O81149 (PSA5A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome subunit alpha type-5-A
EC=3.4.25.1

Alternative name(s):
20S proteasome alpha subunit E-1

Gene names

Name:	PAE1
Ordered Locus Names:	At1g53850
ORF Names:	T18A20.8

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	237 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	Component of the 20S core complex of the 26S proteasome. The 26S proteasome is composed of a core protease (CP), known as the 20S proteasome, capped at one or both ends by the 19S regulatory particle (RP/PA700). The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Ref.7 Ref.8
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	response to cadmium ion Inferred from expression pattern. Source: TAIR ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosolic ribosome Inferred from direct assay. Source: TAIR nucleus Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR proteasome core complex, alpha-subunit complex Inferred from electronic annotation. Source: InterPro vacuolar membrane Inferred from direct assay. Source: TAIR
Molecular function	ribonuclease activity Inferred from direct assay. Source: TAIR threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 237	237	Proteasome subunit alpha type-5-A		PRO_0000124124
Experimental info
	Sequence conflict	121	1	L → F in BAD94476. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	O81149 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: B17DED1D6E2C9680	FASTA	237	25,947
	10 20 30 40 50 60 MFLTRTEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGV KTKEGVVLAV EKRITSPLLE 70 80 90 100 110 120 PSSVEKIMEI DDHIGCAMSG LIADARTLVE HARVETQNHR FSYGEPMTVE STTQALCDLA 130 140 150 160 170 180 LRFGEGEEES MSRPFGVSLL IAGHDENGPS LYYTDPSGTF WQCNAKAIGS GSEGADSSLQ 190 200 210 220 230 EQFNKDLSLQ EAETIAVSIL KQVMEEKVTP NNVDIAKVAP AYHLYTPQEV EAVIARL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular organization of the 20S proteasome gene family from Arabidopsis thaliana." Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D. Genetics 149:677-692(1998) [PubMed: 9611183] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-237. Strain: cv. Columbia.
[7]	"Structure and functional analyses of the 26S proteasome subunits from plants." Fu H., Girod P.-A., Doelling J.H., van Nocker S., Hochstrasser M., Finley D., Vierstra R.D. Mol. Biol. Rep. 26:137-146(1999) [PubMed: 10363660] [Abstract] Cited for: SUBUNIT.
[8]	"Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms." Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D. J. Biol. Chem. 279:6401-6413(2004) [PubMed: 14623884] [Abstract] Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF043524 mRNA. Translation: AAC32060.1. AC009324 Genomic DNA. Translation: AAF02858.1. CP002684 Genomic DNA. Translation: AEE33009.1. CP002684 Genomic DNA. Translation: AEE33010.1. AY072371 mRNA. Translation: AAL62363.1. AY114616 mRNA. Translation: AAM47935.1. AY086045 mRNA. Translation: AAM63255.1. AK220949 mRNA. Translation: BAD94476.1.
IPI	IPI00526133.
PIR	T51972.
RefSeq	NP_001077717.1. NM_001084248.1. NP_175788.1. NM_104262.2.
UniGene	At.23242.
3D structure databases
ProteinModelPortal	O81149.
SMR	O81149. Positions 8-234.
ModBase	Search...
Protein-protein interaction databases
IntAct	O81149. 2 interactions.
STRING	O81149.
Proteomic databases
PRIDE	O81149.
ProMEX	O81149.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G53850.1; AT1G53850.1; AT1G53850. AT1G53850.2; AT1G53850.2; AT1G53850.
GeneID	841822.
GenomeReviews	Gene locus AT1G53850 in contig CT485782_GR.
KEGG	ath:AT1G53850.
NMPDR	fig|3702.1.peg.4889.
Organism-specific databases
TAIR	At1g53850.
Phylogenomic databases
eggNOG	KOG0176.
GeneTree	EPGT00050000005270.
HOGENOM	HBG499923.
InParanoid	O81149.
OMA	RSEYDXC.
PhylomeDB	O81149.
ProtClustDB	CLSN2682144.
Gene expression databases
ArrayExpress	O81149.
Genevestigator	O81149.
GermOnline	AT1G53850. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000426. Proteasome_asu_N. IPR023332. Proteasome_suA-type. IPR001353. Proteasome_sua/b. [Graphical view]
KO	K02729.
Pfam	PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. [Graphical view]
SMART	SM00948. Proteasome_A_N. 1 hit. [Graphical view]
PROSITE	PS00388. PROTEASOME_A_1. 1 hit. PS51475. PROTEASOME_A_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PSA5A_ARATH

Accession

Primary (citable) accession number: O81149
Secondary accession number(s): Q56ZL5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program