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vasorin (protein Slit-like 2, VASN, SLITL2, UNQ314/PRO357/PRO1282)
Function:
1) inhibitor of TGF-beta signaling (putative)
2) interacts with TGFB1, TGFB2 & TGFB3
Structure:
1) N-glycosylated
2) contains 1 EGF-like domain.
3) contains 11 LRR repeats (leucine-rich repeats)
Compartment: membrane, secreted
Expression:
- expressed in aorta > kidney, placenta > brain, heart, liver, lung, skeletal muscle
- within aorta, strongest expression in tunica media
- within kidney, expressed in interstitial cells
General
glycoprotein
membrane protein
secreted protein
Properties
SIZE: MW = 72 kD
entity length = 673 aa
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-23}
leucine-rich repeat
SITE: 51-74
MOTIF: leucine residue (SEVERAL)
leucine-rich repeat
SITE: 75-98
MOTIF: leucine residue (SEVERAL)
leucine-rich repeat
SITE: 100-122
MOTIF: leucine residue (SEVERAL)
N-glycosylation site {N101}
N-glycosylation site {N117}
leucine-rich repeat
SITE: 123-146
MOTIF: leucine residue (SEVERAL)
leucine-rich repeat
SITE: 148-168
MOTIF: leucine residue (SEVERAL)
leucine-rich repeat
SITE: 169-191
MOTIF: leucine residue (SEVERAL)
leucine-rich repeat
SITE: 193-214
MOTIF: leucine residue (SEVERAL)
leucine-rich repeat
SITE: 215-240
MOTIF: leucine residue (SEVERAL)
leucine-rich repeat
SITE: 241-263
MOTIF: leucine residue (SEVERAL)
leucine-rich repeat
SITE: 264-289
MOTIF: leucine residue (SEVERAL)
N-glycosylation site {N273}
leucine-rich repeat
SITE: 290-310
MOTIF: leucine residue (SEVERAL)
EGF domain {405-442}
MOTIF: cysteine residue {C409}
MODIFICATION: cysteine residue {C420}
cysteine residue {C414}
MODIFICATION: cysteine residue {C430}
cysteine residue {C420}
MODIFICATION: cysteine residue {C409}
cysteine residue {C430}
MODIFICATION: cysteine residue {C414}
cysteine residue {C432}
MODIFICATION: cysteine residue {C441}
cysteine residue {C441}
MODIFICATION: cysteine residue {C432}
fibronectin type III domain or F3 module {458-555}
MOTIF: N-glycosylation site {N500}
N-glycosylation site {N528}
transmembrane domain {576-596}
Database Correlations
OMIM 608843
UniProt Q6EMK4
PFAM correlations
References
UniProt :accession Q6EMK4