Cell adhesion molecule 4 (Immunoglobulin superfamily member 4C) (IgSF4C) (Nectin-like protein 4) (NECL-4) (TSLC1-like protein 2)

 CADM4_HUMAN             Reviewed;         388 AA.
 Q8NFZ8; B2R7L5; Q9Y4A4;
 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
 01-OCT-2002, sequence version 1.
 25-MAY-2022, entry version 153.
 RecName: Full=Cell adhesion molecule 4;
 AltName: Full=Immunoglobulin superfamily member 4C;
          Short=IgSF4C;
 AltName: Full=Nectin-like protein 4;
          Short=NECL-4;
 AltName: Full=TSLC1-like protein 2;
 Flags: Precursor;
 Name=CADM4; Synonyms=IGSF4C, NECL4, TSLL2;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
 Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
 Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
 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 [LARGE SCALE MRNA].
 TISSUE=Amygdala;
 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).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=15057824; DOI=10.1038/nature02399;
 Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
 Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
 Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
 Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
 Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
 Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
 Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
 Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
 Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
 McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
 Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
 Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
 She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
 Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
 Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
 Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
 Rubin E.M., Lucas S.M.;
 "The DNA sequence and biology of human chromosome 19.";
 Nature 428:529-535(2004).
 [4]
 FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
 PubMed=16261159; DOI=10.1038/sj.onc.1209192;
 Williams Y.N., Masuda M., Sakurai-Yageta M., Maruyama T., Shibuya M.,
 Murakami Y.;
 "Cell adhesion and prostate tumor-suppressor activity of TSLL2/IGSF4C, an
 immunoglobulin superfamily molecule homologous to TSLC1/IGSF4.";
 Oncogene 25:1446-1453(2006).
 -!- FUNCTION: Involved in the cell-cell adhesion. Has calcium- and
     magnesium-independent cell-cell adhesion activity. May have tumor-
     suppressor activity. {ECO:0000269|PubMed:16261159}.
 -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:16261159}.
 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
     membrane protein {ECO:0000305}.
 -!- TISSUE SPECIFICITY: Expressed in brain, prostate, brain, kidney and
     some other organs. {ECO:0000269|PubMed:11536053,
     ECO:0000269|PubMed:16261159}.
 -!- PTM: N-glycosylated. {ECO:0000250}.
 -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=AAC32740.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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 EMBL; AF363368; AAM60750.1; -; mRNA.
 EMBL; AK313028; BAG35862.1; -; mRNA.
 EMBL; AC005525; AAC32740.1; ALT_SEQ; Genomic_DNA.
 CCDS; CCDS12627.1; -.
 RefSeq; NP_660339.1; NM_145296.1.
 AlphaFoldDB; Q8NFZ8; -.
 SMR; Q8NFZ8; -.
 BioGRID; 128268; 57.
 IntAct; Q8NFZ8; 6.
 MINT; Q8NFZ8; -.
 STRING; 9606.ENSP00000222374; -.
 GlyConnect; 1102; 2 N-Linked glycans (2 sites).
 GlyGen; Q8NFZ8; 5 sites, 2 N-linked glycans (2 sites).
 iPTMnet; Q8NFZ8; -.
 PhosphoSitePlus; Q8NFZ8; -.
 SwissPalm; Q8NFZ8; -.
 BioMuta; CADM4; -.
 DMDM; 74762572; -.
 EPD; Q8NFZ8; -.
 jPOST; Q8NFZ8; -.
 MassIVE; Q8NFZ8; -.
 MaxQB; Q8NFZ8; -.
 PaxDb; Q8NFZ8; -.
 PeptideAtlas; Q8NFZ8; -.
 PRIDE; Q8NFZ8; -.
 ProteomicsDB; 73401; -.
 ABCD; Q8NFZ8; 1 sequenced antibody.
 Antibodypedia; 2174; 298 antibodies from 41 providers.
 DNASU; 199731; -.
 Ensembl; ENST00000222374.3; ENSP00000222374.1; ENSG00000105767.3.
 GeneID; 199731; -.
 KEGG; hsa:199731; -.
 MANE-Select; ENST00000222374.3; ENSP00000222374.1; NM_145296.2; NP_660339.1.
 UCSC; uc002oxc.2; human.
 CTD; 199731; -.
 DisGeNET; 199731; -.
 GeneCards; CADM4; -.
 HGNC; HGNC:30825; CADM4.
 HPA; ENSG00000105767; Tissue enhanced (brain, choroid plexus).
 MIM; 609744; gene.
 neXtProt; NX_Q8NFZ8; -.
