ID   A0A9L0IX39_EQUAS        Unreviewed;       390 AA.
AC   A0A9L0IX39;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   02-SEP-2026, entry version 15.
DE   RecName: Full=Cell adhesion molecule 1 {ECO:0000256|ARBA:ARBA00068781};
DE   AltName: Full=Synaptic cell adhesion molecule {ECO:0000256|ARBA:ARBA00080773};
GN   Name=CADM1 {ECO:0000313|Ensembl:ENSEASP00005045449.1};
OS   Equus asinus (Donkey) (Equus africanus asinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9793 {ECO:0000313|Ensembl:ENSEASP00005045449.1, ECO:0000313|Proteomes:UP000694387};
RN   [1] {ECO:0000313|Ensembl:ENSEASP00005045449.1, ECO:0000313|Proteomes:UP000694387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=33293529;
RA   Wang, C., Li, H., Guo, Y., Huang, J., Sun, Y., Min, J., Wang, J., Fang, X.,
RA   Zhao, Z., Wang, S., Zhang, Y., Liu, Q., Jiang, Q., Wang, X., Guo, Y., Yang,
RA   C., Wang, Y., Tian, F., Zhuang, G., Fan, Y., Gao, Q., Li, Y., Ju, Z., Li,
RA   J., Li, R., Hou, M., Yang, G., Liu, G., Liu, W., Guo, J., Pan, S., Fan, G.,
RA   Zhang, W., Zhang, R., Yu, J., Zhang, X., Yin, Q., Ji, C., Jin, Y., Yue, G.,
RA   Liu, M., Xu, J., Liu, S., Jordana, J., Noce, A., Amills, M., Wu, D.D., Li,
RA   S., Zhou, X. and Zhong, J.;
RT   "Donkey genomes provide new insights into domestication and selection for
RT   coat color.";
RL   Nat. Commun. 11:6014-6014(2020).
RN   [2] {ECO:0000313|Ensembl:ENSEASP00005045449.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- SUBUNIT: Homodimer (via Ig-like V-type domain). Interacts with FARP1.
CC       Interacts (via Ig-like V-type domain) with CRTAM (via Ig-like V-type
CC       domain); the interaction competes with CRTAM homodimerization and CADM1
CC       homodimerization. Interacts (via C-terminus) with EPB41L3/DAL1. The
CC       interaction with EPB41L3/DAL1 may act to anchor CADM1 to the actin
CC       cytoskeleton. Interacts (via C-terminus) with MPP2 (via PDZ domain).
CC       Interacts (via C-terminus) with MPP3 (via PDZ domain); this interaction
CC       connects CADM1 with DLG1. Interacts (via C-terminus) with PALS2 (via
CC       PDZ domain). {ECO:0000256|ARBA:ARBA00063829}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Synapse {ECO:0000256|ARBA:ARBA00034103}.
CC   -!- SIMILARITY: Belongs to the nectin family.
CC       {ECO:0000256|ARBA:ARBA00007810}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00114}.
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DR   AlphaFoldDB; A0A9L0IX39; -.
DR   Ensembl; ENSEAST00005076104.1; ENSEASP00005045449.1; ENSEASG00005006655.2.
DR   GeneTree; ENSGT00940000156093; -.
DR   Proteomes; UP000694387; Chromosome 20.
DR   GO; GO:0043005; C:neuron projection; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:TreeGrafter.
DR   GO; GO:0008037; P:cell recognition; IEA:TreeGrafter.
DR   GO; GO:0051606; P:detection of stimulus; IEA:TreeGrafter.
DR   GO; GO:0007156; P:homophilic cell-cell adhesion; IEA:TreeGrafter.
DR   GO; GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; IEA:TreeGrafter.
DR   CDD; cd05883; IgI_2_Necl-2; 1.
DR   CDD; cd05881; IgV_1_Necl-2; 1.
DR   FunFam; 2.60.40.10:FF:000013; cell adhesion molecule 1 isoform X1; 1.
DR   FunFam; 2.60.40.10:FF:000200; cell adhesion molecule 1 isoform X1; 1.
DR   FunFam; 2.60.40.10:FF:000184; cell adhesion molecule 1 isoform X2; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR45889:SF2; CELL ADHESION MOLECULE 1; 1.
DR   PANTHER; PTHR45889; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319, ECO:0000256|PROSITE-
KW   ProRule:PRU00114};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694387};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..47
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           48..390
FT                   /note="Cell adhesion molecule 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5040254461"
FT   TRANSMEM        350..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          43..142
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          147..241
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          246..320
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
SQ   SEQUENCE   390 AA;  42955 MW;  10E6A23A6C9E82BD CRC64;
     MASAVLPSGS QCAAAAAVAA AAAPPGLRLR LLLLLLSAAA LIPTGDGQNL FTKDVTVIEG
     EVATISCQVN KSDDSVIQLL NPNRQTIYFR DFRPLKDSRF QLLNFSSSEL KVSLTNVSIS
     DEGRYFCQLY TDPPQESYTT ITVLVPPRNL MIDIQKDTVV EGEEIEVNCT AMASKPATTI
     RWFKGNKELK GKSEVEEWSD MYTVTSQLML KVHKEDDGVP VICQVEHPAV TGNLQTQRYL
     EVQYKPQVHI QMTYPLQGLT REGDALELTC EAIGKPQPVM VTWVRVDDEM PQHAVLSGPN
     LFINNLNKTD NGTYRCEASN IVGKAHSDYM LYVYDSRAGE EGAIRAVDHA VIGGVVAVVV
     FAMLCLLIIL GRYFARHKGL FSLTSSPRIK
//