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Protein

NADPH oxidase organizer 1

Gene

Noxo1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Constitutively potentiates the superoxide-generating activity of NOX1 and NOX3 and is required for the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity. Isoform 3 is more potent than isoform 1 in activating NOX3. Together with NOXA1, may also substitute to NCF1/p47phox and NCF2/p67phox in supporting the phagocyte NOX2/gp91phox superoxide-generating activity.2 Publications

GO - Molecular functioni

  1. enzyme binding Source: MGI
  2. identical protein binding Source: MGI
  3. phosphatidylinositol binding Source: InterPro
  4. superoxide-generating NADPH oxidase activator activity Source: MGI

GO - Biological processi

  1. extracellular matrix disassembly Source: UniProtKB
  2. positive regulation of catalytic activity Source: GOC
  3. superoxide metabolic process Source: MGI
Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH oxidase organizer 1
Short name:
Nox organizer 1
Alternative name(s):
Sorting nexin-28
Gene namesi
Name:Noxo1
Synonyms:Snx28
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1919143. Noxo1.

Subcellular locationi

Cell membrane By similarity
Note: Associates with the plasma membrane in a lipid-dependent manner.By similarity

GO - Cellular componenti

  1. NADPH oxidase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice display balance defects being unable to orient themselves with respect to the gravitational force. This is associated with a defect in otoconia biogenesis in the inner ear.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349NADPH oxidase organizer 1PRO_0000227595Add
BLAST

Proteomic databases

PRIDEiQ8VCM2.

PTM databases

PhosphoSiteiQ8VCM2.

Expressioni

Tissue specificityi

Strongly expressed by colon epithelial cells and to a lower extent in small intestine, uterus, stomach and testis. Expressed in different parts of the inner ear including sensory and nonsensory cell layers of the saccule, ampullae of the semicircular canals, the stria vascularis and the spiral glanglion neurons.3 Publications

Developmental stagei

Strongly expressed in inner ear during embryogenesis.1 Publication

Gene expression databases

BgeeiQ8VCM2.
CleanExiMM_NOXO1.
ExpressionAtlasiQ8VCM2. baseline and differential.
GenevestigatoriQ8VCM2.

Interactioni

Subunit structurei

Interacts with NOX1, NOXA1, CYBA/p22phox and NCF2/p67phox. Interacts with SH3PXD2A and SH3PXD2B.By similarity

Protein-protein interaction databases

BioGridi215012. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8VCM2.
SMRiQ8VCM2. Positions 2-143, 184-309.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 126126PXPROSITE-ProRule annotationAdd
BLAST
Domaini157 – 21963SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini231 – 29060SH3 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni315 – 32410Proline-rich region; mediates mutually exclusive interactions with itself and NOXA1By similarity

Domaini

The PX domain mediates lipid-binding, localization to the plasma membrane and is required for NOX1 activation.By similarity
The SH3 domains mediate interaction with CYBA/p22phox.By similarity

Sequence similaritiesi

Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
Contains 2 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG150477.
GeneTreeiENSGT00530000063010.
HOGENOMiHOG000113833.
HOVERGENiHBG082053.
InParanoidiQ8VCM2.
KOiK17934.
OMAiTFVRRSW.
OrthoDBiEOG70GMG8.
PhylomeDBiQ8VCM2.
TreeFamiTF329347.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00787. PX. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8VCM2-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASPRHPVSA HAVALVQMDR LQTFAFSVCW SDNSDTFVRR SWDEFRQLQK
60 70 80 90 100
TLKKTFPVEA GLLRRSEQVL PKLPDAPLLT RRGHTGRGLV RLRLLDTYVQ
110 120 130 140 150
ALLATSEHIL RSSALHGFFV PKPLDLEPML PPGSLVILPT PEEPLSQPRG
160 170 180 190 200
SLDIHSLEAQ SIPCVQPFHT LDIRDRPFHT KAQEILDILL RHPSGWWLVE
210 220 230 240 250
NKDQQVAWFP APYLEEVATC QGQESGLALQ GSGRQFCTTQ AYEGSRSDEL
260 270 280 290 300
SVPSGARVHV LETSDRGWWL CRYNGRTGLL PAMSLQPEGL GSLLGRPGFP
310 320 330 340
DSAGADKVAE DRTIPPVVPT RPCMSAIQSR CCSITRRALG QEQGTRVPR
Length:349
Mass (Da):38,827
Last modified:March 21, 2006 - v2
Checksum:i500F1E1247454101
GO
Isoform 2 (identifier: Q8VCM2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     234-239: RQFCTT → MSPSLL
     240-349: Missing.

