Sequence information
Variant position: 358 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 468 The length of the canonical sequence.
Location on the sequence:
KDDDNILFRDSANATSLPVQ
D SSSVPLPTFLVAGGSLAFGT
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 KDDDNILFRDSANATSL--PVQD SSSVPLPTFLVAGGSLAFGT
Mouse SANHEDQYESSTEATSVLAPVQE SSSMSLPTFLVAGGSLAF
Rat YDNHEDQYGSSTEATSVLAPVQG SSPIPLPTFLVAGGSLAF
Pig EDDEDISSKESANATSL--PVQD SASVPLPTFLVAGGSLAF
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
20 – 468
Interleukin-6 receptor subunit alpha
Topological domain
20 – 365
Extracellular
Glycosylation
350 – 350
N-linked (GlcNAc...) asparagine
Glycosylation
352 – 352
O-linked (GlcNAc) threonine
Alternative sequence
356 – 365
VQDSSSVPLP -> GSRRRGSCGL. In isoform 2.
Mutagenesis
350 – 350
N -> A. No effect on IL6R signaling; when associated with A-55, A-93, A-221 and A-245. Loss of cleavage by ADAM17; when associated with A-55, A-93, A-221 and A-245.
Mutagenesis
352 – 352
T -> A. No effect on IL6R signaling.
Mutagenesis
355 – 355
P -> ID. Reduces cleavage by ADAM17.
Mutagenesis
356 – 356
V -> EG. Abolishes cleavage by ADAM17.
Literature citations
Complete sequencing and characterization of 21,243 full-length human cDNAs.
Ota T.; Suzuki Y.; Nishikawa T.; Otsuki T.; Sugiyama T.; Irie R.; Wakamatsu A.; Hayashi K.; Sato H.; Nagai K.; Kimura K.; Makita H.; Sekine M.; Obayashi M.; Nishi T.; Shibahara T.; Tanaka T.; Ishii S.; Yamamoto J.; Saito K.; Kawai Y.; Isono Y.; Nakamura Y.; Nagahari K.; Murakami K.; Yasuda T.; Iwayanagi T.; Wagatsuma M.; Shiratori A.; Sudo H.; Hosoiri T.; Kaku Y.; Kodaira H.; Kondo H.; Sugawara M.; Takahashi M.; Kanda K.; Yokoi T.; Furuya T.; Kikkawa E.; Omura Y.; Abe K.; Kamihara K.; Katsuta N.; Sato K.; Tanikawa M.; Yamazaki M.; Ninomiya K.; Ishibashi T.; Yamashita H.; Murakawa K.; Fujimori K.; Tanai H.; Kimata M.; Watanabe M.; Hiraoka S.; Chiba Y.; Ishida S.; Ono Y.; Takiguchi S.; Watanabe S.; Yosida M.; Hotuta T.; Kusano J.; Kanehori K.; Takahashi-Fujii A.; Hara H.; Tanase T.-O.; Nomura Y.; Togiya S.; Komai F.; Hara R.; Takeuchi K.; Arita M.; Imose N.; Musashino K.; Yuuki H.; Oshima A.; Sasaki N.; Aotsuka S.; Yoshikawa Y.; Matsunawa H.; Ichihara T.; Shiohata N.; Sano S.; Moriya S.; Momiyama H.; Satoh N.; Takami S.; Terashima Y.; Suzuki O.; Nakagawa S.; Senoh A.; Mizoguchi H.; Goto Y.; Shimizu F.; Wakebe H.; Hishigaki H.; Watanabe T.; Sugiyama A.; Takemoto M.; Kawakami B.; Yamazaki M.; Watanabe K.; Kumagai A.; Itakura S.; Fukuzumi Y.; Fujimori Y.; Komiyama M.; Tashiro H.; Tanigami A.; Fujiwara T.; Ono T.; Yamada K.; Fujii Y.; Ozaki K.; Hirao M.; Ohmori Y.; Kawabata A.; Hikiji T.; Kobatake N.; Inagaki H.; Ikema Y.; Okamoto S.; Okitani R.; Kawakami T.; Noguchi S.; Itoh T.; Shigeta K.; Senba T.; Matsumura K.; Nakajima Y.; Mizuno T.; Morinaga M.; Sasaki M.; Togashi T.; Oyama M.; Hata H.; Watanabe M.; Komatsu T.; Mizushima-Sugano J.; Satoh T.; Shirai Y.; Takahashi Y.; Nakagawa K.; Okumura K.; Nagase T.; Nomura N.; Kikuchi H.; Masuho Y.; Yamashita R.; Nakai K.; Yada T.; Nakamura Y.; Ohara O.; Isogai T.; Sugano S.;
Nat. Genet. 36:40-45(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2); VARIANT ALA-358;
Proteolytic Origin of the Soluble Human IL-6R In Vivo and a Decisive Role of N-Glycosylation.
Riethmueller S.; Somasundaram P.; Ehlers J.C.; Hung C.W.; Flynn C.M.; Lokau J.; Agthe M.; Duesterhoeft S.; Zhu Y.; Groetzinger J.; Lorenzen I.; Koudelka T.; Yamamoto K.; Pickhinke U.; Wichert R.; Becker-Pauly C.; Raedisch M.; Albrecht A.; Hessefort M.; Stahnke D.; Unverzagt C.; Rose-John S.; Tholey A.; Garbers C.;
PLoS Biol. 15:e2000080-e2000080(2017)
Cited for: FUNCTION; PROTEOLYTIC CLEAVAGE; TISSUE SPECIFICITY (ISOFORM 2); GLYCOSYLATION AT ASN-55; ASN-93; ASN-221; ASN-245; ASN-350 AND THR-352; MUTAGENESIS OF ASN-55; THR-57; ASN-93; ASN-221; ASN-245; ASN-350; THR-352; 355-PRO-VAL-356; PRO-355 AND VAL-356; CHARACTERIZATION OF VARIANT ALA-358; SUBCELLULAR LOCATION;
Admixture mapping of an allele affecting interleukin 6 soluble receptor and interleukin 6 levels.
Reich D.; Patterson N.; Ramesh V.; De Jager P.L.; McDonald G.J.; Tandon A.; Choy E.; Hu D.; Tamraz B.; Pawlikowska L.; Wassel-Fyr C.; Huntsman S.; Waliszewska A.; Rossin E.; Li R.; Garcia M.; Reiner A.; Ferrell R.; Cummings S.; Kwok P.Y.; Harris T.; Zmuda J.M.; Ziv E.;
Am. J. Hum. Genet. 80:716-726(2007)
Cited for: POLYMORPHISM; VARIANT ALA-358; ASSOCIATION OF VARIANT ALA-358 WITH IL6 AND SOLUBLE IL6R SERUM LEVELS;
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.