ID   CADM4_XENLA             Reviewed;         390 AA.
AC   Q66KX2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Cell adhesion molecule 4;
DE   AltName: Full=Immunoglobulin superfamily member 4C;
DE            Short=IgSF4C;
DE   Flags: Precursor;
GN   Name=cadm4; Synonyms=igsf4c;
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=Tadpole;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the cell-cell adhesion. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC078527; AAH78527.1; -; mRNA.
DR   RefSeq; NP_001087300.1; NM_001093831.2.
DR   AlphaFoldDB; Q66KX2; -.
DR   SMR; Q66KX2; -.
DR   DNASU; 447122; -.
DR   GeneID; 447122; -.
DR   KEGG; xla:447122; -.
DR   CTD; 447122; -.
DR   Xenbase; XB-GENE-992662; cadm4.L.
DR   OrthoDB; 716894at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 447122; Expressed in brain and 18 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR028807; Cadm4.
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; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR003585; Neurexin-like.
DR   PANTHER; PTHR45889:SF3; PTHR45889:SF3; 1.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..390
FT                   /note="Cell adhesion molecule 4"
FT                   /id="PRO_0000291983"
FT   TOPO_DOM        28..326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        348..390
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..122
FT                   /note="Ig-like V-type"
FT   DOMAIN          127..219
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          226..309
FT                   /note="Ig-like C2-type 2"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        47..107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        148..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        247..293
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   390 AA;  43411 MW;  F262D00DFB8327D0 CRC64;
     MAPALTALNR CFVLGILLLV TAGTAFSQEV QAENVTVVEG STVEISCHLH QYDGSIVVIQ
     NPVRQTLFFN GTRALKDTRF QLVEFTQKVV KIHLSDAKLE DEGGYFCQLY TEDTHHQIAT
     LTVIVPPDNP LVEVKEQAVE GGEIELTCIS PRTKPAATLR WYRDRKELKG FTSKQENGKT
     FSITNSIRFN VDRKDDGNIV TCEASHPALK GQKKQTQYEL DVQFSPTASI QPSQSLVRDG
     DELNLKCEVT GNPRPTEIIW TRLNDSLPDR AQIQGDLLSF PSLNLQDNGT YSCQVSNKHG
     RSSDQYVLVV YDPGAIIEAQ TQVPYAVIGG ILALLVFLVI CILIVMVWCS VRQKGSYLTH
     EASGLDEHGE AREAFLNGGE NHKRKEEFFI