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Proteasome subunit alpha (EC 3.4.25.1) (20S proteasome alpha subunit) (Proteasome core protein PrcA)

 PSA_MYCTU               Reviewed;         248 AA.
P9WHU1; L0T8P4; O33244; Q7D7I3;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
12-SEP-2018, entry version 32.
RecName: Full=Proteasome subunit alpha {ECO:0000255|HAMAP-Rule:MF_00289};
EC=3.4.25.1 {ECO:0000255|HAMAP-Rule:MF_00289};
AltName: Full=20S proteasome alpha subunit {ECO:0000255|HAMAP-Rule:MF_00289};
AltName: Full=Proteasome core protein PrcA {ECO:0000255|HAMAP-Rule:MF_00289};
Name=prcA {ECO:0000255|HAMAP-Rule:MF_00289};
OrderedLocusNames=Rv2109c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY,
SUBSTRATE SPECIFICITY, SUBUNIT, ACTIVITY REGULATION, KINETIC
PARAMETERS, AND MUTAGENESIS OF 1-MET--SER-8.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16468985; DOI=10.1111/j.1365-2958.2005.05035.x;
Lin G., Hu G., Tsu C., Kunes Y.Z., Li H., Dick L., Parsons T., Li P.,
Chen Z., Zwickl P., Weich N., Nathan C.;
"Mycobacterium tuberculosis prcBA genes encode a gated proteasome with
broad oligopeptide specificity.";
Mol. Microbiol. 59:1405-1416(2006).
[3]
PROTEIN SUBSTRATES.
STRAIN=ATCC 25618 / H37Rv;
PubMed=17082771; DOI=10.1038/sj.emboj.7601405;
Pearce M.J., Arora P., Festa R.A., Butler-Wu S.M., Gokhale R.S.,
Darwin K.H.;
"Identification of substrates of the Mycobacterium tuberculosis
proteasome.";
EMBO J. 25:5423-5432(2006).
[4]
IDENTIFICATION BY MASS SPECTROMETRY, DETERMINATION OF TRANSLATIONAL
START SITE, CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT
SER-2.
STRAIN=ATCC 25618 / H37Rv;
PubMed=17259624; DOI=10.1099/mic.0.2006/001537-0;
Rison S.C., Mattow J., Jungblut P.R., Stoker N.G.;
"Experimental determination of translational starts using peptide mass
mapping and tandem mass spectrometry within the proteome of
Mycobacterium tuberculosis.";
Microbiology 153:521-528(2007).
[5]
ROLE IN VIRULENCE, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18059281; DOI=10.1038/nm1683;
Gandotra S., Schnappinger D., Monteleone M., Hillen W., Ehrt S.;
"In vivo gene silencing identifies the Mycobacterium tuberculosis
proteasome as essential for the bacteria to persist in mice.";
Nat. Med. 13:1515-1520(2007).
[6]
IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
PubMed=19099550; DOI=10.1186/1752-0509-2-109;
Raman K., Yeturu K., Chandra N.;
"targetTB: a target identification pipeline for Mycobacterium
tuberculosis through an interactome, reactome and genome-scale
structural analysis.";
BMC Syst. Biol. 2:109-109(2008).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[8]
ELECTRON MICROSCOPY, AND SUBUNIT.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20085764; DOI=10.1016/j.febslet.2009.12.057;
Poulsen C., Holton S., Geerlof A., Wilmanns M., Song Y.H.;
"Stoichiometric protein complex formation and over-expression using
the prokaryotic native operon structure.";
FEBS Lett. 584:669-674(2010).
[9]
ROLE IN PERSISTENCE, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=20711362; DOI=10.1371/journal.ppat.1001040;
Gandotra S., Lebron M.B., Ehrt S.;
"The Mycobacterium tuberculosis proteasome active site threonine is
essential for persistence yet dispensable for replication and
resistance to nitric oxide.";
PLoS Pathog. 6:E1001040-E1001040(2010).
[10]
PHOSPHORYLATION AT THR-84; THR-178 AND THR-202.
