CADM3_MOUSE
ID CADM3_MOUSE Reviewed; 396 AA.
AC Q99N28; Q8BSQ8; Q8K1H8;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cell adhesion molecule 3;
DE AltName: Full=Immunoglobulin superfamily member 4B;
DE Short=IgSF4B;
DE AltName: Full=Nectin-like protein 1;
DE Short=NECL-1;
DE AltName: Full=Synaptic cell adhesion molecule 3;
DE AltName: Full=TSLC1-like protein 1;
DE Flags: Precursor;
GN Name=Cadm3; Synonyms=Igsf4b, Necl1, Syncam3, Tsll1;
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], SUBCELLULAR LOCATION, 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 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EPB41L1, SUBCELLULAR
RP LOCATION, TOPOLOGY, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=15893517; DOI=10.1016/j.bbamem.2005.01.013;
RA Zhou Y., Du G., Hu X., Yu S., Liu Y., Xu Y., Huang X., Liu J., Yin B.,
RA Fan M., Peng X., Qiang B., Yuan J.;
RT "Nectin-like molecule 1 is a protein 4.1N associated protein and recruits
RT protein 4.1N from cytoplasm to the plasma membrane.";
RL Biochim. Biophys. Acta 1669:142-154(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-396.
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH NECTIN3; DLG3; PALS2 AND CASK, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15741237; DOI=10.1242/jcs.01656;
RA Kakunaga S., Ikeda W., Itoh S., Deguchi-Tawarada M., Ohtsuka T.,
RA Mizoguchi A., Takai Y.;
RT "Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific
RT immunoglobulin-like cell-cell adhesion molecule localizing at non-
RT junctional contact sites of presynaptic nerve terminals, axons and glia
RT cell processes.";
RL J. Cell Sci. 118:1267-1277(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [7]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-136.
RX PubMed=33889941; DOI=10.1093/brain/awab019;
RA Rebelo A.P., Cortese A., Abraham A., Eshed-Eisenbach Y., Shner G.,
RA Vainshtein A., Buglo E., Camarena V., Gaidosh G., Shiekhattar R., Abreu L.,
RA Courel S., Burns D.K., Bai Y., Bacon C., Feely S.M.E., Castro D., Peles E.,
RA Reilly M.M., Shy M.E., Zuchner S.;
RT "A CADM3 variant causes Charcot-Marie-Tooth disease with marked upper limb
RT involvement.";
RL Brain 144:1197-1213(2021).
RN [8]
RP ERRATUM OF PUBMED:33889941.
RX PubMed=34037698; DOI=10.1093/brain/awab181;
RA Rebelo A.P., Cortese A., Abraham A., Eshed-Eisenbach Y., Shner G.,
RA Vainshtein A., Buglo E., Camarena V., Gaidosh G., Shiekhattar R., Abreu L.,
RA Courel S., Burns D.K., Bai Y., Bacon C., Feely S.M.E., Castro D., Peles E.,
RA Reilly M.M., Shy M.E., Zuchner S.;
RL Brain 144:e64-e64(2021).
CC -!- FUNCTION: Involved in the cell-cell adhesion. Has both calcium-
CC independent homophilic cell-cell adhesion activity and calcium-
CC independent heterophilic cell-cell adhesion activity with IGSF4,
CC NECTIN1 and NECTIN3. Interaction with EPB41L1 may regulate structure or
CC function of cell-cell junctions. {ECO:0000269|PubMed:15741237,
CC ECO:0000269|PubMed:15893517}.
CC -!- SUBUNIT: Homodimer. Can form trans-heterodimers with NECTIN3. Interacts
CC with EPB41L1, DLG3, PALS2 and CASK. {ECO:0000269|PubMed:15741237,
CC ECO:0000269|PubMed:15893517}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14659875,
CC ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:15893517,
CC ECO:0000269|PubMed:33889941}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:15893517}. Cell junction
CC {ECO:0000269|PubMed:14659875, ECO:0000269|PubMed:15741237,
CC ECO:0000269|PubMed:15893517}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain, in neuronal cell bodies
CC of cerebellum, cortex, hippocampus, hypothalamus and spinal cord. In
CC spinal cord predominantly expressed in motor neurons. Expressed in
CC axons, presynaptic nerve terminals, glia cell processes.
