P35122 (UCHL_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase
EC=3.4.19.12

Alternative name(s):
Ubiquitin thioesterase

Gene names

Name:	Uch
Synonyms:	ubc-D
ORF Names:	CG4265

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Ubiquitin-protein hydrolase is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Ref.2
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).
Developmental stage	Expressed both maternally and zygotically. Ref.2
Sequence similarities	Belongs to the peptidase C12 family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein deubiquitination Inferred from direct assay Ref.2. Source: FlyBase ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	microtubule associated complex Inferred from direct assay. Source: FlyBase
Molecular function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from direct assay Ref.2. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 227	227	Ubiquitin carboxyl-terminal hydrolase		PRO_0000211072
Sites
	Active site	93	1	Nucleophile By similarity
	Active site	164	1	Proton donor By similarity
	Site	179	1	Important for enzyme activity By similarity
Experimental info
	Sequence conflict	22	1	G → A in AAA15411. Ref.2
	Sequence conflict	22	1	G → A in CAA49358. Ref.2
	Sequence conflict	22	1	G → A in CAA49359. Ref.2
	Sequence conflict	65	1	A → T Ref.1
	Sequence conflict	65	1	A → T Ref.2
	Sequence conflict	107	1	E → G Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P35122 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 298A025569C3D409	FASTA	227	25,850
	10 20 30 40 50 60 MLTWTPLESN PEVLTKYIHK LGVSPAWSVT DVIGLEDDTL EWIPRPVKAF ILLFPCSETY 70 80 90 100 110 120 EKHRAEEHDR IKEVEEQHPE DLFYMRQFTH NACGTVALIH SVANNKEVDI DRGVLKDFLE 130 140 150 160 170 180 KTASLSPEER GRALEKDEKF TADHEALAQE GQTNAANHEK VIHHFIALVN KEGTLYELDG 190 200 210 220 RKSFPIKHGP TSEETFVKDA AKVCKEFMAR DPNEVRFTVL ALTAAQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases." Wilkinson K.D., Deshpande S., Larsen C.N. Biochem. Soc. Trans. 20:631-637(1992) [PubMed: 1426603] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning and analysis of expression of a ubiquitin carboxyl terminal hydrolase expressed during oogenesis in Drosophila melanogaster." Zhang N., Wilkinson K., Bownes M. Dev. Biol. 157:214-223(1993) [PubMed: 7683284] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL STAGE. Strain: Oregon-R.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	"A Drosophila complementary DNA resource." Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A. Science 287:2222-2224(2000) [PubMed: 10731138] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S60346 Genomic DNA. Translation: AAA15411.1. X69678 mRNA. Translation: CAA49358.1. X69679 Genomic DNA. Translation: CAA49359.1. AE014134 Genomic DNA. Translation: AAF51291.1. AF145600 mRNA. Translation: AAD38575.1.
PIR	S33956.
RefSeq	NP_001188681.1. NM_001201752.1. NP_476940.1. NM_057592.3.
UniGene	Dm.4794.
3D structure databases
ProteinModelPortal	P35122.
SMR	P35122. Positions 3-225.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1599795.
STRING	P35122.
Protein family/group databases
MEROPS	C12.008.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0077844; FBpp0077516; FBgn0010288. FBtr0303459; FBpp0292511; FBgn0010288.
GeneID	33397.
KEGG	dme:Dmel_CG4265.
NMPDR	fig|7227.3.peg.341.
Organism-specific databases
CTD	33397.
FlyBase	FBgn0010288. Uch.
Phylogenomic databases
eggNOG	inNOG07327.
GeneTree	EMGT00050000007616.
InParanoid	P35122.
OMA	YEIDSRR.
OrthoDB	EOG4G4F6N.
PhylomeDB	P35122.
Gene expression databases
Bgee	P35122.
GermOnline	CG4265. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001578. Peptidase_C12. [Graphical view]
Gene3D	G3DSA:3.40.532.10. Peptidase_C12. 1 hit.
KO	K05609.
PANTHER	PTHR10589. Peptidase_C12. 1 hit.
Pfam	PF01088. Peptidase_C12. 1 hit. [Graphical view]
PRINTS	PR00707. UBCTHYDRLASE.
PROSITE	PS00140. UCH_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	783351.

Entry information

Entry name

UCHL_DROME

Accession

Primary (citable) accession number: P35122
Secondary accession number(s): Q4PIX7, Q9TWA0, Q9V417

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	August 30, 2005
Last modified:	January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project