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Proteasome-associated ATPase (AAA ATPase forming ring-shaped complexes) (ARC) (Mycobacterial proteasome ATPase)

 ARC_MYCTU               Reviewed;         609 AA.
P9WQN5; L0T8W3; O33250; P63345; Q0G9Y7;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
12-SEP-2018, entry version 30.
RecName: Full=Proteasome-associated ATPase {ECO:0000255|HAMAP-Rule:MF_02112};
AltName: Full=AAA ATPase forming ring-shaped complexes {ECO:0000255|HAMAP-Rule:MF_02112};
Short=ARC {ECO:0000255|HAMAP-Rule:MF_02112};
AltName: Full=Mycobacterial proteasome ATPase {ECO:0000255|HAMAP-Rule:MF_02112};
Name=mpa {ECO:0000255|HAMAP-Rule:MF_02112}; OrderedLocusNames=Rv2115c;
ORFNames=MTCY261.11c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN ATPASE,
BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND
MUTAGENESIS OF LYS-299; ASP-371; GLU-372 AND 608-TYR-GLU-609.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15659170; DOI=10.1111/j.1365-2958.2004.04403.x;
Darwin K.H., Lin G., Chen Z., Li H., Nathan C.F.;
"Characterization of a Mycobacterium tuberculosis proteasomal ATPase
homologue.";
Mol. Microbiol. 55:561-571(2005).
[2]
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).
[3]
GENE NAME, ROLE IN RESISTANCE TO RNI, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=14671303; DOI=10.1126/science.1091176;
Darwin K.H., Ehrt S., Gutierrez-Ramos J.-C., Weich N., Nathan C.F.;
"The proteasome of Mycobacterium tuberculosis is required for
resistance to nitric oxide.";
Science 302:1963-1966(2003).
[4]
TARGET OF RNI, AND S-NITROSYLATION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15626759; DOI=10.1073/pnas.0406133102;
Rhee K.Y., Erdjument-Bromage H., Tempst P., Nathan C.F.;
"S-nitroso proteome of Mycobacterium tuberculosis: enzymes of
intermediary metabolism and antioxidant defense.";
Proc. Natl. Acad. Sci. U.S.A. 102:467-472(2005).
[5]
FUNCTION IN THE PROTEASOME DEGRADATION PATHWAY, REGULATION OF MPA
LEVELS, PROTEASOME SUBSTRATE, AND MUTAGENESIS OF TYR-608 AND
608-TYR-GLU-609.
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).
[6]
INTERACTION WITH PUP, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18832610; DOI=10.1126/science.1163885;
Pearce M.J., Mintseris J., Ferreyra J., Gygi S.P., Darwin K.H.;
"Ubiquitin-like protein involved in the proteasome pathway of
Mycobacterium tuberculosis.";
Science 322:1104-1107(2008).
[7]
INTERACTION WITH PUP.
PubMed=19580545; DOI=10.1042/BJ20090738;
Liao S., Shang Q., Zhang X., Zhang J., Xu C., Tu X.;
"Pup, a prokaryotic ubiquitin-like protein, is an intrinsically
disordered protein.";
Biochem. J. 422:207-215(2009).
[8]
INTERACTION WITH PUP, STOICHIOMETRY OF THE PUP-MPA COMPLEX, AND
DOMAIN.
STRAIN=ATCC 25618 / H37Rv;
PubMed=19761766; DOI=10.1016/j.febslet.2009.09.020;
Sutter M., Striebel F., Damberger F.F., Allain F.H., Weber-Ban E.;
"A distinct structural region of the prokaryotic ubiquitin-like
protein (Pup) is recognized by the N-terminal domain of the
proteasomal ATPase Mpa.";
FEBS Lett. 583:3151-3157(2009).
[9]
INTERACTION WITH PUP, AND STOICHIOMETRY OF THE PUP-MPA COMPLEX.
PubMed=19607839; DOI=10.1016/j.jmb.2009.07.018;
Chen X., Solomon W.C., Kang Y., Cerda-Maira F., Darwin K.H.,
Walters K.J.;
"Prokaryotic ubiquitin-like protein Pup is intrinsically disordered.";
J. Mol. Biol. 392:208-217(2009).
[10]
INTERACTION WITH PUP, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=19448618; DOI=10.1038/nsmb.1597;
Striebel F., Imkamp F., Sutter M., Steiner M., Mamedov A.,
Weber-Ban E.;
"Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to
substrates by distinct but homologous enzymes.";
Nat. Struct. Mol. Biol. 16:647-651(2009).
