Variant position: 708 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1047 The length of the canonical sequence.
Location on the sequence:
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 APELLSGNPLPTTGMQKADV YSFGIILQEIALRSGPFYLEG
Mouse APELLSGNPLPTTGMQKADV YSFAIILQEIALRSGPFYLEG
Rat APELLSGNPLPTTGMQKADV YSFAIILQEIALRSGPFYLEG
Bovine APELLSGNPLPTTGMQKADV YSFGIILQEIALRSGPFYLEG
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
23 – 1047 Atrial natriuretic peptide receptor 2
479 – 1047 Cytoplasmic
513 – 786 Protein kinase
Mutations in the transmembrane natriuretic peptide receptor NPR-B impair skeletal growth and cause acromesomelic dysplasia, type Maroteaux.
Bartels C.F.; Buekuelmez H.; Padayatti P.; Rhee D.K.; van Ravenswaaij-Arts C.; Pauli R.M.; Mundlos S.; Chitayat D.; Shih L.-Y.; Al-Gazali L.I.; Kant S.; Cole T.; Morton J.; Cormier-Daire V.; Faivre L.; Lees M.; Kirk J.; Mortier G.R.; Leroy J.; Zabel B.; Kim C.A.; Crow Y.; Braverman N.E.; van den Akker F.; Warman M.L.;
Am. J. Hum. Genet. 75:27-34(2004)
Cited for: FUNCTION; VARIANTS AMDM THR-32; GLY-115; GLU-176; MET-297; CYS-338; THR-409; GLU-413; CYS-708; TRP-776; CYS-957 AND ALA-959; CHARACTERIZATION OF VARIANTS AMDM GLY-115; MET-297 AND GLU-413;
Catalytically active guanylyl cyclase b requires endoplasmic reticulum-mediated glycosylation, and mutations that inhibit this process cause dwarfism.
Dickey D.M.; Edmund A.B.; Otto N.M.; Chaffee T.S.; Robinson J.W.; Potter L.R.;
J. Biol. Chem. 291:11385-11393(2016)
Cited for: CHARACTERIZATION OF VARIANTS AMDM PHE-658; CYS-708; TRP-776 AND ALA-959; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; TOPOLOGY; GLYCOSYLATION; PHOSPHORYLATION; MUTAGENESIS OF ASN-24;
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