ID   CADM2_XENTR             Reviewed;         433 AA.
AC   Q6DJ83;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Cell adhesion molecule 2;
DE   AltName: Full=Immunoglobulin superfamily member 4D;
DE            Short=IgSF4D;
DE   Flags: Precursor;
GN   Name=cadm2; Synonyms=igsf4d;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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DR   EMBL; BC075300; AAH75300.1; -; mRNA.
DR   RefSeq; NP_001005713.1; NM_001005713.1.
DR   AlphaFoldDB; Q6DJ83; -.
DR   SMR; Q6DJ83; -.
DR   STRING; 8364.ENSXETP00000041944; -.
DR   PaxDb; Q6DJ83; -.
DR   DNASU; 448238; -.
DR   GeneID; 448238; -.
DR   KEGG; xtr:448238; -.
DR   CTD; 253559; -.
DR   Xenbase; XB-GENE-998536; cadm2.
DR   eggNOG; ENOG502QV9X; Eukaryota.
DR   HOGENOM; CLU_047574_2_1_1; -.
DR   InParanoid; Q6DJ83; -.
DR   OrthoDB; 716894at2759; -.
DR   Reactome; R-XTR-418990; Adherens junctions interactions.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000026489; Expressed in brain and 4 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0032809; C:neuronal cell body membrane; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
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; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR003585; Neurexin-like.
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; 3.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..433
FT                   /note="Cell adhesion molecule 2"
FT                   /id="PRO_0000291973"
FT   TOPO_DOM        25..365
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        387..433
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..114
FT                   /note="Ig-like V-type"
FT   DOMAIN          127..217
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          227..312
FT                   /note="Ig-like C2-type 2"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        44..104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        146..203
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        248..296
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   433 AA;  47302 MW;  D90D903B1A5410FF CRC64;
     MILQPSALLC LSSLWGVIVQ ASQGQFPVTQ NVTVVEGGTI NLTCRVDQND NTSLQWSNPA
     QQTLYFDDKK ALRDNRIELV RASWHELSIS ISDVSLSDEG QYTCSLFTMP VKTSKAYLMV
     LGVPENPHIS GFTSPVMEGD TIQLTCKSSG SKPAADIRWF KNDQEITDVQ KIQQQDSNGK
     TFTVTSSLVF QGDRKDDGAV IRCRVDHESL TSTPQIAKQV LEIHYTPTVR ILPSTPLPQE
     GQPLILICES KGKPLPEPVL WTKDGGELPD PERMTVNGRE LTISFLNKTD NGTYRCEATN
     SIGQSSAEYV LIINDVPKPL FPTTIIPLFT SATVKTNVAM STRTTKSAFI TKDPNALPGP
     VATDHALIGG VVAVVVFVTL CSIILIGRYL ARHKGTYLTN EAKGAEDAPD ADTAIINAEG
     SQVNAEEKKE YFI