Show »
Length:239
Mass (Da):26,844
Checksum:iE514D86B1CB07516
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131V → I in BAE34305. (PubMed:16141072)Curated
Sequence conflicti195 – 1951G → S in AAK94017. 1 PublicationCurated
Sequence conflicti195 – 1951G → S in BAB26387. (PubMed:16141072)Curated
Sequence conflicti239 – 2391T → I in BAE34305. (PubMed:16141072)Curated
Sequence conflicti340 – 3401G → A in AAH19525. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei234 – 2396RQFCTT → MSPSLL in isoform 2. 2 PublicationsVSP_017562
Alternative sequencei240 – 349110Missing in isoform 2. 2 PublicationsVSP_017563Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF539797 mRNA. Translation: AAN75142.1.
AF399754 mRNA. Translation: AAK94017.1.
AK009605 mRNA. Translation: BAB26387.1.
AK088226 mRNA. Translation: BAC40222.1.
AK157993 mRNA. Translation: BAE34305.1.
BC019525 mRNA. Translation: AAH19525.1.
CCDSiCCDS50018.1. [Q8VCM2-1]
RefSeqiNP_082264.2. NM_027988.4. [Q8VCM2-1]
XP_006525012.1. XM_006524949.1. [Q8VCM2-1]
XP_006525013.1. XM_006524950.1. [Q8VCM2-1]
UniGeneiMm.390971.

Genome annotation databases

EnsembliENSMUST00000019464; ENSMUSP00000019464; ENSMUSG00000019320. [Q8VCM2-1]
GeneIDi71893.
KEGGimmu:71893.
UCSCiuc008axs.2. mouse. [Q8VCM2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF539797 mRNA. Translation: AAN75142.1.
AF399754 mRNA. Translation: AAK94017.1.
AK009605 mRNA. Translation: BAB26387.1.
AK088226 mRNA. Translation: BAC40222.1.
AK157993 mRNA. Translation: BAE34305.1.
BC019525 mRNA. Translation: AAH19525.1.
CCDSiCCDS50018.1. [Q8VCM2-1]
RefSeqiNP_082264.2. NM_027988.4. [Q8VCM2-1]
XP_006525012.1. XM_006524949.1. [Q8VCM2-1]
XP_006525013.1. XM_006524950.1. [Q8VCM2-1]
UniGeneiMm.390971.

3D structure databases

ProteinModelPortaliQ8VCM2.
SMRiQ8VCM2. Positions 2-143, 184-309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215012. 2 interactions.

PTM databases

PhosphoSiteiQ8VCM2.

Proteomic databases

PRIDEiQ8VCM2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019464; ENSMUSP00000019464; ENSMUSG00000019320. [Q8VCM2-1]
GeneIDi71893.
KEGGimmu:71893.
UCSCiuc008axs.2. mouse. [Q8VCM2-1]

Organism-specific databases

CTDi124056.
MGIiMGI:1919143. Noxo1.

Phylogenomic databases

eggNOGiNOG150477.
GeneTreeiENSGT00530000063010.
HOGENOMiHOG000113833.
HOVERGENiHBG082053.
InParanoidiQ8VCM2.
KOiK17934.
OMAiTFVRRSW.
OrthoDBiEOG70GMG8.
PhylomeDBiQ8VCM2.
TreeFamiTF329347.

Miscellaneous databases

NextBioi334872.
PROiQ8VCM2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VCM2.
CleanExiMM_NOXO1.
ExpressionAtlasiQ8VCM2. baseline and differential.
GenevestigatoriQ8VCM2.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00787. PX. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two novel proteins activate superoxide generation by the NADPH oxidase NOX1."
    Banfi B., Clark R.A., Steger K., Krause K.-H.
    J. Biol. Chem. 278:3510-3513(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Colon.
  2. Hong W.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Inner ear and Thymus.
  4. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Colon.
  5. "Alternative mRNA splice forms of NOXO1: differential tissue expression and regulation of Nox1 and Nox3."
    Cheng G., Lambeth J.D.
    Gene 356:118-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Inactivation of NADPH oxidase organizer 1 results in severe imbalance."
    Kiss P.J., Knisz J., Zhang Y., Baltrusaitis J., Sigmund C.D., Thalmann R., Smith R.J.H., Verpy E., Banfi B.
    Curr. Biol. 16:208-213(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiNOXO1_MOUSE
AccessioniPrimary (citable) accession number: Q8VCM2
Secondary accession number(s): Q3TZA4, Q8BH41, Q9D747
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: February 4, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.