[11]
FUNCTION AS UNFOLDASE AND TRANSLOCASE, DOMAIN, MUTAGENESIS OF PHE-341
AND 608-TYR-GLU-609, AND RECONSTITUTION OF THE PROTEASOME DEGRADATION
PATHWAY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20203624; DOI=10.1038/emboj.2010.23;
Striebel F., Hunkeler M., Summer H., Weber-Ban E.;
"The mycobacterial Mpa-proteasome unfolds and degrades pupylated
substrates by engaging Pup's N-terminus.";
EMBO J. 29:1262-1271(2010).
[12]
PUPYLATION AT LYS-591, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20066036; DOI=10.1371/journal.pone.0008589;
Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
Gygi S.P., Darwin K.H.;
"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium
tuberculosis.";
PLoS ONE 5:E8589-E8589(2010).
[13]
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).
[14]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 98-245, FUNCTION, INTERACTION
WITH PROTEASOME, DOMAIN, AND MUTAGENESIS OF ARG-120; ARG-173; TRP-187;
LYS-225; LYS-235; LYS-299; VAL-342; ASP-371 AND TYR-608.
STRAIN=ATCC 25618 / H37Rv;
PubMed=19836337; DOI=10.1016/j.str.2009.08.010;
Wang T., Li H., Lin G., Tang C., Li D., Nathan C., Darwin K.H., Li H.;
"Structural insights on the Mycobacterium tuberculosis proteasomal
ATPase Mpa.";
Structure 17:1377-1385(2009).
-!- FUNCTION: ATPase which is responsible for recognizing, binding,
unfolding and translocation of pupylated proteins into the
bacterial 20S proteasome core particle. May be essential for
opening the gate of the 20S proteasome via an interaction with its
C-terminus, thereby allowing substrate entry and access to the
site of proteolysis. Thus, the C-termini of the proteasomal ATPase
may function like a 'key in a lock' to induce gate opening and
therefore regulate proteolysis. Is required but not sufficient to
confer resistance against the lethal effects of reactive nitrogen
intermediates (RNI), antimicrobial molecules produced by activated
macrophages and other cell types. {ECO:0000255|HAMAP-
Rule:MF_02112, ECO:0000269|PubMed:14671303,
ECO:0000269|PubMed:15659170, ECO:0000269|PubMed:17082771,
ECO:0000269|PubMed:19836337, ECO:0000269|PubMed:20203624}.
-!- ACTIVITY REGULATION: ATPase activity is inhibited by EDTA, N-
ethylmaleimide (NEM) and sodium azide.
{ECO:0000269|PubMed:15659170}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=330 uM for ATP {ECO:0000269|PubMed:15659170};
Vmax=62 pmol/min/ug enzyme {ECO:0000269|PubMed:15659170};
pH dependence:
Optimum pH is 7.4-7.5. {ECO:0000269|PubMed:15659170};
-!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
{ECO:0000255|HAMAP-Rule:MF_02112}.
-!- SUBUNIT: Homohexamer. Assembles into a hexameric ring structure
that caps the 20S proteasome core. Strongly interacts with the
prokaryotic ubiquitin-like protein Pup through a hydrophobic
interface; the interacting region of Mpa lies in its N-terminal
coiled-coil domain. There is one Pup binding site per Mpa hexamer
ring; the K(D) measured is about 3.8 uM. Upon ATP-binding, the C-
terminus of Mpa interacts with the alpha-rings of the proteasome
core, possibly by binding to the intersubunit pockets.
{ECO:0000255|HAMAP-Rule:MF_02112, ECO:0000269|PubMed:15659170,
ECO:0000269|PubMed:18832610, ECO:0000269|PubMed:19448618,
ECO:0000269|PubMed:19580545, ECO:0000269|PubMed:19607839,
ECO:0000269|PubMed:19761766, ECO:0000269|PubMed:19836337}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-7241067, EBI-7241067;
P9WHN5:pup; NbExp=6; IntAct=EBI-7241067, EBI-7241023;
-!- DOMAIN: Consists of three main regions, an N-terminal coiled-coil
domain (residues 1-96) that binds to protein Pup and functions as
a docking station, an interdomain (residues 97-245) involved in
Mpa hexamerization, and a C-terminal ATPase domain of the AAA type
(residues 246-609). {ECO:0000269|PubMed:19761766,
ECO:0000269|PubMed:19836337, ECO:0000269|PubMed:20203624}.
