CAD18_HUMAN » Cadherin-18

CAD18_HUMAN » Cadherin-18
Magnify CAD18_HUMAN » Cadherin-18Enlarged view of image
3D view in GLMol or JMol

gray dot

Download Coordinates

gray dot

Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
CAD18_HUMAN » Cadherin-18 » Cadherin-14;
Hydrophobic Thickness 38.8 ± 3.4 Å
Tilt Angle 3 ± 2°
ΔGtransfer -62.1 kcal/mol
ΔGfold -32.2 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 611-636 (608-640)
Pathways

Cell-Cell communication (Reactome)

PDB none
OPM none
Complexes none
Interactions

CAD12, Complex: CAD18:CAD12, PubMed

CADH6, Complex: CADH6:CAD18, PubMed

CADH9, Complex: CAD18:CADH9, PubMed

Domains

AA: 59-150, PDBID: 3LND, Subunit B, Seq Identity:64%, Cadherin domain

AA: 164-259, PDBID: 3LND, Subunit B, Seq Identity:81%, Cadherin domain

AA: 273-374, PDBID: 2A62, Subunit A, Seq Identity:32%, Cadherin domain

AA: 388-479, PDBID: 4ZPL, Subunit A, Seq Identity:34%, Cadherin domain

AA: 492-589, PDBID: 4ZPM, Subunit A, Seq Identity:29%, Cadherin domain

AA: 637-784, PDBID: 1I7W, Subunit B, Seq Identity:44%, Cadherin cytoplasmic region

UniProt annotation for CAD18_HUMAN » Cadherin-18
FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.

DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.

UniProt features for CAD18_HUMAN » Cadherin-18
SIGNAL 1 24 Potential.
PROPEP 25 53 Potential.
CHAIN 54 790 Cadherin-18.
DOMAIN 54 159 Cadherin 1.
DOMAIN 160 268 Cadherin 2.
DOMAIN 269 383 Cadherin 3.
DOMAIN 384 486 Cadherin 4.
DOMAIN 487 608 Cadherin 5.
Amino Acid Sequence for CAD18_HUMAN » Cadherin-18
MKITSTSCIC PVLVCLCFVQ RCYGTAHHSS IKVMRNQTKH IEGETEVHHR PKRGWVWNQF FVLEEHMGPD PQYVGKLHSN SDKGDGSVKY ILTGEGAGTI FIIDDTTGDI HSTKSLDREQ KTHYVLHAQA IDRRTNKPLE PESEFIIKVQ DINDNAPKFT DGPYIVTVPE MSDMGTSVLQ VTATDADDPT YGNSARVVYS ILQGQPYFSV DPKTGVIRTA LHNMDREARE HYSVVIQAKD MAGQVGGLSG STTVNITLTD VNDNPPRFPQ KHYQLYVPES AQVGSAVGKI KANDADTGSN ADMTYSIING DGMGIFSIST DKETREGILS LKKPLNYEKK KSYTLNIEGA NTHLDFRFSH LGPFKDATML KIIVGDVDEP PLFSMPSYLM EVYENAKIGT VVGTVLAQDP DSTNSLVRYF INYNVEDDRF FNIDANTGTI RTTKVLDREE TPWYNITVTA SEIDNPDLLS HVTVGIRVLD VNDNPPELAR EYDIIVCENS KPGQVIHTIS ATDKDDFANG PRFNFFLDER LPVNPNFTLK DNEDNTASIL TRRRRFSRTV QDVYYLPIMI SDGGIPSLSS SSTLTIRVCA CERDGRVRTC HAEAFLSSAG LSTGALIAIL LCVLILLAIV VLFITLRRSK KEPLIISEED VRENVVTYDD EGGGEEDTEA FDITALRNPS AAEELKYRRD IRPEVKLTPR HQTSSTLESI DVQEFIKQRL AEADLDPSVP PYDSLQTYAY EGQRSEAGSI SSLDSATTQS DQDYHYLGDW GPEFKKLAEL YGEIESERTT