STRAIN=H37Rv;
PubMed=25224505; DOI=10.1007/s12275-014-4416-2;
Anandan T., Han J., Baun H., Nyayapathy S., Brown J.T., Dial R.L.,
Moltalvo J.A., Kim M.S., Yang S.H., Ronning D.R., Husson R.N., Suh J.,
Kang C.M.;
"Phosphorylation regulates mycobacterial proteasome.";
J. Microbiol. 52:743-754(2014).
[11]
INTERACTION WITH BPA.
STRAIN=ATCC 25618 / H37Rv;
PubMed=25469515; DOI=10.1371/journal.pone.0114348;
Delley C.L., Laederach J., Ziemski M., Bolten M., Boehringer D.,
Weber-Ban E.;
"Bacterial proteasome activator Bpa (Rv3780) is a novel ring-shaped
interactor of the mycobacterial proteasome.";
PLoS ONE 9:E114348-E114348(2014).
[12]
X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 2-248 IN COMPLEXES WITH THE
BETA SUBUNIT AND WITH THE MLN-273 INHIBITOR, AND SUBUNIT.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16468986; DOI=10.1111/j.1365-2958.2005.05036.x;
Hu G., Lin G., Wang M., Dick L., Xu R.-M., Nathan C., Li H.;
"Structure of the Mycobacterium tuberculosis proteasome and mechanism
of inhibition by a peptidyl boronate.";
Mol. Microbiol. 59:1417-1428(2006).
[13]
X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF WILD-TYPE AND OPEN-GATE
MUTANT IN COMPLEXES WITH BETA SUBUNIT; INHIBITOR HT1171 AND INHIBITOR
GL1, ACTIVITY REGULATION, AND BIOTECHNOLOGY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=19759536; DOI=10.1038/nature08357;
Lin G., Li D., de Carvalho L.P., Deng H., Tao H., Vogt G., Wu K.,
Schneider J., Chidawanyika T., Warren J.D., Li H., Nathan C.;
"Inhibitors selective for mycobacterial versus human proteasomes.";
Nature 461:621-626(2009).
[14]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT
AND FELLUTAMIDE B INHIBITOR, AND ACTIVITY REGULATION.
PubMed=20558127; DOI=10.1016/j.abb.2010.06.009;
Lin G., Li D., Chidawanyika T., Nathan C., Li H.;
"Fellutamide B is a potent inhibitor of the Mycobacterium tuberculosis
proteasome.";
Arch. Biochem. Biophys. 501:214-220(2010).
[15]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF WILD-TYPE AND OPEN-GATE
MUTANT IN COMPLEX WITH BETA SUBUNIT, SUBUNIT, GATED STRUCTURE, AND
PROTEASOME ASSEMBLY PROCESS.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20461058; DOI=10.1038/emboj.2010.95;
Li D., Li H., Wang T., Pan H., Lin G., Li H.;
"Structural basis for the assembly and gate closure mechanisms of the
Mycobacterium tuberculosis 20S proteasome.";
EMBO J. 29:2037-2047(2010).
-!- FUNCTION: Component of the proteasome core, a large protease
complex with broad specificity involved in protein degradation.
The M.tuberculosis proteasome is able to cleave oligopeptides not
only after hydrophobic but also after basic, acidic and small
neutral residues (PubMed:16468985). In complex with the ATPase
Mpa, degrades protein targets conjugated to a prokaryotic
ubiquitin-like protein (Pup). Among the identified substrates of
the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa
proteins (PubMed:17082771). One function of the proteasome is to
contribute to M.tuberculosis ability to resist killing by host
macrophages, since the core proteasome is essential for
persistence of the pathogen during the chronic phase of infection
in mice (PubMed:18059281). Likely functions to recycle amino acids
under nutrient starvation, thereby enabling the cell to maintain
basal metabolic activities (PubMed:20711362) (By similarity). The
mechanism of protection against bactericidal chemistries of the
host's immune response probably involves the degradation of
proteins that are irreversibly oxidized, nitrated, or nitrosated.
