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Cell adhesion molecule 3 (Immunoglobulin superfamily member 4B) (IgSF4B) (Nectin-like protein 1) (NECL-1) (Synaptic cell adhesion molecule 3) (TSLC1-like protein 1)

 CADM3_MOUSE             Reviewed;         396 AA.
Q99N28; Q8BSQ8; Q8K1H8;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
23-MAY-2018, entry version 138.
RecName: Full=Cell adhesion molecule 3;
AltName: Full=Immunoglobulin superfamily member 4B;
Short=IgSF4B;
AltName: Full=Nectin-like protein 1;
Short=NECL-1;
AltName: Full=Synaptic cell adhesion molecule 3;
AltName: Full=TSLC1-like protein 1;
Flags: Precursor;
Name=Cadm3; Synonyms=Igsf4b, Necl1, Syncam3, Tsll1;
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], SUBCELLULAR LOCATION, 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]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EPB41L1,
SUBCELLULAR LOCATION, TOPOLOGY, DEVELOPMENTAL STAGE, 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 [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-396.
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, INTERACTION WITH NECTIN3; DLG3; MPP6 AND CASK, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=15741237; DOI=10.1242/jcs.01656;
Kakunaga S., Ikeda W., Itoh S., Deguchi-Tawarada M., Ohtsuka T.,
Mizoguchi A., Takai Y.;
"Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific
immunoglobulin-like cell-cell adhesion molecule localizing at non-
junctional contact sites of presynaptic nerve terminals, axons and
glia cell processes.";
J. Cell Sci. 118:1267-1277(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
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 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.
{ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:15893517}.
-!- SUBUNIT: Homodimer. Can form trans-heterodimers with NECTIN3.
Interacts with EPB41L1, DLG3, MPP6 and CASK.
{ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:15893517}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14659875,
ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:15893517}; Single-
pass type I membrane protein {ECO:0000269|PubMed:15893517}. Cell
junction {ECO:0000269|PubMed:14659875,
ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:15893517}.
-!- TISSUE SPECIFICITY: Mainly expressed in brain, in neuronal cell
bodies of cerebellum, cortex, hippocampus, hypothalamus and spinal
cord. In spinal cord predominantly expressed in motor neurons.
Expressed in axons, presynaptic nerve terminals, glia cell
processes. {ECO:0000269|PubMed:14659875,
ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:15893517}.
-!- DEVELOPMENTAL STAGE: At E14.5 predominantly expressed in the
nervous system. {ECO:0000269|PubMed:15893517}.
-!- DOMAIN: The cytoplasmic region mediates interaction with EPB41L1,
DLG3, MPP6 and CASK.
-!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH29659.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY059393; AAL29691.1; -; mRNA.
EMBL; AF195662; AAG35584.1; -; mRNA.
EMBL; AK030782; BAC27137.1; -; mRNA.
EMBL; AK038917; BAC30168.1; -; mRNA.
EMBL; AK053077; BAC35258.1; -; mRNA.
EMBL; BC029659; AAH29659.1; ALT_INIT; mRNA.
CCDS; CCDS15528.1; -.
RefSeq; NP_444429.1; NM_053199.3.
UniGene; Mm.330524; -.
ProteinModelPortal; Q99N28; -.
BioGrid; 220505; 3.
IntAct; Q99N28; 3.
MINT; Q99N28; -.
STRING; 10090.ENSMUSP00000106851; -.
iPTMnet; Q99N28; -.
PhosphoSitePlus; Q99N28; -.
MaxQB; Q99N28; -.
PaxDb; Q99N28; -.
PeptideAtlas; Q99N28; -.
PRIDE; Q99N28; -.
Ensembl; ENSMUST00000111220; ENSMUSP00000106851; ENSMUSG00000005338.
GeneID; 94332; -.
KEGG; mmu:94332; -.
UCSC; uc007drh.1; mouse.
CTD; 57863; -.
MGI; MGI:2137858; Cadm3.
eggNOG; ENOG410IFCE; Eukaryota.
eggNOG; ENOG411017U; LUCA.
GeneTree; ENSGT00900000140811; -.
HOGENOM; HOG000036057; -.
HOVERGEN; HBG057086; -.
InParanoid; Q99N28; -.
KO; K06780; -.
PhylomeDB; Q99N28; -.
TreeFam; TF326804; -.
Reactome; R-MMU-418990; Adherens junctions interactions.
Reactome; R-MMU-420597; Nectin/Necl trans heterodimerization.
ChiTaRS; Cadm3; mouse.
PRO; PR:Q99N28; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000005338; -.
CleanEx; MM_CADM3; -.
ExpressionAtlas; Q99N28; baseline and differential.
Genevisible; Q99N28; MM.
GO; GO:0005913; C:cell-cell adherens junction; IBA:GO_Central.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0008037; P:cell recognition; IBA:GO_Central.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:HGNC.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:HGNC.
GO; GO:0008104; P:protein localization; IMP:MGI.
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; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR003585; Neurexin-like.
Pfam; PF08205; C2-set_2; 1.
Pfam; PF07679; I-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;
Calcium; Cell adhesion; Cell junction; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000250|UniProtKB:Q8N126}.
CHAIN 23 396 Cell adhesion molecule 3.
/FTId=PRO_0000046068.
TOPO_DOM 23 328 Extracellular. {ECO:0000255}.
TRANSMEM 329 349 Helical. {ECO:0000255}.
TOPO_DOM 350 396 Cytoplasmic. {ECO:0000255}.
DOMAIN 23 124 Ig-like V-type.
DOMAIN 128 226 Ig-like C2-type 1.
DOMAIN 231 313 Ig-like C2-type 2.
MOD_RES 386 386 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 108 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 150 207 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 252 297 {ECO:0000255|PROSITE-ProRule:PRU00114}.
SEQUENCE 396 AA; 42964 MW; C1ADF8B57D141F3A CRC64;
MGAPSALPLL LLLACSWAPG GANLSQDDSQ PWTSDETVVA GGTVVLKCQV KDHEDSSLQW
SNPAQQTLYF GEKRALRDNR IQLVSSTPHE LSISISNVAL ADEGEYTCSI FTMPVRTAKS
LVTVLGIPQK PIITGYKSSL REKETATLNC QSSGSKPAAQ LTWRKGDQEL HGDQTRIQED
PNGKTFTVSS SVSFQVTRED DGANIVCSVN HESLKGADRS TSQRIEVLYT PTAMIRPEPA
HPREGQKLLL HCEGRGNPVP QQYVWVKEGS EPPLKMTQES ALIFPFLNKS DSGTYGCTAT
SNMGSYTAYF TLNVNDPSPV PSSSSTYHAI IGGIVAFIVF LLLILLIFLG HYLIRHKGTY
LTHEAKGSDD APDADTAIIN AEGGQSGGDD KKEYFI


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