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roundabout homolog 1 (H-Robo-1, deleted in U twenty twenty, ROBO1, DUTT1)
Function:
1) receptor for SLIT1 & SLIT2
2) molecular guidance in cellular migration
- axonal navigation at the ventral midline of the neural tube
- projection of axons to different regions during neuronal development
3) in axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex
4) lung development ?
Structure:
1) belongs to the immunoglobulin superfamily, ROBO family
2) contains 3 fibronectin F3 modules
- contains 5 Ig-like C2-type domains (immunoglobulin-like)
Compartment: membrane
Alternative splicing: named isoforms=3
Expression: widely expressed, with exception of kidney
Pathology:
- defects in ROBO1 may be a cause of breast cancer & small cell lung cancer
General
membrane protein
phosphoprotein
receptor
Properties
SIZE: MW = 181 kD
entity length = 1651 aa
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-25}
immunoglobulin superfamily domain {68-164}
MOTIF: cysteine residue {C89}
MODIFICATION: cysteine residue {C147}
cysteine residue {C147}
MODIFICATION: cysteine residue {C89}
N-glycosylation site {N160}
immunoglobulin superfamily domain {170-257}
MOTIF: cysteine residue {C191}
MODIFICATION: cysteine residue {C240}
cysteine residue {C240}
MODIFICATION: cysteine residue {C191}
immunoglobulin superfamily domain {262-346}
MOTIF: cysteine residue {C283}
MODIFICATION: cysteine residue {C330}
cysteine residue {C330}
MODIFICATION: cysteine residue {C283}
immunoglobulin superfamily domain {351-446}
MOTIF: cysteine residue {C372}
MODIFICATION: cysteine residue {C428}
cysteine residue {C428}
MODIFICATION: cysteine residue {C372}
immunoglobulin superfamily domain {455-541}
MOTIF: N-glycosylation site {N463}
cysteine residue {C476}
MODIFICATION: cysteine residue {C525}
cysteine residue {C525}
MODIFICATION: cysteine residue {C476}
fibronectin type III domain or F3 module {561-646}
fibronectin type III domain or F3 module {673-763}
fibronectin type III domain or F3 module {775-864}
MOTIF: N-glycosylation site {N790}
N-glycosylation site {N820}
N-glycosylation site {N827}
transmembrane domain {898-918}
Tyr phosphorylation site {Y1038}
Tyr phosphorylation site {Y1073}
Tyr phosphorylation site {Y1114}
Database Correlations
OMIM 602430
UniProt Q9Y6N7
PFAM correlations
References
UniProt :accession Q9Y6N7