Variant position: 191 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 411 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 YRVLHWENPVVSSQFYGALL GTVCMLYLLPLCWVLTLLNST
Mouse YRVLHWENPVVSSQFYGALL GMVCMLYLLPLCWVLALLNST
Rat YRVLHWENPVVSSQFYGALL GMVCMLYLLPLCWVLALLNST
Bovine YRVLHWENPAVSSQFYGALL GTVCMLYLLPLCWVLALLNST
Chicken YRVLYWENPTVSSQFYGALL GSVCILYLLPLCWVMAILNST
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
1 – 411 Protrudin
188 – 208 Helical
1 – 205 Sufficient for localization to endoplasmic reticulum tubular network and for interactions with REEP1, REEP5, ATL1, ATL2, ATL3 and SPAST
ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia.
Mannan A.U.; Krawen P.; Sauter S.M.; Boehm J.; Chronowska A.; Paulus W.; Neesen J.; Engel W.;
Am. J. Hum. Genet. 79:351-357(2006)
Cited for: VARIANT SPG33 VAL-191; CHARACTERIZATION OF VARIANT SPG33 VAL-191; SUBCELLULAR LOCATION; INTERACTION WITH SPAST;
The role of ZFYVE27/protrudin in hereditary spastic paraplegia.
Martignoni M.; Riano E.; Rugarli E.I.;
Am. J. Hum. Genet. 83:127-130(2008)
Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191;
Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation.
Chang J.; Lee S.; Blackstone C.;
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013)
Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191; FUNCTION; SUBUNIT; SUBCELLULAR LOCATION; TOPOLOGY; INTERACTION WITH REEP1; REEP5; ATL1; ATL2; ATL3 AND SPAST;
Protrudin regulates endoplasmic reticulum morphology and function associated with the pathogenesis of hereditary spastic paraplegia.
Hashimoto Y.; Shirane M.; Matsuzaki F.; Saita S.; Ohnishi T.; Nakayama K.I.;
J. Biol. Chem. 289:12946-12961(2014)
Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191; FUNCTION; SUBCELLULAR LOCATION; INTERACTION WITH REEP1; REEP5 AND ATL1;
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.