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Protein

Ecto-NOX disulfide-thiol exchanger 2

Gene

Enox2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

May be involved in cell growth. Probably acts as a terminal oxidase of plasma electron transport from cytosolic NAD(P)H via hydroquinones to acceptors at the cell surface. Hydroquinone oxidase activity alternates with a protein disulfide-thiol interchange/oxidoreductase activity which may control physical membrane displacements associated with vesicle budding or cell enlargement. The activities oscillate with a period length of 22 minutes and play a role in control of the ultradian cellular biological clock (By similarity).By similarity

Cofactori

Cu cationBy similarity

Enzyme regulationi

Inhibited by the antitumor sulfonylurea LY181984, the vabilloid capsaicin, and retinoids.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Biological rhythms, Electron transport, Growth regulation, Transport

Keywords - Ligandi

Copper, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Ecto-NOX disulfide-thiol exchanger 2
Alternative name(s):
APK1 antigen
Cytosolic ovarian carcinoma antigen 1
Tumor-associated hydroquinone oxidase
Short name:
tNOX
Including the following 2 domains:
Hydroquinone [NADH] oxidase (EC:1.-.-.-)
Protein disulfide-thiol oxidoreductase (EC:1.-.-.-)
Gene namesi
Name:Enox2
Synonyms:Cova1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:2384799. Enox2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 598598Ecto-NOX disulfide-thiol exchanger 2PRO_0000079276Add
BLAST

Post-translational modificationi

Glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8R0Z2.
PaxDbiQ8R0Z2.
PRIDEiQ8R0Z2.

PTM databases

iPTMnetiQ8R0Z2.
PhosphoSiteiQ8R0Z2.

Expressioni

Gene expression databases

BgeeiQ8R0Z2.
CleanExiMM_ENOX2.
GenevisibleiQ8R0Z2. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033437.

Structurei

3D structure databases

ProteinModelPortaliQ8R0Z2.
SMRiQ8R0Z2. Positions 98-180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini99 – 17880RRMPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili264 – 29936Sequence analysisAdd
BLAST
Coiled coili352 – 476125Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi29 – 9668Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the ENOX family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEVY. Eukaryota.
ENOG410XVWG. LUCA.
GeneTreeiENSGT00390000006788.
HOGENOMiHOG000049275.
HOVERGENiHBG051083.
InParanoidiQ8R0Z2.
OMAiRNANNFY.
OrthoDBiEOG7DVD9H.
PhylomeDBiQ8R0Z2.
TreeFamiTF323802.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1Curated (identifier: Q8R0Z2-1) [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
MTLPVSDPAA WATAMNNLGM APLGIAGQPI LPDFDPALGM MTGIPPITPM
60 70 80 90 100
MPGLGIVPPP IPPDMPVAKE IIHCKSCTLF PPNPNLPPPA TRERPPGCKT
110 120 130 140 150
VFVGGLPENG TEQIIVEVFE QCGEIIAIRK SKKNFCHIRF AEEYMVDKAL
160 170 180 190 200
YLSGYRIRLG SSTDKKDTGR LHVDFAQARD DLYEWECKQR MLAREERHRR
210 220 230 240 250
RMEEERMRPP SPPPVVHYSD HECSIVAEKL KDDSKFSEAV QTLLTWIERG
260 270 280 290 300
EVNRRSANHF YSMIQSANSH VRRLVNEKAT HEKEMEEAKE KFKQALSGIL
310 320 330 340 350
IQFEQIVAVY HSASKQKAWD HFTKAQRKNI SVWCKQAEEI RNIHNDELMG
360 370 380 390 400
IRREEEMEMS DDEIEETTET KETEESALVS QAEALKEEND SLRWQLDAYR
410 420 430 440 450
NEVELLKQEQ GKAHREDDPN KEQQLKLLQQ ALQGMQQHLL KVQEEYKKKE
460 470 480 490 500
AELDRIKDDN LQVEQLLENF HEKQENCGSR LCASSQEGEQ PLEKTAVSNP
510 520 530 540 550
VKSEREALLV GIISTFLHVH PFGASIEYIC SYLNRLDNKA SYQIPSKLTT
560 570 580 590
SPLLPISTSD VESLMSRLQH TFRQEMTGVG ASLEKRWKFC GFEGLKLT
Length:598
Mass (Da):68,285
Last modified:June 1, 2002 - v1
Checksum:iC115D1130E4D6094
GO
Isoform 2Curated (identifier: Q8R0Z2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     463-473: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:587
Mass (Da):66,917
Checksum:i91B5EBB24FA83CEF
GO
Isoform 3Curated (identifier: Q8R0Z2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     540-555: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:582
Mass (Da):66,587
Checksum:i2A143B3F09CB59B2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei463 – 47311Missing in isoform 2. 1 PublicationVSP_051830Add
BLAST
Alternative sequencei540 – 55516Missing in isoform 3. 1 PublicationVSP_051831Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034058 mRNA. Translation: BAC28565.1.
AK041822 mRNA. Translation: BAC31077.1.
BX294194 Genomic DNA. Translation: CAM21582.1.
BC025915 mRNA. Translation: AAH25915.1.
BC026450 mRNA. Translation: AAH26450.1.
CCDSiCCDS30115.1. [Q8R0Z2-1]
CCDS72377.1. [Q8R0Z2-3]
CCDS72378.1. [Q8R0Z2-2]
RefSeqiNP_001258376.1. NM_001271447.1. [Q8R0Z2-1]
NP_001258377.1. NM_001271448.1. [Q8R0Z2-1]
NP_001258378.1. NM_001271449.1. [Q8R0Z2-1]
NP_001258379.1. NM_001271450.1. [Q8R0Z2-2]
NP_666063.1. NM_145951.5. [Q8R0Z2-1]
UniGeneiMm.327730.

