Sequence information
Variant position: 125 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 476 The length of the canonical sequence.
Location on the sequence:
PFTAMVSTPENRQTFITSVI
K FLRQYEFDGLDFDWEYPGSR
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human PFTAMVSTPENRQTFITSVIK FLRQYEFDGLDFDWEYPGSR
Mouse PFTTMVSTSQNRQTFITSVIK FLRQYGFDGLDLDWEYPGSR
Rat PFTTMVSTSQNRQTFITSVIK FLRQYGFDGLDLDWEYPGSR
Bovine PFTAMVATPENRKTFISSVIK FLHQYGFDGLDFDWEYPGFR
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
Chain
22 – 476
Acidic mammalian chitinase
Domain
22 – 390
GH18
Active site
140 – 140
Proton donor
Binding site
141 – 141
Chitooligosaccharide
Disulfide bond
49 – 394
Alternative sequence
1 – 161
Missing. In isoform 3.
Mutagenesis
138 – 138
D -> A. Loss of chitinase activity. No effect on protection against apoptosis or on AKT1 activation.
Helix
113 – 130
Literature citations
Differential enzymatic activity of common haplotypic versions of the human acidic mammalian chitinase protein.
Seibold M.A.; Reese T.A.; Choudhry S.; Salam M.T.; Beckman K.; Eng C.; Atakilit A.; Meade K.; Lenoir M.; Watson H.G.; Thyne S.; Kumar R.; Weiss K.B.; Grammer L.C.; Avila P.; Schleimer R.P.; Fahy J.V.; Rodriguez-Santana J.; Rodriguez-Cintron W.; Boot R.G.; Sheppard D.; Gilliland F.D.; Locksley R.M.; Burchard E.G.;
J. Biol. Chem. 284:19650-19658(2009)
Cited for: VARIANTS ASP-45; ASN-47; MET-61; ARG-102; ARG-125; VAL-339; SER-354 AND GLY-432; CATALYTIC ACTIVITY; FUNCTION; CHARACTERIZATION OF VARIANTS ASP-45; ASN-47 AND MET-61;
Disclaimer:
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.