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

 CADM4_MOUSE             Reviewed;         388 AA.
Q8R464;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
25-MAY-2022, entry version 139.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=129/SvJ;
PubMed=14659875; DOI=10.1016/j.gene.2003.09.018;
Fukami T., Satoh H., Williams Y.N., Masuda M., Fukuhara H., Maruyama T.,
Yageta M., Kuramochi M., Takamoto S., Murakami Y.;
"Isolation of the mouse Tsll1 and Tsll2 genes, orthologues of the human
TSLC1-like genes 1 and 2 (TSLL1 and TSLL2).";
Gene 323:11-18(2003).
[2]
GLYCOSYLATION.
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).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Involved in the cell-cell adhesion. Has calcium- and
magnesium-independent cell-cell adhesion activity. May have tumor-
suppressor activity. {ECO:0000269|PubMed:14659875}.
-!- SUBUNIT: Monomer and homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in the brain and several organs including
the kidney and liver. {ECO:0000269|PubMed:14659875}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:16261159}.
-!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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EMBL; AY059394; AAL29692.1; -; mRNA.
CCDS; CCDS20951.1; -.
RefSeq; NP_694752.1; NM_153112.3.
PDB; 5ZO1; X-ray; 2.20 A; A=25-317.
PDB; 5ZO2; X-ray; 3.29 A; A/C=25-317.
PDBsum; 5ZO1; -.
PDBsum; 5ZO2; -.
AlphaFoldDB; Q8R464; -.
SMR; Q8R464; -.
BioGRID; 234426; 2.
IntAct; Q8R464; 1.
STRING; 10090.ENSMUSP00000066880; -.
GlyConnect; 2200; 11 N-Linked glycans (3 sites).
GlyGen; Q8R464; 4 sites, 11 N-linked glycans (3 sites).
iPTMnet; Q8R464; -.
PhosphoSitePlus; Q8R464; -.
SwissPalm; Q8R464; -.
jPOST; Q8R464; -.
MaxQB; Q8R464; -.
PaxDb; Q8R464; -.
PeptideAtlas; Q8R464; -.
PRIDE; Q8R464; -.
ProteomicsDB; 265500; -.
ABCD; Q8R464; 1 sequenced antibody.
Antibodypedia; 2174; 298 antibodies from 41 providers.
DNASU; 260299; -.
Ensembl; ENSMUST00000068023; ENSMUSP00000066880; ENSMUSG00000054793.
GeneID; 260299; -.
KEGG; mmu:260299; -.
UCSC; uc009fps.1; mouse.
CTD; 199731; -.
MGI; MGI:2449088; Cadm4.
VEuPathDB; HostDB:ENSMUSG00000054793; -.
eggNOG; ENOG502RFJZ; Eukaryota.
GeneTree; ENSGT00940000161223; -.
HOGENOM; CLU_047574_2_0_1; -.
InParanoid; Q8R464; -.
OMA; CITPRCQ; -.
OrthoDB; 716894at2759; -.
PhylomeDB; Q8R464; -.
TreeFam; TF338300; -.
BioGRID-ORCS; 260299; 6 hits in 73 CRISPR screens.
ChiTaRS; Cadm4; mouse.
PRO; PR:Q8R464; -.
Proteomes; UP000000589; Chromosome 7.
RNAct; Q8R464; protein.
Bgee; ENSMUSG00000054793; Expressed in primary visual cortex and 254 other tissues.
Genevisible; Q8R464; MM.
GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
GO; GO:0044291; C:cell-cell contact zone; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; IPI:UniProtKB.
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; IMP:UniProtKB.
GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IMP: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.
DisProt; DP02679; -.
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;
3D-structure; 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_0000291981"
TOPO_DOM 25..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:0007744|PubMed:21183079"
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"
STRAND 26..28
/evidence="ECO:0007829|PDB:5ZO2"
STRAND 30..35
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 40..45
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 54..57
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 63..66
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 77..82
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 84..91
/evidence="ECO:0007829|PDB:5ZO1"
HELIX 96..98
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 100..106
/evidence="ECO:0007829|PDB:5ZO1"
TURN 107..109
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 113..122
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 128..133
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 139..152
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 155..160
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 163..165
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 168..174
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 177..187
/evidence="ECO:0007829|PDB:5ZO1"
HELIX 190..192
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 196..202
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 204..206
/evidence="ECO:0007829|PDB:5ZO2"
STRAND 212..217
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 220..231
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 233..236
/evidence="ECO:0007829|PDB:5ZO2"
STRAND 241..251
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 257..263
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 270..272
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 275..278
/evidence="ECO:0007829|PDB:5ZO1"
HELIX 283..285
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 287..295
/evidence="ECO:0007829|PDB:5ZO1"
STRAND 298..306
/evidence="ECO:0007829|PDB:5ZO1"
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


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