CADM3_RAT
ID CADM3_RAT Reviewed; 396 AA.
AC Q1WIM3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Flags: Precursor;
GN Name=Cadm3; Synonyms=Igsf4b, Necl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Maurel P., Einheber S., Rubin M.B., Galinska J., Thaker P., Murakami Y.,
RA Salzer J.L.;
RT "The nectin-like proteins: candidate cell adhesion molecules to mediate
RT axo-glial interactions.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Can form trans-heterodimers with NECTIN3. Interacts
CC with EPB41L1, DLG3, PALS2 and CASK (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99N28};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99N28}.
CC Cell junction {ECO:0000250|UniProtKB:Q99N28}.
CC -!- DOMAIN: The cytoplasmic region mediates interaction with EPB41L1, DLG3,
CC PALS2 and CASK. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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DR EMBL; DQ272743; ABB85362.1; -; mRNA.
DR RefSeq; NP_001040568.1; NM_001047103.1.
DR AlphaFoldDB; Q1WIM3; -.
DR SMR; Q1WIM3; -.
DR BioGRID; 262276; 2.
DR STRING; 10116.ENSRNOP00000004613; -.
DR GlyGen; Q1WIM3; 1 site.
DR iPTMnet; Q1WIM3; -.
DR PhosphoSitePlus; Q1WIM3; -.
DR PaxDb; Q1WIM3; -.
DR PRIDE; Q1WIM3; -.
DR GeneID; 360882; -.
DR KEGG; rno:360882; -.
DR UCSC; RGD:1307035; rat.
DR CTD; 57863; -.
DR RGD; 1307035; Cadm3.
DR VEuPathDB; HostDB:ENSRNOG00000003365; -.
DR eggNOG; ENOG502QWJ8; Eukaryota.
DR HOGENOM; CLU_047574_1_0_1; -.
DR InParanoid; Q1WIM3; -.
DR PhylomeDB; Q1WIM3; -.
DR TreeFam; TF326804; -.
DR Reactome; R-RNO-418990; Adherens junctions interactions.
DR Reactome; R-RNO-420597; Nectin/Necl trans heterodimerization.
DR PRO; PR:Q1WIM3; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003365; Expressed in cerebellum and 19 other tissues.
DR ExpressionAtlas; Q1WIM3; baseline and differential.
DR Genevisible; Q1WIM3; RN.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
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 Calcium; Cell adhesion; Cell junction; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; 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_0000247989"
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:22673903"
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"
SQ SEQUENCE 396 AA; 42906 MW; 6F9C38384CD0E3BD CRC64;
MGAPSALPLL LLLACSWAPG GANLSQDDSQ PWTSDETVVA GGTVVLKCQV KDHEDSSLQW
SNPAQQTLYF GEKRALRDNR IQLVSSTPHE LSISISNVAL ADEGEYTCSI FTMPVRTAKS
LVTVLGIPQK PIITGYKSSL REKETATLNC QSSGSKPAAQ LAWRKGDQEL HGDQTRIQED
PNGKTFTVSS SVSFQVTRDD DGANVVCSVN HESLKGADRS TSQRIEVLYT PTAMIRPEPA
HPREGQKLLL HCEGRGNPVP QQYVWVKEGS EPPLKMTQES ALIFPFLNKS DSGTYGCTAT
SNMGSYTAYF TLNVNDPSPV PSSSSTYHAI IGGIVAFIVF LLLILLIFLG HYLIRHKGTY
LTHEAKGSDD APDADTAIIN AEGGQSGGDD KKEYFI
