Q9QUM9 (PSA6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome subunit alpha type-6
EC=3.4.25.1

Alternative name(s):
Macropain iota chain
Multicatalytic endopeptidase complex iota chain
Proteasome iota chain

Gene names

Name:

Psma6

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

Protein attributes

Sequence length	246 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	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. 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.8
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › P-body. Note: Co-localizes with TRIM5 in the cytoplasmic bodies. Ref.9
Induction	Up-regulated in liver tumor tissues (at protein level). Ref.6
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
PTM	Acetylation Glycoprotein Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity. Source: BHF-UCL proteolysis involved in cellular protein catabolic process Inferred from sequence or structural similarity. Source: BHF-UCL skeletal muscle tissue development Non-traceable author statement PubMed 10852819. Source: BHF-UCL ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasmic mRNA processing body Inferred from direct assay Ref.9. Source: UniProtKB cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: Compara nuclear matrix Inferred from direct assay PubMed 10852819. Source: BHF-UCL polysome Inferred from sequence or structural similarity. Source: BHF-UCL proteasome core complex, alpha-subunit complex Inferred from sequence or structural similarity. Source: BHF-UCL sarcomere Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	RNA binding Inferred from direct assay PubMed 10852819. Source: BHF-UCL 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 – 246

246

Proteasome subunit alpha type-6

PRO_0000124131

Amino acid modifications

Modified residue

102

1

N6-acetyllysine By similarity

Modified residue

104

1

N6-acetyllysine By similarity

Modified residue

159

1

Phosphotyrosine Ref.7

Glycosylation

5

1

O-linked (GlcNAc...) Ref.10

Cross-link

59

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict

133

1

P → T in BAE36518. Ref.3

Secondary structure

1

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246

Helix Strand Turn

Details...

Turn

10 – 12

3

Helix

23 – 32

10

Helix

33 – 35

3

Beta strand

38 – 43

6

Beta strand

45 – 53

9

Turn

63 – 65

3

Beta strand

69 – 71

3

Beta strand

73 – 82

10

Helix

84 – 105

22

Helix

111 – 127

17

Beta strand

128 – 131

4

Beta strand

135 – 144

10

Turn

145 – 147

3

Beta strand

148 – 154

7

Beta strand

156 – 158

3

Beta strand

160 – 169

10

Helix

172 – 184

13

Helix

191 – 206

16

Turn

212 – 214

3

Beta strand

215 – 223

9

Helix

232 – 242

11

Sequences

	Sequence		Length	Mass (Da)
	Q9QUM9 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6DF57BE87FA48D32	FASTA	246	27,372
	10 20 30 40 50 60 MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL 70 80 90 100 110 120 LDSSTVTHLF KITESIGCVM TGMTADSRSQ VQRARYEAAN WKYKYGYEIP VDMLCKRIAD 130 140 150 160 170 180 ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ VYKCDPAGYY CGFKATAAGV KQTESTSFLE 190 200 210 220 230 240 KKVKKKFDWT FEQTVETAIT CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV ALAERD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of mouse prosomal subunit iota." Thomson S.A., Fechheimer M. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Carcinoma.
[2]	"The complete primary structure of mouse 20S proteasomes." Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N., Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J. Immunogenetics 49:835-842(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: B10.BR.
[3]	"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: C57BL/6J and NOD. Tissue: Bone marrow and Thymus.
[4]	"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/6. Tissue: Eye.
[5]	Lubec G., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 60-71; 105-116; 118-132 AND 229-245, MASS SPECTROMETRY. Strain: OF1. Tissue: Brain and Hippocampus.
[6]	"The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice." Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X., Zhang X., Yang X. Proteomics 6:498-504(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, MASS SPECTROMETRY.
[7]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-159, MASS SPECTROMETRY. Tissue: Brain.
[8]	"Mapping the murine cardiac 26S proteasome complexes." Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J., Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P. Circ. Res. 99:362-371(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
[9]	"TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions." Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., Luban J., Campbell E.M. Retrovirology 8:93-93(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel biotin-cystamine tag." Overath T., Kuckelkorn U., Henklein P., Strehl B., Bonar D., Kloss A., Siele D., Kloetzel P.M., Janek K. Mol. Cell. Proteomics 11:467-477(2012) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT SER-5. Tissue: Brain and Spleen.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U60288 mRNA. Translation: AAF21459.1.
AF060087 mRNA. Translation: AAD50532.1.
AK088143 mRNA. Translation: BAC40169.1.
AK152915 mRNA. Translation: BAE31592.1.
AK161662 mRNA. Translation: BAE36518.1.
BC086685 mRNA. Translation: AAH86685.1.

IPI

IPI00131845.

RefSeq

NP_036098.1. NM_011968.3.

UniGene

Mm.30210.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3UNB	X-ray	2.90	G/U/i/w	1-246	[»]
3UNE	X-ray	3.20	G/U/i/w	1-246	[»]
3UNF	X-ray	2.90	G/U	1-246	[»]
3UNH	X-ray	3.20	G/U	1-246	[»]

ProteinModelPortal

Q9QUM9.

SMR

Q9QUM9. Positions 2-245.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9QUM9. 3 interactions.

Protein family/group databases

MEROPS

T01.971.

PTM databases

PhosphoSite

Q9QUM9.

2D gel databases

COMPLUYEAST-2DPAGE

Q9QUM9.

REPRODUCTION-2DPAGE

Q9QUM9.

Proteomic databases

PaxDb

Q9QUM9.

PRIDE

Q9QUM9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000021412; ENSMUSP00000021412; ENSMUSG00000021024.

GeneID

26443.

KEGG

mmu:26443.

UCSC

uc007noq.2. mouse.

Organism-specific databases

CTD

5687.

MGI

MGI:1347006. Psma6.

Phylogenomic databases

eggNOG

COG0638.

GeneTree

ENSGT00550000074807.

HOGENOM

HOG000091084.

HOVERGEN

HBG107363.

InParanoid

Q9QUM9.

KO

K02730.

OMA

FRYKYGY.

OrthoDB

EOG4BP1CH.

Enzyme and pathway databases

Reactome

REACT_102124. Immune System.

Gene expression databases

ArrayExpress

Q9QUM9.

Bgee

Q9QUM9.

Genevestigator

Q9QUM9.

GermOnline

ENSMUSG00000021024. Mus musculus.

Family and domain databases

InterPro

IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]

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...

Other

ChiTaRS

PSMA6. mouse.

NextBio

304529.

SOURCE

Search...

Entry information

Entry name

PSA6_MOUSE

Accession

Primary (citable) accession number: Q9QUM9
Secondary accession number(s): Q0VGS3, Q3TT07, Q3U6Y2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program