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Down syndrome cell adhesion molecule-like protein 1 (Down syndrome cell adhesion molecule 2, DSCAML1, DSCAM2, KIAA1132)
Function:
1) cell adhesion molecule
2) mediates cation-independent homophilic binding
3) nervous system development.
Compartment: membrane
Alternative splicing: named isoforms=2
Expression:
- expressed in heart, liver, pancreas, skeletal muscle, kidney, brain
- in brain, expressed in amygdala, caudate nucleus, corpus callosum, hippocampus, substantia nigra, thalamus, subthalamus
General
adhesion receptor
glycoprotein
Properties
SIZE: MW = 224 kD
entity length = 2053 aa
COMPARTMENT: plasma membrane
MOTIF: signal sequence {1-18}
immunoglobulin superfamily domain {19-119}
MOTIF: N-glycosylation site {N29}
cysteine residue {C47}
MODIFICATION: cysteine residue {C103}
N-glycosylation site {N79}
cysteine residue {C103}
MODIFICATION: cysteine residue {C47}
immunoglobulin superfamily domain {115-217}
MOTIF: cysteine residue {C146}
MODIFICATION: cysteine residue {C198}
cysteine residue {C198}
MODIFICATION: cysteine residue {C146}
immunoglobulin superfamily domain {226-306}
MOTIF: cysteine residue {C247}
MODIFICATION: cysteine residue {C294}
cysteine residue {C294}
MODIFICATION: cysteine residue {C247}
immunoglobulin superfamily domain {314-402}
MOTIF: cysteine residue {C336}
MODIFICATION: cysteine residue {C386}
N-glycosylation site {N368}
cysteine residue {C386}
MODIFICATION: cysteine residue {C336}
immunoglobulin superfamily domain {408-501}
MOTIF: cysteine residue {C429}
MODIFICATION: cysteine residue {C485}
N-glycosylation site {N471}
cysteine residue {C485}
MODIFICATION: cysteine residue {C429}
immunoglobulin superfamily domain {506-586}
MOTIF: N-glycosylation site {N513}
cysteine residue {C526}
MODIFICATION: cysteine residue {C575}
N-glycosylation site {N556}
cysteine residue {C575}
MODIFICATION: cysteine residue {C526}
immunoglobulin superfamily domain {596-685}
MOTIF: cysteine residue {C617}
MODIFICATION: cysteine residue {C669}
N-glycosylation site {N666}
cysteine residue {C669}
MODIFICATION: cysteine residue {C617}
immunoglobulin superfamily domain {690-784}
MOTIF: N-glycosylation site {N710}
cysteine residue {C711}
MODIFICATION: cysteine residue {C767}
N-glycosylation site {N749}
cysteine residue {C767}
MODIFICATION: cysteine residue {C711}
immunoglobulin superfamily domain {788-885}
MOTIF: N-glycosylation site {N796}
N-glycosylation site {N809}
cysteine residue {C810}
MODIFICATION: cysteine residue {C867}
cysteine residue {C867}
MODIFICATION: cysteine residue {C810}
fibronectin type III domain or F3 module {887-980}
MOTIF: N-glycosylation site {N926}
fibronectin type III domain or F3 module {986-1085}
MOTIF: N-glycosylation site {N1082}
fibronectin type III domain or F3 module {1090-1186}
MOTIF: N-glycosylation site {N1144}
N-glycosylation site {N1162}
fibronectin type III domain or F3 module {1191-1283}
MOTIF: N-glycosylation site {N1275}
immunoglobulin superfamily domain {1278-1377}
MOTIF: cysteine residue {C1311}
MODIFICATION: cysteine residue {C1363}
N-glycosylation site {N1345}
cysteine residue {C1363}
MODIFICATION: cysteine residue {C1311}
fibronectin type III domain or F3 module {1380-1474}
fibronectin type III domain or F3 module {1479-1569}
MOTIF: N-glycosylation site {N1492}
N-glycosylation site {N1531}
N-glycosylation site {N1561}
transmembrane domain {1592-1612}
proline-rich region
SITE: 1956-2016
MOTIF: proline residue (SEVERAL)
Database Correlations
UniProt Q8TD84
PFAM correlations
References
UniProt :accession Q8TD84