Genome annotation databases

EnsembliENSMUST00000033437; ENSMUSP00000033437; ENSMUSG00000031109. [Q8R0Z2-1]
ENSMUST00000114911; ENSMUSP00000110561; ENSMUSG00000031109. [Q8R0Z2-2]
ENSMUST00000114912; ENSMUSP00000110562; ENSMUSG00000031109. [Q8R0Z2-3]
ENSMUST00000114914; ENSMUSP00000110564; ENSMUSG00000031109. [Q8R0Z2-1]
ENSMUST00000114918; ENSMUSP00000110568; ENSMUSG00000031109. [Q8R0Z2-1]
ENSMUST00000167659; ENSMUSP00000128885; ENSMUSG00000031109. [Q8R0Z2-1]
GeneIDi209224.
KEGGimmu:209224.
UCSCiuc009tcv.2. mouse. [Q8R0Z2-1]
uc009tcz.2. mouse. [Q8R0Z2-3]
uc012hgt.2. mouse. [Q8R0Z2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034058 mRNA. Translation: BAC28565.1.
AK041822 mRNA. Translation: BAC31077.1.
BX294194 Genomic DNA. Translation: CAM21582.1.
BC025915 mRNA. Translation: AAH25915.1.
BC026450 mRNA. Translation: AAH26450.1.
CCDSiCCDS30115.1. [Q8R0Z2-1]
CCDS72377.1. [Q8R0Z2-3]
CCDS72378.1. [Q8R0Z2-2]
RefSeqiNP_001258376.1. NM_001271447.1. [Q8R0Z2-1]
NP_001258377.1. NM_001271448.1. [Q8R0Z2-1]
NP_001258378.1. NM_001271449.1. [Q8R0Z2-1]
NP_001258379.1. NM_001271450.1. [Q8R0Z2-2]
NP_666063.1. NM_145951.5. [Q8R0Z2-1]
UniGeneiMm.327730.

3D structure databases

ProteinModelPortaliQ8R0Z2.
SMRiQ8R0Z2. Positions 98-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033437.

PTM databases

iPTMnetiQ8R0Z2.
PhosphoSiteiQ8R0Z2.

Proteomic databases

MaxQBiQ8R0Z2.
PaxDbiQ8R0Z2.
PRIDEiQ8R0Z2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033437; ENSMUSP00000033437; ENSMUSG00000031109. [Q8R0Z2-1]
ENSMUST00000114911; ENSMUSP00000110561; ENSMUSG00000031109. [Q8R0Z2-2]
ENSMUST00000114912; ENSMUSP00000110562; ENSMUSG00000031109. [Q8R0Z2-3]
ENSMUST00000114914; ENSMUSP00000110564; ENSMUSG00000031109. [Q8R0Z2-1]
ENSMUST00000114918; ENSMUSP00000110568; ENSMUSG00000031109. [Q8R0Z2-1]
ENSMUST00000167659; ENSMUSP00000128885; ENSMUSG00000031109. [Q8R0Z2-1]
GeneIDi209224.
KEGGimmu:209224.
UCSCiuc009tcv.2. mouse. [Q8R0Z2-1]
uc009tcz.2. mouse. [Q8R0Z2-3]
uc012hgt.2. mouse. [Q8R0Z2-2]

Organism-specific databases

CTDi10495.
MGIiMGI:2384799. Enox2.

Phylogenomic databases

eggNOGiENOG410IEVY. Eukaryota.
ENOG410XVWG. LUCA.
GeneTreeiENSGT00390000006788.
HOGENOMiHOG000049275.
HOVERGENiHBG051083.
InParanoidiQ8R0Z2.
OMAiRNANNFY.
OrthoDBiEOG7DVD9H.
PhylomeDBiQ8R0Z2.
TreeFamiTF323802.

Miscellaneous databases

ChiTaRSiEnox2. mouse.
PROiQ8R0Z2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R0Z2.
CleanExiMM_ENOX2.
GenevisibleiQ8R0Z2. MM.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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.
    Tissue: Diencephalon and Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 328-598 (ISOFORM 3).
    Strain: FVB/NImported.
    Tissue: KidneyImported and Mammary glandImported.

Entry informationi

Entry nameiENOX2_MOUSE
AccessioniPrimary (citable) accession number: Q8R0Z2
Secondary accession number(s): B1B073, Q8BY59, Q8R372
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 109 of the entry and version 1 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

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 one 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.