A proteolysis-independent activity of the proteasome core is
required for optimal growth of M.tuberculosis in mouse lungs and
for RNI resistance; in contrast, long-term survival of
M.tuberculosis in stationary phase and during starvation in vitro
and in the chronic phase of mouse infection required a
proteolytically active proteasome (PubMed:20711362).
{ECO:0000250|UniProtKB:A0QZ46, ECO:0000255|HAMAP-Rule:MF_00289,
ECO:0000269|PubMed:16468985, ECO:0000269|PubMed:17082771,
ECO:0000269|PubMed:18059281, ECO:0000269|PubMed:20711362}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000255|HAMAP-Rule:MF_00289,
ECO:0000269|PubMed:16468985}.
-!- ACTIVITY REGULATION: The formation of the proteasomal ATPase ARC-
20S proteasome complex, likely via the docking of the C-termini of
ARC into the intersubunit pockets in the alpha-rings, may trigger
opening of the gate for substrate entry. Interconversion between
the open-gate and close-gate conformations leads to a dynamic
regulation of the 20S proteasome proteolysis activity. In vitro,
chymotryptic and tryptic activities of the proteasome are both
completely inhibited by epoxomicin and by the peptidyl boronate
inhibitor MLN-273. Also inhibited by Mg(2+), Ca(2+) and SDS. It
was also shown that certain oxathiazol-2-one compounds can act as
selective suicide-substrate inhibitors of the M.tuberculosis
proteasome by irreversibly cyclocarbonylating its active site
threonine. Proteasome activity is potently inhibited by
fellutamide B (Ki=6.8 nM), a lipopeptide aldehyde that forms a
reversible bond with the beta-OH of the active site threonine
(PubMed:20558127). {ECO:0000255|HAMAP-Rule:MF_00289,
ECO:0000269|PubMed:16468985, ECO:0000269|PubMed:19759536,
ECO:0000269|PubMed:20558127}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=56 uM for succinyl-LLVY-7-amino-4-methylcoumarin
{ECO:0000269|PubMed:16468985};
Vmax=0.24 nmol/min/mg enzyme with succinyl-LLVY-7-amino-4-
methylcoumarin as substrate {ECO:0000269|PubMed:16468985};
-!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
{ECO:0000255|HAMAP-Rule:MF_00289}.
-!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14
beta subunits that assemble into four stacked heptameric rings,
resulting in a barrel-shaped structure. The two inner rings, each
composed of seven catalytic beta subunits, are sandwiched by two
outer rings, each composed of seven alpha subunits. The catalytic
chamber with the active sites is on the inside of the barrel. Has
a gated structure, the ends of the cylinder being occluded by the
N-termini of the alpha-subunits. Is capped by the proteasome-
associated ATPase, ARC (Mpa). Can also interact with the bacterial
proteasome activator Bpa through the C-terminal hydrophobic-
tyrosine-X motif (HbYX motif) of Bpa; Bpa forms a homooligomeric
ring-like structure which stacks co-axially with the proteasomal
alpha-rings (PubMed:25469515). {ECO:0000255|HAMAP-Rule:MF_00289,
ECO:0000269|PubMed:16468985, ECO:0000269|PubMed:16468986,
ECO:0000269|PubMed:20085764, ECO:0000269|PubMed:20461058,
ECO:0000269|PubMed:25469515}.
-!- INTERACTION:
P9WHT9:prcB; NbExp=6; IntAct=EBI-7948002, EBI-7947958;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
-!- PTM: Phosphorylated by the PknB kinase at three threonine residues
(Thr-84, Thr-202, and Thr-178) in a sequential manner.
Phosphorylation enhances proteolytic activity of the proteasome.
{ECO:0000269|PubMed:25224505}.
-!- DISRUPTION PHENOTYPE: Cells lacking the core proteasome prcBA
subunits exhibit reduced growth and persistence in mice. They are
also attenuated in interferon-gamma-deficient mice. They also
display increased sensitivity to reactive nitrogen intermediates
(RNI) and increased resistance to oxidative stress.
