Reviewed, UniProtKB/Swiss-Prot Q9R1P0 (PSA4_MOUSE)

Names and origin

Protein names

Recommended name:
    Proteasome subunit alpha type-4
    EC=3.4.25.1
Alternative name(s):
    Proteasome component C9
    Macropain subunit C9
    Multicatalytic endopeptidase complex subunit C9
    Proteasome subunit L

Gene names

Name:

Psma4

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	261 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.
Subcellular location	Cytoplasm. Nucleus.
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex, alpha-subunit complex Inferred from electronic annotation. Source: InterPro
Molecular function	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 – 261	261	Proteasome subunit alpha type-4		PRO_0000124105
Amino acid modifications
	Modified residue	13	1	Phosphoserine By similarity
	Modified residue	75	1	Phosphoserine By similarity
	Modified residue	127	1	N6-acetyllysine By similarity
	Modified residue	176	1	N6-acetyllysine By similarity
	Modified residue	238	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9R1P0-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: BB7CC8113791E13B	FASTA	261	29,471
	10 20 30 40 50 60 MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR NIHKLLDEVF 70 80 90 100 110 120 FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ YQEPIPCEQL VTALCDIKQA 130 140 150 160 170 180 YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK 190 200 210 220 230 240 EGEMTLKSAL ALAVKVLNKT MDVSKLSAEK VEIATLTRES GKTVIRVLKQ KEVEQLIKKH 250 260 EEEEAKAERE KKEKEQREKD K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 10436176] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: B10.BR.
[2]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and DBA/2. Tissue: Heart.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	Lubec G., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 55-64. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF060093 mRNA. Translation: AAD50538.1. AK085937 mRNA. Translation: BAC39573.1. AK168150 mRNA. Translation: BAE40115.1. BC001982 mRNA. Translation: AAH01982.1.
IPI	IPI00277001.
RefSeq	NP_036096.1.
UniGene	Mm.30270
3D structure databases
SMR	Q9R1P0. Positions 2-237.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9R1P0.
PTM databases
PhosphoSite	Q9R1P0.
Proteomic databases
PRIDE	Q9R1P0.
Genome annotation databases
Ensembl	ENSMUST00000034848; ENSMUSP00000034848; ENSMUSG00000032301; Mus musculus. [Genome view]
GeneID	26441.
KEGG	mmu:26441.
NMPDR	fig|10090.3.peg.20227.
UCSC	uc009pru.1. mouse.
Organism-specific databases
CTD	26441.
MGI	MGI:1347060. Psma4.
Phylogenomic databases
eggNOG	roNOG06617.
HOGENOM	HBG499923.
HOVERGEN	Q9R1P0.
InParanoid	Q9R1P0.
OMA	MARRYDS.
OrthoDB	EOG9J402D.
PhylomeDB	Q9R1P0.
Enzyme and pathway databases
BRENDA	3.4.25.1. 244.
Gene expression databases
ArrayExpress	Q9R1P0.
Bgee	Q9R1P0.
Genevestigator	Q9R1P0.
GermOnline	ENSMUSG00000032301. Mus musculus.
Family and domain databases
InterPro	IPR000426. Proteasome_asu_CS. IPR016050. Proteasome_bsu_CS. IPR001353. Proteasome_sua/b. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. PF10584. 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 Resources
NextBio	304521.
SOURCE	Search...

Entry information

Entry name

PSA4_MOUSE

Accession

Primary (citable) accession number: Q9R1P0
Secondary accession number(s): Q3THT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)