ID   CADM3_XENLA             Reviewed;         394 AA.
AC   Q7ZXX1;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Cell adhesion molecule 3;
DE   AltName: Full=Immunoglobulin superfamily member 4B;
DE            Short=IgSF4B;
DE   Flags: Precursor;
GN   Name=cadm3; Synonyms=igsf4b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the cell-cell adhesion. {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   -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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DR   EMBL; BC044084; AAH44084.1; -; mRNA.
DR   RefSeq; NP_001080468.1; NM_001086999.1.
DR   AlphaFoldDB; Q7ZXX1; -.
DR   SMR; Q7ZXX1; -.
DR   DNASU; 380160; -.
DR   GeneID; 380160; -.
DR   CTD; 380160; -.
DR   Xenbase; XB-GENE-1012968; cadm3.S.
DR   OrthoDB; 716894at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 380160; Expressed in brain and 9 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cell adhesion; Cell junction; Cell membrane; Disulfide bond;
KW   Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..394
FT                   /note="Cell adhesion molecule 3"
FT                   /id="PRO_0000046069"
FT   TOPO_DOM        18..326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        348..394
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..120
FT                   /note="Ig-like V-type"
FT   DOMAIN          128..223
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          228..306
FT                   /note="Ig-like C2-type 2"
FT   REGION          217..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        45..105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        147..204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        249..295
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   394 AA;  42730 MW;  F1141D8E6B69254A CRC64;
     MHHPVILLLC LSSLAGAANL PPEDLSQPVT ADVIVPTGGT AILKCTVQEH LESSLQWSNT
     AQQTLYFGEK RALRDNRIQL VHSSPNELTI SISNVVLSDE GEYTCSIFTM PVRTAKAVVT
     VLGVPQKPQV SGFESAFKEN DKAKLRCTTS GSKPAANIKW YKGPEELEGA KTSVLEDGNG
     KTFTVKSFIE FDVTKDDDGA EITCAVGHES LHDSAKSSSH KIQVQYKPTA KIESRPSMPR
     EGDKLRLQCD AYGNPVPDNY VWERENGEVP LLANIEGNSL VFFNLNKTDS GTYTCKASNT
     LGTFITHYKL DVNDPSPIPS TSSIDHAVIG GVVAVIAFLL FCLLIVLGRY LIRHKGTYLT
     HEAKGSDDAP DADTAIINAE GGQGGSDDKK EYFI