{ECO:0000269|PubMed:18059281, ECO:0000269|PubMed:20711362}.
-!- BIOTECHNOLOGY: In the course of search for new antibiotics, a
class of oxathiazol-2-one compounds has been identified that
selectively inhibits the M.tuberculosis proteasome over the human
proteasome and that kills non-replicating M.tuberculosis.
{ECO:0000269|PubMed:19759536}.
-!- MISCELLANEOUS: Was identified as a high-confidence drug target.
-!- SIMILARITY: Belongs to the peptidase T1A family.
{ECO:0000255|HAMAP-Rule:MF_00289}.
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EMBL; AL123456; CCP44884.1; -; Genomic_DNA.
PIR; H70511; H70511.
RefSeq; NP_216625.1; NC_000962.3.
RefSeq; WP_003906749.1; NZ_KK339370.1.
PDB; 2FHG; X-ray; 3.23 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=2-248.
PDB; 2FHH; X-ray; 2.99 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=2-248.
PDB; 3H6F; X-ray; 2.51 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=1-248.
PDB; 3H6I; X-ray; 2.43 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=1-248.
PDB; 3HF9; X-ray; 2.88 A; 1/3/A/B/D/F/I/K/M/O/Q/S/U/W/Y/a/b/d/f/i/k/m/o/q/s/u/w/y=10-248.
PDB; 3HFA; X-ray; 2.50 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=10-248.
PDB; 3KRD; X-ray; 2.50 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=1-248.
PDB; 3MFE; X-ray; 2.60 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=10-248.
PDB; 3MI0; X-ray; 2.20 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=1-248.
PDB; 3MKA; X-ray; 2.51 A; 1/A/B/D/F/I/K/M/O/Q/S/U/W/Y=1-248.
PDB; 5LZP; EM; 3.45 A; 0/2/4/6/8/B/D/H/J/M/Q/S/W/Y=8-248.
PDB; 5THO; X-ray; 3.00 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
PDB; 5TRG; X-ray; 2.80 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
PDB; 5TRR; X-ray; 3.10 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
PDB; 5TRS; X-ray; 3.08 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
PDB; 5TRY; X-ray; 3.00 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
PDB; 5TS0; X-ray; 2.85 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=10-248.
PDB; 6BGL; EM; 3.40 A; A/C/D/E/F/G/H/I/J/K/L/M/N/O=1-248.
PDB; 6BGO; EM; 4.20 A; A/C/D/E/F/G/H/I/J/K/L/M/N/O=1-248.
PDBsum; 2FHG; -.
PDBsum; 2FHH; -.
PDBsum; 3H6F; -.
PDBsum; 3H6I; -.
PDBsum; 3HF9; -.
PDBsum; 3HFA; -.
PDBsum; 3KRD; -.
PDBsum; 3MFE; -.
PDBsum; 3MI0; -.
PDBsum; 3MKA; -.
PDBsum; 5LZP; -.
PDBsum; 5THO; -.
PDBsum; 5TRG; -.
PDBsum; 5TRR; -.
PDBsum; 5TRS; -.
PDBsum; 5TRY; -.
PDBsum; 5TS0; -.
PDBsum; 6BGL; -.
PDBsum; 6BGO; -.
ProteinModelPortal; P9WHU1; -.
SMR; P9WHU1; -.
IntAct; P9WHU1; 1.
MINT; P9WHU1; -.
STRING; 83332.Rv2109c; -.
iPTMnet; P9WHU1; -.
PaxDb; P9WHU1; -.
PRIDE; P9WHU1; -.
EnsemblBacteria; CCP44884; CCP44884; Rv2109c.
GeneID; 887538; -.
KEGG; mtu:Rv2109c; -.
TubercuList; Rv2109c; -.
eggNOG; ENOG4105F7N; Bacteria.
eggNOG; COG0638; LUCA.
KO; K03432; -.
OMA; KYNEFEN; -.
PhylomeDB; P9WHU1; -.
