Q9FPS0 (UBP27_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 27
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 27
Short name=AtUBP27
Ubiquitin thioesterase 27
Ubiquitin-specific-processing protease 27

Gene names

Name:	UBP27
Ordered Locus Names:	At4g39370
ORF Names:	F23K16.5

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins 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).
Subcellular location	Membrane; Single-pass membrane protein Potential.
Sequence similarities	Belongs to the peptidase C19 family.
Sequence caution	The sequence CAB52824.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB80600.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9FPS0-1)

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: Q9FPS0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     314-361: TEIEKLRSCG...LIIARFPKLL → VVNLSQLLML...AQELWRRGPM
     362-494: Missing.

Note: Derived from EST data. May be due to an intron retention. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 494	494	Ubiquitin carboxyl-terminal hydrolase 27		PRO_0000313052
Regions
	Transmembrane	30 – 50	21	Helical; Potential
Sites
	Active site	83	1	Nucleophile By similarity
	Active site	440	1	Proton acceptor By similarity
Natural variations
	Alternative sequence	314 – 361	48	TEIEK…FPKLL → VVNLSQLLMLLYFSFVHASR LYLTRVSWKRFQSDGNRKAQ ELWRRGPM in isoform 2.		VSP_029992
	Alternative sequence	362 – 494	133	Missing in isoform 2.		VSP_029993

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: B8CBDF5799FA9FA6	FASTA	494	55,771
	10 20 30 40 50 60 MVSRRGSETK AIVCVLTDRI RISNQWVSHL SFAGLLGVAG FVFAQQHGLF RNLNNLKLFS 70 80 90 100 110 120 GREKDSGDDS FLVPGLQNLG NNCFLNVILQ ALASCKDFRS FLQWVLEDAR GSLAGEQEEQ 130 140 150 160 170 180 LPLTFALSAL LQELGTVGSR RSVSNPRKVM VTLTDYAKNF NLTSQQDAAE ALLHLISSLQ 190 200 210 220 230 240 EEIVVCYRPS QSSNLSDILF SRNLRMLAPS EGLHGLMELK RWHKHLRGPF DGILGSTLMC 250 260 270 280 290 300 RTCSSQISLE FQFFHTLPLS PLLHHGGYNI MSGCTLEHCL KKFLNTEKVE NYFCYRCWHG 310 320 330 340 350 360 AALKYLSVIG AAETEIEKLR SCGGEDQCDC KTSLHLQRMP WSNSYSHILK QLIIARFPKL 370 380 390 400 410 420 LCIQVQRASF NMFEEFKLSG HIAFPLVLNL SLFTPSSIGV NIEERIEMSS EYQKPEASKN 430 440 450 460 470 480 HGMYRLVTVV EHFGRTGSGH YTVYRSVRVF SQEEEEEDCD EDLSWFSISD SEVCRVSESD 490 VLGAEASLLF YERL
	Isoform 2 [UniParc]. Checksum: EBD855CB345C1129	FASTA	361	40,770
	10 20 30 40 50 60 MVSRRGSETK AIVCVLTDRI RISNQWVSHL SFAGLLGVAG FVFAQQHGLF RNLNNLKLFS 70 80 90 100 110 120 GREKDSGDDS FLVPGLQNLG NNCFLNVILQ ALASCKDFRS FLQWVLEDAR GSLAGEQEEQ 130 140 150 160 170 180 LPLTFALSAL LQELGTVGSR RSVSNPRKVM VTLTDYAKNF NLTSQQDAAE ALLHLISSLQ 190 200 210 220 230 240 EEIVVCYRPS QSSNLSDILF SRNLRMLAPS EGLHGLMELK RWHKHLRGPF DGILGSTLMC 250 260 270 280 290 300 RTCSSQISLE FQFFHTLPLS PLLHHGGYNI MSGCTLEHCL KKFLNTEKVE NYFCYRCWHG 310 320 330 340 350 360 AALKYLSVIG AAEVVNLSQL LMLLYFSFVH ASRLYLTRVS WKRFQSDGNR KAQELWRRGP M

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine." Yan N., Doelling J.H., Falbel T.G., Durski A.M., Vierstra R.D. Plant Physiol. 124:1828-1843(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY ORGANIZATION, NOMENCLATURE (ISOFORM 1). Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF302675 mRNA. Translation: AAG42765.1. AL078620 Genomic DNA. Translation: CAB52824.1. Sequence problems. AL161595 Genomic DNA. Translation: CAB80600.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE87061.1. CP002687 Genomic DNA. Translation: AEE87062.1. AF370208 mRNA. Translation: AAK44023.1. AY133770 mRNA. Translation: AAM91704.1.
IPI	IPI00516325. IPI00545191.
PIR	B85466.
RefSeq	NP_568058.1. NM_120097.2. NP_974714.1. NM_202985.1.
UniGene	At.3432.
3D structure databases
HSSP	HSSP built from PDB template 2GFO based on UniProtKB P40818.
ProteinModelPortal	Q9FPS0.
SMR	Q9FPS0. Positions 75-492.
ModBase	Search...
Proteomic databases
PaxDb	Q9FPS0.
PRIDE	Q9FPS0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G39370.1; AT4G39370.1; AT4G39370.
GeneID	830092.
KEGG	ath:AT4G39370.
Organism-specific databases
TAIR	At4g39370.
Phylogenomic databases
eggNOG	COG5533.
HOGENOM	HOG000070653.
InParanoid	Q9FPS0.
KO	K11851.
PhylomeDB	Q9FPS0.
ProtClustDB	CLSN2689838.
Gene expression databases
ArrayExpress	Q9FPS0.
Genevestigator	Q9FPS0.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. False negative. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBP27_ARATH

Accession

Primary (citable) accession number: Q9FPS0
Secondary accession number(s): Q3E9N3, Q9SVC0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program