 OpenTargets; ENSG00000105767; -.
 PharmGKB; PA162380931; -.
 VEuPathDB; HostDB:ENSG00000105767; -.
 eggNOG; ENOG502RFJZ; Eukaryota.
 GeneTree; ENSGT00940000161223; -.
 HOGENOM; CLU_047574_2_0_1; -.
 InParanoid; Q8NFZ8; -.
 OMA; CITPRCQ; -.
 OrthoDB; 716894at2759; -.
 PhylomeDB; Q8NFZ8; -.
 TreeFam; TF338300; -.
 PathwayCommons; Q8NFZ8; -.
 SignaLink; Q8NFZ8; -.
 BioGRID-ORCS; 199731; 186 hits in 1079 CRISPR screens.
 ChiTaRS; CADM4; human.
 GenomeRNAi; 199731; -.
 Pharos; Q8NFZ8; Tbio.
 PRO; PR:Q8NFZ8; -.
 Proteomes; UP000005640; Chromosome 19.
 RNAct; Q8NFZ8; protein.
 Bgee; ENSG00000105767; Expressed in C1 segment of cervical spinal cord and 195 other tissues.
 Genevisible; Q8NFZ8; HS.
 GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
 GO; GO:0044291; C:cell-cell contact zone; IDA:UniProtKB.
 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
 GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
 GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
 GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; IEA:Ensembl.
 GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IPI:UniProtKB.
 GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:UniProtKB.
 GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
 GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
 GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
 GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; ISS:UniProtKB.
 GO; GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
 GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
 GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
 GO; GO:0035020; P:regulation of Rac protein signal transduction; IMP:UniProtKB.
 GO; GO:0061041; P:regulation of wound healing; IMP:UniProtKB.
 Gene3D; 2.60.40.10; -; 3.
 InterPro; IPR028807; Cadm4.
 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.
 PANTHER; PTHR45889:SF3; PTHR45889:SF3; 1.
 Pfam; PF08205; C2-set_2; 1.
 Pfam; PF07686; V-set; 1.
 SMART; SM00294; 4.1m; 1.
 SMART; SM00409; IG; 3.
 SMART; SM00408; IGc2; 2.
 SUPFAM; SSF48726; SSF48726; 3.
 PROSITE; PS50835; IG_LIKE; 2.
 1: Evidence at protein level;
 Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
 Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
 Transmembrane; Transmembrane helix; Tumor suppressor.
 SIGNAL          1..20
                 /evidence="ECO:0000255"
 CHAIN           21..388
                 /note="Cell adhesion molecule 4"
                 /id="PRO_0000291980"
 TOPO_DOM        21..324
                 /note="Extracellular"
                 /evidence="ECO:0000255"
 TRANSMEM        325..345
                 /note="Helical"
                 /evidence="ECO:0000255"
 TOPO_DOM        346..388
                 /note="Cytoplasmic"
                 /evidence="ECO:0000255"
 DOMAIN          21..119
                 /note="Ig-like V-type"
 DOMAIN          124..219
                 /note="Ig-like C2-type 1"
 DOMAIN          224..307
                 /note="Ig-like C2-type 2"
 MOD_RES         361
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8R464"
 CARBOHYD        31
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        67
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        286
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 DISULFID        44..104
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
 DISULFID        145..199
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
 DISULFID        245..291
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
 VARIANT         225
                 /note="T -> A (in dbSNP:rs34246023)"
                 /id="VAR_032906"
 SEQUENCE   388 AA;  42785 MW;  B22301C9E21A9339 CRC64;
 MGRARRFQWP LLLLWAAAAG PGAGQEVQTE NVTVAEGGVA EITCRLHQYD GSIVVIQNPA
 RQTLFFNGTR ALKDERFQLE EFSPRRVRIR LSDARLEDEG GYFCQLYTED THHQIATLTV
 LVAPENPVVE VREQAVEGGE VELSCLVPRS RPAATLRWYR DRKELKGVSS SQENGKVWSV
 ASTVRFRVDR KDDGGIIICE AQNQALPSGH SKQTQYVLDV QYSPTARIHA SQAVVREGDT
 LVLTCAVTGN PRPNQIRWNR GNESLPERAE AVGETLTLPG LVSADNGTYT CEASNKHGHA
 RALYVLVVYD PGAVVEAQTS VPYAIVGGIL ALLVFLIICV LVGMVWCSVR QKGSYLTHEA
 SGLDEQGEAR EAFLNGSDGH KRKEEFFI

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