Cell adhesion molecule 1

UniProt data

UniProt name: CADM1_HUMAN (Q9BY67)

Gene name: CADM1 {ECO:0000312|HGNC:HGNC:5951}

Organism: Homo sapiens (Human).

Function: Mediates homophilic cell-cell adhesion in a Ca(2+)- independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and NECTIN3 in a Ca(2+)-independent manner. Acts as a tumor suppressor in non-small-cell lung cancer (NSCLC) cells. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. May contribute to the less invasive phenotypes of lepidic growth tumor cells. In mast cells, may mediate attachment to and promote communication with nerves. CADM1, together with MITF, is essential for development and survival of mast cells in vivo. Acts as a synaptic cell adhesion molecule and plays a role in the formation of dendritic spines and in synapse assembly (By similarity). May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa. {ECO:0000250, ECO:0000269|PubMed:11279526, ECO:0000269|PubMed:12050160, ECO:0000269|PubMed:12234973, ECO:0000269|PubMed:12920246, ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:15905536, ECO:0000269|PubMed:22438059}.

Subcellular location: Cell membrane {ECO:0000269|PubMed:11279526, ECO:0000269|PubMed:22438059}; Single-pass type I membrane protein {ECO:0000269|PubMed:11279526}. Cell junction, synapse {ECO:0000250|UniProtKB:Q8R5M8}. Note=Localized to the basolateral plasma membrane of epithelial cells in gall bladder. {ECO:0000250|UniProtKB:Q8R5M8}.

Transmembrane domains:

  1. 375-395, 21 AA, Helical. {ECO:0000255}.

Sequence: 442 AA

10 20 30 40 50 60 MASVVLPSGS QCAAAAAAAA PPGLRLRLLL LLFSAAALIP TGDGQNLFTK DVTVIEGEVA 70 80 90 100 110 120 TISCQVNKSD DSVIQLLNPN RQTIYFRDFR PLKDSRFQLL NFSSSELKVS LTNVSISDEG 130 140 150 160 170 180 RYFCQLYTDP PQESYTTITV LVPPRNLMID IQKDTAVEGE EIEVNCTAMA SKPATTIRWF 190 200 210 220 230 240 KGNTELKGKS EVEEWSDMYT VTSQLMLKVH KEDDGVPVIC QVEHPAVTGN LQTQRYLEVQ 250 260 270 280 290 300 YKPQVHIQMT YPLQGLTREG DALELTCEAI GKPQPVMVTW VRVDDEMPQH AVLSGPNLFI 310 320 330 340 350 360 NNLNKTDNGT YRCEASNIVG KAHSDYMLYV YDPPTTIPPP TTTTTTTTTT TTTILTIITD 370 380 390 400 410 420 SRAGEEGSIR AVDHAVIGGV VAVVVFAMLC LLIILGRYFA RHKGTYFTHE AKGADDAADA 430 440 DTAIINAEGG QNNSEEKKEY FI

CATM prediction

The sequence of CADM1_HUMAN returned 2 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
          380       390      
   +    |    +    |    +   		 (Å) (°) (Å) (°)  
Model 1 VDHAVIGGVVAVVVFAMLCLLIILGRY 6.9 -43.0° 4.5 35.0 -29.3
Model 2 VDHAVIGGVVAVVVFAMLCLLIILGRY 6.5 -55.0° 4.2 38.0 -9.3

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


Click on the image to enlarge

Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 378, GLY, HA1 A, 375, ALA, O 2.76Å
B, 379, GLY, HA2 A, 378, GLY, O 3.42Å
A, 378, GLY, HA1 B, 375, ALA, O 2.76Å
A, 379, GLY, HA2 B, 378, GLY, O 3.42Å