UniProtKB/Swiss-Prot Q9NPH5: Variant p.Met315Ile

NADPH oxidase 4
Gene: NOX4
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Variant information Variant position:

315 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B The variants are classified into three categories: LP/P, LB/B and US.

LP/P: likely pathogenic or pathogenic.
LB/B: likely benign or benign.
US: uncertain significance

Residue change:

From Methionine (M) to Isoleucine (I) at position 315 (M315I, p.Met315Ile). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:

Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:

Lowest score: -4 (low probability of substitution).
Highest score: 11 (high probability of substitution).

More information can be found on the following page
Other resources:

Links to websites of interest for the variant.

Variant rs317139 [ dbSNP | Ensembl ]

Sequence information Variant position:

315 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

578 The length of the canonical sequence.
Location on the sequence:

CAERLYRYIRSNKPVTIISV M SHPSDVMEIRMVKENFKARP 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                         CAERLYRYIRSNKPVTIISVMSHPSDVMEIRMVKENFKARP

Mouse                         CAERLYRCIRSNKPVTIISVINHPSDVMELRMIKENFKARP

Rat                           CAERLYRCIRSNKPVTIISVINHPSDVMELRMIKENFKARP

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	1 – 578	NADPH oxidase 4
Topological domain	210 – 424	Extracellular
Domain	304 – 419	FAD-binding FR-type
Region	248 – 575	Mediates interaction with TLR4
Alternative sequence	52 – 358	Missing. In isoform 3 and isoform 4.
Alternative sequence	55 – 578	Missing. In isoform 7.
Alternative sequence	225 – 578	Missing. In isoform 5.
Mutagenesis	304 – 304	R -> RGT. Partial loss of catalytic activity. No effect on CYBA localization.

Literature citations
Identification of renox, an NAD(P)H oxidase in kidney.
Geiszt M.; Kopp J.B.; Varnai P.; Leto T.L.;
Proc. Natl. Acad. Sci. U.S.A. 97:8010-8014(2000)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); DEVELOPMENTAL STAGE; VARIANT ILE-315; FUNCTION; CATALYTIC ACTIVITY; Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5.
Cheng G.; Cao Z.; Xu X.; van Meir E.G.; Lambeth J.D.;
Gene 269:131-140(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); TISSUE SPECIFICITY; DEVELOPMENTAL STAGE; VARIANT ILE-315; A novel superoxide-producing NAD(P)H oxidase in kidney.
Shiose A.; Kuroda J.; Tsuruya K.; Hirai M.; Hirakata H.; Naito S.; Hattori M.; Sakaki Y.; Sumimoto H.;
J. Biol. Chem. 276:1417-1423(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); FUNCTION; TISSUE SPECIFICITY; DEVELOPMENTAL STAGE; VARIANT ILE-315; CATALYTIC ACTIVITY; NADPH oxidase-dependent acid production in airway epithelial cells.
Schwarzer C.; Machen T.E.; Illek B.; Fischer H.;
J. Biol. Chem. 279:36454-36461(2004)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6); TISSUE SPECIFICITY; VARIANT ILE-315; Identification of novel Nox4 splice variants with impact on ROS levels in A549 cells.
Goyal P.; Weissmann N.; Rose F.; Grimminger F.; Schaefers H.J.; Seeger W.; Haenze J.;
Biochem. Biophys. Res. Commun. 329:32-39(2005)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5 AND 6); FUNCTION (ISOFORMS 3 AND 4); SUBCELLULAR LOCATION; GLYCOSYLATION; VARIANT ILE-315; CATALYTIC ACTIVITY (ISOFORM 4); 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 6 AND 9); VARIANT ILE-315; The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7); VARIANT ILE-315;

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.