CC {ECO:0000269|PubMed:14659875, ECO:0000269|PubMed:15741237,
CC ECO:0000269|PubMed:15893517}.
CC -!- DEVELOPMENTAL STAGE: At 14.5 dpc predominantly expressed in the nervous
CC system. {ECO:0000269|PubMed:15893517}.
CC -!- DOMAIN: The cytoplasmic region mediates interaction with EPB41L1, DLG3,
CC PALS2 and CASK.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29659.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY059393; AAL29691.1; -; mRNA.
DR EMBL; AF195662; AAG35584.1; -; mRNA.
DR EMBL; AK030782; BAC27137.1; -; mRNA.
DR EMBL; AK038917; BAC30168.1; -; mRNA.
DR EMBL; AK053077; BAC35258.1; -; mRNA.
DR EMBL; BC029659; AAH29659.1; ALT_INIT; mRNA.
DR CCDS; CCDS15528.1; -.
DR RefSeq; NP_444429.1; NM_053199.3.
DR PDB; 5ZO2; X-ray; 3.29 A; B=23-133.
DR PDBsum; 5ZO2; -.
DR AlphaFoldDB; Q99N28; -.
DR SMR; Q99N28; -.
DR BioGRID; 220505; 3.
DR IntAct; Q99N28; 2.
DR STRING; 10090.ENSMUSP00000106851; -.
DR GlyGen; Q99N28; 1 site.
DR iPTMnet; Q99N28; -.
DR PhosphoSitePlus; Q99N28; -.
DR SwissPalm; Q99N28; -.
DR MaxQB; Q99N28; -.
DR PaxDb; Q99N28; -.
DR PeptideAtlas; Q99N28; -.
DR PRIDE; Q99N28; -.
DR ProteomicsDB; 265419; -.
DR ABCD; Q99N28; 3 sequenced antibodies.
DR Antibodypedia; 669; 364 antibodies from 34 providers.
DR DNASU; 94332; -.
DR Ensembl; ENSMUST00000111220; ENSMUSP00000106851; ENSMUSG00000005338.
DR GeneID; 94332; -.
DR KEGG; mmu:94332; -.
DR UCSC; uc007drh.1; mouse.
DR CTD; 57863; -.
DR MGI; MGI:2137858; Cadm3.
DR VEuPathDB; HostDB:ENSMUSG00000005338; -.
DR eggNOG; ENOG502QWJ8; Eukaryota.
DR GeneTree; ENSGT00940000159779; -.
DR HOGENOM; CLU_047574_1_0_1; -.
DR InParanoid; Q99N28; -.
DR OMA; MTQERAL; -.
DR PhylomeDB; Q99N28; -.
DR TreeFam; TF326804; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-420597; Nectin/Necl trans heterodimerization.
DR BioGRID-ORCS; 94332; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Cadm3; mouse.
DR PRO; PR:Q99N28; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q99N28; protein.
DR Bgee; ENSMUSG00000005338; Expressed in cerebellar cortex and 191 other tissues.
DR ExpressionAtlas; Q99N28; baseline and differential.
DR Genevisible; Q99N28; MM.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC-UCL.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:HGNC-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:HGNC-UCL.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 3.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR003585; Neurexin-like.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:Q8N126"
FT CHAIN 23..396
FT /note="Cell adhesion molecule 3"
FT /id="PRO_0000046068"
FT TOPO_DOM 23..328
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..124
FT /note="Ig-like V-type"
FT DOMAIN 128..226
FT /note="Ig-like C2-type 1"
FT DOMAIN 231..313
FT /note="Ig-like C2-type 2"
FT REGION 365..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 150..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 252..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 136
FT /note="Y->C: Nerves from mutant mice exhibit abnormal
FT axonal organization."
FT /evidence="ECO:0000269|PubMed:33889941"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:5ZO2"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:5ZO2"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:5ZO2"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:5ZO2"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:5ZO2"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:5ZO2"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5ZO2"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:5ZO2"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5ZO2"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:5ZO2"
SQ 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
