CADM4_MOUSE
ID CADM4_MOUSE Reviewed; 388 AA.
AC Q8R464;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=14659875; DOI=10.1016/j.gene.2003.09.018;
RA Fukami T., Satoh H., Williams Y.N., Masuda M., Fukuhara H., Maruyama T.,
RA Yageta M., Kuramochi M., Takamoto S., Murakami Y.;
RT "Isolation of the mouse Tsll1 and Tsll2 genes, orthologues of the human
RT TSLC1-like genes 1 and 2 (TSLL1 and TSLL2).";
RL Gene 323:11-18(2003).
RN [2]
RP GLYCOSYLATION.
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:14659875}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain and several organs including
CC the kidney and liver. {ECO:0000269|PubMed:14659875}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16261159}.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY059394; AAL29692.1; -; mRNA.
DR CCDS; CCDS20951.1; -.
DR RefSeq; NP_694752.1; NM_153112.3.
DR PDB; 5ZO1; X-ray; 2.20 A; A=25-317.
DR PDB; 5ZO2; X-ray; 3.29 A; A/C=25-317.
DR PDBsum; 5ZO1; -.
DR PDBsum; 5ZO2; -.
DR AlphaFoldDB; Q8R464; -.
DR SMR; Q8R464; -.
DR BioGRID; 234426; 2.
DR IntAct; Q8R464; 1.
DR STRING; 10090.ENSMUSP00000066880; -.
DR GlyConnect; 2200; 11 N-Linked glycans (3 sites).
DR GlyGen; Q8R464; 4 sites, 11 N-linked glycans (3 sites).
DR iPTMnet; Q8R464; -.
DR PhosphoSitePlus; Q8R464; -.
DR SwissPalm; Q8R464; -.
DR jPOST; Q8R464; -.
DR MaxQB; Q8R464; -.
DR PaxDb; Q8R464; -.
DR PeptideAtlas; Q8R464; -.
DR PRIDE; Q8R464; -.
DR ProteomicsDB; 265500; -.
DR ABCD; Q8R464; 1 sequenced antibody.
DR Antibodypedia; 2174; 300 antibodies from 41 providers.
DR DNASU; 260299; -.
DR Ensembl; ENSMUST00000068023; ENSMUSP00000066880; ENSMUSG00000054793.
DR GeneID; 260299; -.
DR KEGG; mmu:260299; -.
DR UCSC; uc009fps.1; mouse.
DR CTD; 199731; -.
DR MGI; MGI:2449088; Cadm4.
DR VEuPathDB; HostDB:ENSMUSG00000054793; -.
DR eggNOG; ENOG502RFJZ; Eukaryota.
DR GeneTree; ENSGT00940000161223; -.
DR HOGENOM; CLU_047574_2_0_1; -.
DR InParanoid; Q8R464; -.
DR OMA; CITPRCQ; -.
DR OrthoDB; 716894at2759; -.
DR PhylomeDB; Q8R464; -.
DR TreeFam; TF338300; -.
DR BioGRID-ORCS; 260299; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Cadm4; mouse.
DR PRO; PR:Q8R464; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R464; protein.
DR Bgee; ENSMUSG00000054793; Expressed in embryonic brain and 206 other tissues.
DR Genevisible; Q8R464; MM.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0044291; C:cell-cell contact zone; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; IPI:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IMP: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 DisProt; DP02679; -.
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 3D-structure; Cell adhesion; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; 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_0000291981"
FT TOPO_DOM 25..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:0007744|PubMed:21183079"
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 STRAND 26..28
FT /evidence="ECO:0007829|PDB:5ZO2"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:5ZO1"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:5ZO1"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 139..152
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 177..187
FT /evidence="ECO:0007829|PDB:5ZO1"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:5ZO2"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 220..231
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:5ZO2"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:5ZO1"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:5ZO1"
FT STRAND 298..306
FT /evidence="ECO:0007829|PDB:5ZO1"
SQ SEQUENCE 388 AA; 42723 MW; 8E3A9DF1C3B9D23E CRC64;
MGRARRFQWP LLLLWAAAAG PGTGQEVQTE NVTVAEGGVA EITCRLHQYD GSIVVIQNPA
RQTLFFNGTR ALKDERFQLE EFSPRRVRIR LSDARLEDEG GYFCQLYTED THHQIATLTV
LVAPENPVVE VREQAVEGGE VELSCLVPRS RPAAVLRWYR DRKELKGVSS GQENGKVWSV
ASTVRFRVDR KDDGGIVICE AQNQALPSGH SKQTQYVLDV QYSPTARIHA SQAVVREGDT
LVLTCAVTGN PRPNQIRWNR GNESLPERAE AVGETLTLPG LVSADNGTYT CEAANKHGHA
RALYVLVVYD PGAVVEAQTS VPYAIVGGIL ALLVFLIICV LVGMVWCSVR QKGSYLTHEA
SGLDEQGEAR EAFLNGGDGH KRKEEFFI
