC-UCL.
 GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:HGNC-UCL.
 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; IPR003599; Ig_sub.
 InterPro; IPR003598; Ig_sub2.
 InterPro; IPR013106; Ig_V-set.
 InterPro; IPR003585; Neurexin-like.
 Pfam; PF08205; C2-set_2; 1.
 Pfam; PF07686; V-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; Direct protein sequencing; Disulfide bond; Glycoprotein;
 Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
 Repeat; Signal; Transmembrane; Transmembrane helix.
 SIGNAL          1..24
                 /evidence="ECO:0000269|PubMed:15340161"
 CHAIN           25..398
                 /note="Cell adhesion molecule 3"
                 /id="PRO_0000046067"
 TOPO_DOM        25..330
                 /note="Extracellular"
                 /evidence="ECO:0000255"
 TRANSMEM        331..351
                 /note="Helical"
                 /evidence="ECO:0000255"
 TOPO_DOM        352..398
                 /note="Cytoplasmic"
                 /evidence="ECO:0000255"
 DOMAIN          25..126
                 /note="Ig-like V-type"
 DOMAIN          130..228
                 /note="Ig-like C2-type 1"
 DOMAIN          233..315
                 /note="Ig-like C2-type 2"
 REGION          367..398
                 /note="Disordered"
                 /evidence="ECO:0000256|SAM:MobiDB-lite"
 SITE            25
                 /note="Not glycosylated"
                 /evidence="ECO:0000269|PubMed:18420026"
 MOD_RES         388
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q99N28"
 CARBOHYD        290
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000269|PubMed:18420026"
 DISULFID        50..110
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
                 ECO:0000269|PubMed:16467305"
 DISULFID        152..209
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
 DISULFID        254..299
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
 VAR_SEQ         29
                 /note="D -> DGYWQEQDLELGTLAPLDEAISSTVWSSPDMLASQ (in isoform
                 2)"
                 /evidence="ECO:0000303|PubMed:15893517"
                 /id="VSP_017221"
 VAR_SEQ         185..231
                 /note="GKTFTVSSSVTFQVTREDDGASIVCSVNHESLKGADRSTSQRIEVLY -> D
                 (in isoform 3)"
                 /evidence="ECO:0000303|Ref.6"
                 /id="VSP_022008"
 VARIANT         162
                 /note="R -> W (in dbSNP:rs3026987)"
                 /id="VAR_059383"
 STRAND          38..41
                 /evidence="ECO:0007829|PDB:1Z9M"
 STRAND          46..51
                 /evidence="ECO:0007829|PDB:1Z9M"
 STRAND          60..63
                 /evidence="ECO:0007829|PDB:1Z9M"
 STRAND          69..72
                 /evidence="ECO:0007829|PDB:1Z9M"
 STRAND          83..88
                 /evidence="ECO:0007829|PDB:1Z9M"
 STRAND          90..97
                 /evidence="ECO:0007829|PDB:1Z9M"
 HELIX           102..104
                 /evidence="ECO:0007829|PDB:1Z9M"
 STRAND          106..112
                 /evidence="ECO:0007829|PDB:1Z9M"
 STRAND          114..116
                 /evidence="ECO:0007829|PDB:1Z9M"
 STRAND          118..127
                 /evidence="ECO:0007829|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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