UniPathway; UPA00997; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:UniProtKB.
GO; GO:0004298; F:threonine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0019941; P:modification-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0009405; P:pathogenesis; IDA:MTBBASE.
GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:MTBBASE.
Gene3D; 3.60.20.10; -; 1.
HAMAP; MF_00289_B; Proteasome_A_B; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR023332; Proteasome_alpha-type.
InterPro; IPR022296; Proteasome_asu_bac.
InterPro; IPR001353; Proteasome_sua/b.
PANTHER; PTHR11599:SF69; PTHR11599:SF69; 1.
Pfam; PF00227; Proteasome; 1.
SUPFAM; SSF56235; SSF56235; 1.
TIGRFAMs; TIGR03691; 20S_bact_alpha; 1.
PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Phosphoprotein; Protease;
Proteasome; Reference proteome; Threonine protease; Virulence.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:21969609,
ECO:0000269|PubMed:17259624}.
CHAIN 2 248 Proteasome subunit alpha.
/FTId=PRO_0000383482.
MOD_RES 2 2 N-acetylserine; partial.
{ECO:0000244|PubMed:21969609,
ECO:0000269|PubMed:17259624}.
MOD_RES 84 84 Phosphothreonine.
{ECO:0000269|PubMed:25224505}.
MOD_RES 178 178 Phosphothreonine.
{ECO:0000269|PubMed:25224505}.
MOD_RES 202 202 Phosphothreonine.
{ECO:0000269|PubMed:25224505}.
MUTAGEN 1 8 Missing: Markedly increases peptidolytic
activity. Disappearance of the apparent
obstruction in alpha rings. Designated
open-gate mutant.
{ECO:0000269|PubMed:16468985}.
HELIX 9 25 {ECO:0000244|PDB:3MI0}.
STRAND 30 35 {ECO:0000244|PDB:3MI0}.
STRAND 38 44 {ECO:0000244|PDB:3MI0}.
STRAND 48 50 {ECO:0000244|PDB:3MI0}.
STRAND 52 57 {ECO:0000244|PDB:3MI0}.
STRAND 60 66 {ECO:0000244|PDB:3MI0}.
HELIX 68 88 {ECO:0000244|PDB:3MI0}.
HELIX 91 93 {ECO:0000244|PDB:3MI0}.
HELIX 96 113 {ECO:0000244|PDB:3MI0}.
STRAND 114 116 {ECO:0000244|PDB:3MI0}.
STRAND 120 126 {ECO:0000244|PDB:3MI0}.
STRAND 130 132 {ECO:0000244|PDB:3HF9}.
STRAND 137 141 {ECO:0000244|PDB:3MI0}.
STRAND 147 158 {ECO:0000244|PDB:3MI0}.
HELIX 160 170 {ECO:0000244|PDB:3MI0}.
HELIX 171 173 {ECO:0000244|PDB:3HFA}.
HELIX 177 190 {ECO:0000244|PDB:3MI0}.
HELIX 205 207 {ECO:0000244|PDB:3H6I}.
STRAND 208 214 {ECO:0000244|PDB:3MI0}.
STRAND 217 219 {ECO:0000244|PDB:3MI0}.
STRAND 222 224 {ECO:0000244|PDB:3MI0}.
HELIX 227 232 {ECO:0000244|PDB:3MI0}.
