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Protein

2-aminoethanethiol dioxygenase

Gene

Ado

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2-aminoethanethiol + O2 = hypotaurine.1 Publication

Cofactori

Fe cation1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.19. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
2-aminoethanethiol dioxygenase (EC:1.13.11.19)
Alternative name(s):
Cysteamine dioxygenase
Gene namesi
Name:Ado
Synonyms:Gm237
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2685083. Ado.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2562562-aminoethanethiol dioxygenasePRO_0000089785Add
BLAST

Proteomic databases

EPDiQ6PDY2.
MaxQBiQ6PDY2.
PaxDbiQ6PDY2.
PRIDEiQ6PDY2.

PTM databases

iPTMnetiQ6PDY2.
PhosphoSiteiQ6PDY2.

Expressioni

Tissue specificityi

Ubiquitous, with highest expression in brain, heart and skeletal muscle (at protein level).1 Publication

Gene expression databases

BgeeiQ6PDY2.
CleanExiMM_ADO.
GenevisibleiQ6PDY2. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000075107.

Structurei

3D structure databases

ProteinModelPortaliQ6PDY2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiKOG4281. Eukaryota.
ENOG4111Y3H. LUCA.
GeneTreeiENSGT00390000014082.
HOGENOMiHOG000037604.
HOVERGENiHBG050966.
InParanoidiQ6PDY2.
KOiK10712.
OMAiAPMPQGF.
OrthoDBiEOG7NKKMH.
PhylomeDBiQ6PDY2.
TreeFamiTF314673.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR012864. PCO/ADO.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF07847. DUF1637. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6PDY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRDNMASLI QRIARQACLT FRGSSTGSEG PAPGFPENLS LLKSLLTQVR
60 70 80 90 100
AEDLNIAPRK ALPQPLPRNL PPVTYMHIYE TEGFSLGVFL LKSGTCIPLH
110 120 130 140 150
DHPGMHGMLK VLYGTVRISC MDKLDTGAGH RRPPPEQQFE PPLQPLEREA
160 170 180 190 200
VRPGVLRSRA EYTEASGPCV LTPHRDNLHQ IDAVDGPAAF LDILAPPYDP
210 220 230 240 250
EDGRDCHYYR VVEPIRPKEA SGSACDLPRE VWLLETPQAD DFWCEGEPYP

GPKVLP
Length:256
Mass (Da):28,372
Last modified:February 21, 2006 - v2
Checksum:iC5E23C4A72A79678
GO

Sequence cautioni

The sequence AAH57106.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH58407.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK155334 mRNA. Translation: BAE33200.1.
BC057106 mRNA. Translation: AAH57106.1. Different initiation.
BC058407 mRNA. Translation: AAH58407.1. Different initiation.
CCDSiCCDS48588.1.
RefSeqiNP_001005419.2. NM_001005419.2.
UniGeneiMm.297250.
Mm.491461.

Genome annotation databases

EnsembliENSMUST00000075686; ENSMUSP00000075107; ENSMUSG00000057134.
GeneIDi211488.
KEGGimmu:211488.
UCSCiuc007flz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK155334 mRNA. Translation: BAE33200.1.
BC057106 mRNA. Translation: AAH57106.1. Different initiation.
BC058407 mRNA. Translation: AAH58407.1. Different initiation.
CCDSiCCDS48588.1.
RefSeqiNP_001005419.2. NM_001005419.2.
UniGeneiMm.297250.
Mm.491461.

3D structure databases

ProteinModelPortaliQ6PDY2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000075107.

PTM databases

iPTMnetiQ6PDY2.
PhosphoSiteiQ6PDY2.

Proteomic databases

EPDiQ6PDY2.
MaxQBiQ6PDY2.
PaxDbiQ6PDY2.
PRIDEiQ6PDY2.

Protocols and materials databases

DNASUi211488.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000075686; ENSMUSP00000075107; ENSMUSG00000057134.
GeneIDi211488.
KEGGimmu:211488.
UCSCiuc007flz.2. mouse.

Organism-specific databases

CTDi84890.
MGIiMGI:2685083. Ado.

Phylogenomic databases

eggNOGiKOG4281. Eukaryota.
ENOG4111Y3H. LUCA.
GeneTreeiENSGT00390000014082.
HOGENOMiHOG000037604.
HOVERGENiHBG050966.
InParanoidiQ6PDY2.
KOiK10712.
OMAiAPMPQGF.
OrthoDBiEOG7NKKMH.
PhylomeDBiQ6PDY2.
TreeFamiTF314673.

Enzyme and pathway databases

BRENDAi1.13.11.19. 3474.

Miscellaneous databases

NextBioi373260.
PROiQ6PDY2.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PDY2.
CleanExiMM_ADO.
GenevisibleiQ6PDY2. MM.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR012864. PCO/ADO.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF07847. DUF1637. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
    Strain: NOD.
    Tissue: Dendritic cell.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase."
    Dominy J.E. Jr., Simmons C.R., Hirschberger L.L., Hwang J., Coloso R.M., Stipanuk M.H.
    J. Biol. Chem. 282:25189-25198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiAEDO_MOUSE
AccessioniPrimary (citable) accession number: Q6PDY2
Secondary accession number(s): Q3U2E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: February 21, 2006
Last modified: May 11, 2016
This is version 98 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

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.