CADM4_HUMAN
ID CADM4_HUMAN Reviewed; 388 AA.
AC Q8NFZ8; B2R7L5; Q9Y4A4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cell adhesion molecule 4;
DE AltName: Full=Immunoglobulin superfamily member 4C;
DE Short=IgSF4C;
DE AltName: Full=Nectin-like protein 4;
DE Short=NECL-4;
DE AltName: Full=TSLC1-like protein 2;
DE Flags: Precursor;
GN Name=CADM4; Synonyms=IGSF4C, NECL4, TSLL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11536053; DOI=10.1038/sj.onc.1204696;
RA Fukuhara H., Kuramochi M., Nobukuni T., Fukami T., Saino M., Maruyama T.,
RA Nomura S., Sekiya T., Murakami Y.;
RT "Isolation of the TSLL1 and TSLL2 genes, members of the tumor suppressor
RT TSLC1 gene family encoding transmembrane proteins.";
RL Oncogene 20:5401-5407(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=16261159; DOI=10.1038/sj.onc.1209192;
RA Williams Y.N., Masuda M., Sakurai-Yageta M., Maruyama T., Shibuya M.,
RA Murakami Y.;
RT "Cell adhesion and prostate tumor-suppressor activity of TSLL2/IGSF4C, an
RT immunoglobulin superfamily molecule homologous to TSLC1/IGSF4.";
RL Oncogene 25:1446-1453(2006).
CC -!- FUNCTION: Involved in the cell-cell adhesion. Has calcium- and
CC magnesium-independent cell-cell adhesion activity. May have tumor-
CC suppressor activity. {ECO:0000269|PubMed:16261159}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:16261159}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, prostate, brain, kidney and
CC some other organs. {ECO:0000269|PubMed:11536053,
CC ECO:0000269|PubMed:16261159}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC32740.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF363368; AAM60750.1; -; mRNA.
DR EMBL; AK313028; BAG35862.1; -; mRNA.
DR EMBL; AC005525; AAC32740.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS12627.1; -.
DR RefSeq; NP_660339.1; NM_145296.1.
DR AlphaFoldDB; Q8NFZ8; -.
DR SMR; Q8NFZ8; -.
DR BioGRID; 128268; 57.
DR IntAct; Q8NFZ8; 6.
DR MINT; Q8NFZ8; -.
DR STRING; 9606.ENSP00000222374; -.
DR GlyConnect; 1102; 2 N-Linked glycans (2 sites).
DR GlyGen; Q8NFZ8; 5 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q8NFZ8; -.
DR PhosphoSitePlus; Q8NFZ8; -.
DR SwissPalm; Q8NFZ8; -.
DR BioMuta; CADM4; -.
DR DMDM; 74762572; -.
DR EPD; Q8NFZ8; -.
DR jPOST; Q8NFZ8; -.
DR MassIVE; Q8NFZ8; -.
DR MaxQB; Q8NFZ8; -.
DR PaxDb; Q8NFZ8; -.
DR PeptideAtlas; Q8NFZ8; -.
DR PRIDE; Q8NFZ8; -.
DR ProteomicsDB; 73401; -.
DR ABCD; Q8NFZ8; 1 sequenced antibody.
DR Antibodypedia; 2174; 300 antibodies from 41 providers.
DR DNASU; 199731; -.
DR Ensembl; ENST00000222374.3; ENSP00000222374.1; ENSG00000105767.3.
DR GeneID; 199731; -.
DR KEGG; hsa:199731; -.
DR MANE-Select; ENST00000222374.3; ENSP00000222374.1; NM_145296.2; NP_660339.1.
DR UCSC; uc002oxc.2; human.
DR CTD; 199731; -.
DR DisGeNET; 199731; -.
DR GeneCards; CADM4; -.
DR HGNC; HGNC:30825; CADM4.
DR HPA; ENSG00000105767; Tissue enhanced (brain, choroid plexus).
DR MIM; 609744; gene.
DR neXtProt; NX_Q8NFZ8; -.
DR OpenTargets; ENSG00000105767; -.
DR PharmGKB; PA162380931; -.
DR VEuPathDB; HostDB:ENSG00000105767; -.
DR eggNOG; ENOG502RFJZ; Eukaryota.
DR GeneTree; ENSGT00940000161223; -.
DR HOGENOM; CLU_047574_2_0_1; -.
DR InParanoid; Q8NFZ8; -.
DR OMA; CITPRCQ; -.
DR OrthoDB; 716894at2759; -.
DR PhylomeDB; Q8NFZ8; -.
DR TreeFam; TF338300; -.
DR PathwayCommons; Q8NFZ8; -.
DR SignaLink; Q8NFZ8; -.
DR BioGRID-ORCS; 199731; 186 hits in 1079 CRISPR screens.
DR ChiTaRS; CADM4; human.
DR GenomeRNAi; 199731; -.
DR Pharos; Q8NFZ8; Tbio.
DR PRO; PR:Q8NFZ8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8NFZ8; protein.
DR Bgee; ENSG00000105767; Expressed in cortical plate and 143 other tissues.
DR Genevisible; Q8NFZ8; HS.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; IEA:Ensembl.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IPI:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:UniProtKB.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IMP:UniProtKB.
DR GO; GO:0061041; P:regulation of wound healing; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR028807; Cadm4.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR003585; Neurexin-like.
DR PANTHER; PTHR45889:SF3; PTHR45889:SF3; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Tumor suppressor.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..388
FT /note="Cell adhesion molecule 4"
FT /id="PRO_0000291980"
FT TOPO_DOM 21..324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..119
FT /note="Ig-like V-type"
FT DOMAIN 124..219
FT /note="Ig-like C2-type 1"
FT DOMAIN 224..307
FT /note="Ig-like C2-type 2"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R464"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 145..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 245..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 225
FT /note="T -> A (in dbSNP:rs34246023)"
FT /id="VAR_032906"
SQ 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