SEQUENCE 248 AA; 26881 MW; 0356FED74869998A CRC64;
MSFPYFISPE QAMRERSELA RKGIARAKSV VALAYAGGVL FVAENPSRSL QKISELYDRV
GFAAAGKFNE FDNLRRGGIQ FADTRGYAYD RRDVTGRQLA NVYAQTLGTI FTEQAKPYEV
ELCVAEVAHY GETKRPELYR ITYDGSIADE PHFVVMGGTT EPIANALKES YAENASLTDA
LRIAVAALRA GSADTSGGDQ PTLGVASLEV AVLDANRPRR AFRRITGSAL QALLVDQESP
QSDGESSG


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18-003-44182 Proteasome subunit alpha type-1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.1 mg Protein A
EIAAB32718 HC9,Homo sapiens,Human,Macropain subunit C9,Multicatalytic endopeptidase complex subunit C9,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,PSC9,PSMA4
EIAAB32714 Macropain subunit C8,Mouse,Multicatalytic endopeptidase complex subunit C8,Mus musculus,Proteasome component C8,Proteasome subunit alpha type-3,Proteasome subunit K,Psma3
EIAAB32715 Macropain subunit C9,Mouse,Multicatalytic endopeptidase complex subunit C9,Mus musculus,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,Psma4
EIAAB32716 Macropain subunit C9,Multicatalytic endopeptidase complex subunit C9,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,Psma4,Rat,Rattus norvegicus
EIAAB32711 Macropain subunit C8,Multicatalytic endopeptidase complex subunit C8,Proteasome component C8,Proteasome subunit alpha type-3,Proteasome subunit K,Psma3,Rat,Rattus norvegicus
EIAAB32704 Macropain subunit C2,Mouse,Multicatalytic endopeptidase complex subunit C2,Mus musculus,Proteasome component C2,Proteasome nu chain,Proteasome subunit alpha type-1,Psma1
EIAAB32706 Macropain subunit C2,Multicatalytic endopeptidase complex subunit C2,Proteasome component C2,Proteasome nu chain,Proteasome subunit alpha type-1,Psma1,Rat,Rattus norvegicus
EIAAB32729 Homo sapiens,HSPC,Human,Proteasome subunit alpha type-7,Proteasome subunit RC6-1,Proteasome subunit XAPC7,PSMA7
EIAAB32808 26S proteasome non-ATPase regulatory subunit 7,26S proteasome regulatory subunit RPN8,26S proteasome regulatory subunit S12,Homo sapiens,Human,Mov34 protein homolog,MOV34L,Proteasome subunit p40,PSMD7
EIAAB32776 Homo sapiens,Human,LMP7,Low molecular mass protein 7,Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit b
EIAAB32846 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Homo sapiens,Human,Protein 55.11,PSMD2,TRAP2,Tumor
EIAAB32703 30 kDa prosomal protein,HC2,Homo sapiens,Human,Macropain subunit C2,Multicatalytic endopeptidase complex subunit C2,NU,PROS30,PROS-30,Proteasome component C2,Proteasome nu chain,Proteasome subunit alp
EIAAB32772 Lmp7,Low molecular mass protein 7,Macropain subunit C13,Mc13,Mouse,Multicatalytic endopeptidase complex subunit C13,Mus musculus,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subu
EIAAB32847 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Bos taurus,Bovine,PSMD2,TRAP2,Tumor necrosis facto
EIAAB32654 26S protease regulatory subunit 6A,26S proteasome AAA-ATPase subunit RPT5,Homo sapiens,Human,Proteasome 26S subunit ATPase 3,Proteasome subunit P50,PSMC3,Tat-binding protein 1,TBP1,TBP-1
EIAAB32669 26S protease regulatory subunit 8,26S proteasome AAA-ATPase subunit RPT6,p45_SUG,Pig,Proteasome 26S subunit ATPase 5,Proteasome subunit p45,PSMC5,Sus scrofa,Tat-binding protein homolog 10,TBP10
EIAAB32710 Macropain subunit C3,Multicatalytic endopeptidase complex subunit C3,Proteasome component C3,Proteasome subunit alpha type-2,Psma2,Rat,Rattus norvegicus
EIAAB32850 26S proteasome non-ATPase regulatory subunit 3,26S proteasome regulatory subunit RPN3,26S proteasome regulatory subunit S3,Mouse,Mus musculus,P91a,Proteasome subunit p58,Psmd3,Transplantation antigen
EIAAB32707 Lmpc3,Macropain subunit C3,Mouse,Multicatalytic endopeptidase complex subunit C3,Mus musculus,Proteasome component C3,Proteasome subunit alpha type-2,Psma2


 

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