Q2YDU3 (OTUD5_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
OTU domain-containing protein 5
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme A
Short name=DUBA

Gene names

Name:

Otud5

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	566 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Deubiquitinating enzyme that functions as negative regulator of the innate immune system. Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'-linked ubiquitin chains (in vitro) By similarity.
Catalytic activity	Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Enzyme regulation	Inhibited by N-ethyl-maleimide (NEM) By similarity.
Subunit structure	Interacts with TRAF3 By similarity.
Post-translational modification	Phosphorylation at Ser-177 is required for deubiquitinating activity By similarity.
Sequence similarities	Belongs to the peptidase C85 family. Contains 1 OTU domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein K48-linked deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K63-linked deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to lipopolysaccharide Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q2YDU3-1)

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.

Isoform 2 (identifier: Q2YDU3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     118-160: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 566	566	OTU domain-containing protein 5		PRO_0000278225
Regions
	Domain	213 – 336	124	OTU
	Compositional bias	5 – 113	109	Pro-rich
	Compositional bias	33 – 174	142	Gly-rich
Sites
	Active site	221	1	Potential
	Active site	224	1	Nucleophile By similarity
	Active site	329	1	By similarity
Amino acid modifications
	Modified residue	64	1	Phosphoserine By similarity
	Modified residue	165	1	Phosphoserine By similarity
	Modified residue	175	1	Phosphotyrosine By similarity
	Modified residue	177	1	Phosphoserine By similarity
	Modified residue	447	1	Phosphoserine By similarity
	Modified residue	502	1	Phosphothreonine By similarity
	Modified residue	503	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	118 – 160	43	Missing in isoform 2.		VSP_023197

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 20, 2007. Version 2. Checksum: 1B49AF4337634A07	FASTA	566	60,288
	10 20 30 40 50 60 MTILPKKKPP PPDADPANEP PPPGPLPPAP RRGGGVGVGG GGTGVGGGER DRDSGVVGAR 70 80 90 100 110 120 PRASPPPQGP LPGPPGALHR WALAVPPGAV AGPRPQQASP PPCGGPGGPG GGPGDALGAT 130 140 150 160 170 180 TAGVGAAGVV VGVGGPVGVG GCCSGPGHSK RRRQAPGVGA VGGASPEREE VGAGYNSEDE 190 200 210 220 230 240 YEAAAARIEA MDPATVEQQE HWFEKALRDK KGFIIKQMKE DGACLFRAVA DQVYGDQDMH 250 260 270 280 290 300 EVVRKHCMDY LMKNADYFSN YVTEDFTTYI NRKRKNNCHG NHIEMQAMAE MYNRPVEVYQ 310 320 330 340 350 360 YSTEPINTFH GIHQNEDEPI RVSYHRNIHY NSVVNPNKAT IGVGLGLPSF KPGFAEQSLM 370 380 390 400 410 420 KNAIKTSEES WIEQQMLEDK KRATDWEATN EAIEEQVARE SYLQWLRDQE KQARQVRGPS 430 440 450 460 470 480 QPRKASATCS SATAAASSGL EEWTSRSPRQ RSSASSPEHP ELHAELGIKP PSPGTVLALA 490 500 510 520 530 540 KPPSPCAPGT SSQFSAGADR ATSPLVSLYP ALECRALIQQ MSPSAFGLND WDDDEILASV 550 560 LAVSQQEYLD SMKKNKVHRD PPPDKS
	Isoform 2 [UniParc]. Checksum: CB83BE543DEACE23	FASTA	523	56,534
	10 20 30 40 50 60 MTILPKKKPP PPDADPANEP PPPGPLPPAP RRGGGVGVGG GGTGVGGGER DRDSGVVGAR 70 80 90 100 110 120 PRASPPPQGP LPGPPGALHR WALAVPPGAV AGPRPQQASP PPCGGPGGPG GGPGDALVGG 130 140 150 160 170 180 ASPEREEVGA GYNSEDEYEA AAARIEAMDP ATVEQQEHWF EKALRDKKGF IIKQMKEDGA 190 200 210 220 230 240 CLFRAVADQV YGDQDMHEVV RKHCMDYLMK NADYFSNYVT EDFTTYINRK RKNNCHGNHI 250 260 270 280 290 300 EMQAMAEMYN RPVEVYQYST EPINTFHGIH QNEDEPIRVS YHRNIHYNSV VNPNKATIGV 310 320 330 340 350 360 GLGLPSFKPG FAEQSLMKNA IKTSEESWIE QQMLEDKKRA TDWEATNEAI EEQVARESYL 370 380 390 400 410 420 QWLRDQEKQA RQVRGPSQPR KASATCSSAT AAASSGLEEW TSRSPRQRSS ASSPEHPELH 430 440 450 460 470 480 AELGIKPPSP GTVLALAKPP SPCAPGTSSQ FSAGADRATS PLVSLYPALE CRALIQQMSP 490 500 510 520 SAFGLNDWDD DEILASVLAV SQQEYLDSMK KNKVHRDPPP DKS

References

[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[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] (ISOFORM 2). Tissue: Placenta.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR03119131 Genomic DNA. No translation available. BC110054 mRNA. Translation: AAI10055.1.
IPI	IPI00565030. IPI00679234.
RefSeq	NP_001032585.1. NM_001037496.1.
UniGene	Rn.97794.
3D structure databases
ProteinModelPortal	Q2YDU3.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000039455.
Protein family/group databases
MEROPS	C85.001.
Proteomic databases
PaxDb	Q2YDU3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000006233; ENSRNOP00000006233; ENSRNOG00000008764. ENSRNOT00000044743; ENSRNOP00000039455; ENSRNOG00000008764.
GeneID	363452.
KEGG	rno:363452.
UCSC	RGD:1563027. rat.
Organism-specific databases
CTD	55593.
RGD	1563027. Otud5.
Phylogenomic databases
eggNOG	NOG286112.
GeneTree	ENSGT00510000048473.
HOGENOM	HOG000231360.
HOVERGEN	HBG060214.
InParanoid	Q2YDU3.
KO	K12655.
OMA	WEDDEIL.
OrthoDB	EOG4KWJSV.
Gene expression databases
Genevestigator	Q2YDU3.
Family and domain databases
InterPro	IPR003323. OTU. [Graphical view]
Pfam	PF02338. OTU. 1 hit. [Graphical view]
PROSITE	PS50802. OTU. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	683365.

Entry information

Entry name

OTUD5_RAT

Accession

Primary (citable) accession number: Q2YDU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 20, 2007
Last sequence update:	February 20, 2007
Last modified:	April 3, 2013
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program