-!- PTM: Pupylated at Lys-591 by the prokaryotic ubiquitin-like
protein Pup, which leads to its degradation by the proteasome. Mpa
thus promotes its own turnover. {ECO:0000269|PubMed:20066036}.
-!- PTM: Mpa is a target of RNI, thereby is S-nitrosylated in the
phagosome of immunologically activated host macrophages, which
causes enzyme inhibition. {ECO:0000269|PubMed:15626759}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate pupylated
proteins. These cells also become hypersensitive to reactive
nitrogen intermediates (RNI) and are severely attenuated in both
wild-type and nitric oxide synthase 2 deficient mice. Moreover,
they display increased resistance to hydrogen peroxide.
{ECO:0000269|PubMed:14671303, ECO:0000269|PubMed:18832610}.
-!- MISCELLANEOUS: Was identified as a natural substrate of the
M.tuberculosis proteasome.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP-
Rule:MF_02112}.
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EMBL; DQ888314; ABI36485.1; -; Genomic_DNA.
EMBL; AL123456; CCP44890.1; -; Genomic_DNA.
PIR; F70512; F70512.
RefSeq; NP_216631.1; NC_000962.3.
RefSeq; WP_003411035.1; NZ_KK339370.1.
PDB; 3FP9; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=98-245.
PDB; 3M91; X-ray; 1.80 A; A/C=46-96.
PDB; 3M9B; X-ray; 3.94 A; A/B/C/D/E/F/G/H/I/J/K/L=1-234.
PDB; 3M9D; X-ray; 4.50 A; A/B/C/D/E/F/J/K/L/M/N/O=1-234.
PDB; 3M9H; X-ray; 2.00 A; A/B/C/D/E/F=46-96.
PDB; 5KWA; X-ray; 2.90 A; A/B=95-602.
PDB; 5KZF; X-ray; 3.49 A; A/B/C/D/E/F/G/H/I/J/K/L=98-609.
PDBsum; 3FP9; -.
PDBsum; 3M91; -.
PDBsum; 3M9B; -.
PDBsum; 3M9D; -.
PDBsum; 3M9H; -.
PDBsum; 5KWA; -.
PDBsum; 5KZF; -.
ProteinModelPortal; P9WQN5; -.
SMR; P9WQN5; -.
IntAct; P9WQN5; 1.
MINT; P9WQN5; -.
STRING; 83332.Rv2115c; -.
PaxDb; P9WQN5; -.
EnsemblBacteria; CCP44890; CCP44890; Rv2115c.
GeneID; 887297; -.
KEGG; mtu:Rv2115c; -.
TubercuList; Rv2115c; -.
eggNOG; ENOG4105DHM; Bacteria.
eggNOG; COG0464; LUCA.
KO; K13527; -.
OMA; CVDEFKE; -.
PhylomeDB; P9WQN5; -.
UniPathway; UPA00997; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0022623; C:proteasome-activating nucleotidase complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0070628; F:proteasome binding; IPI:MTBBASE.
GO; GO:0140035; F:ubiquitination-like modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0071732; P:cellular response to nitric oxide; IMP:UniProtKB.
GO; GO:0019941; P:modification-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0009405; P:pathogenesis; IMP:UniProtKB.
GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB.
GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:MTBBASE.
GO; GO:0043335; P:protein unfolding; IDA:UniProtKB.
GO; GO:0051409; P:response to nitrosative stress; IMP:MTBBASE.
HAMAP; MF_02112; ARC_ATPase; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR032501; Prot_ATP_ID_OB.
InterPro; IPR022482; Proteasome_ATPase.
Pfam; PF00004; AAA; 1.
Pfam; PF16450; Prot_ATP_ID_OB; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 2.
TIGRFAMs; TIGR03689; pup_AAA; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Chaperone; Coiled coil; Complete proteome;
Isopeptide bond; Nucleotide-binding; Proteasome; Reference proteome;
S-nitrosylation; Ubl conjugation; Virulence.
CHAIN 1 609 Proteasome-associated ATPase.
/FTId=PRO_0000084778.
NP_BIND 296 301 ATP. {ECO:0000255|HAMAP-Rule:MF_02112}.
REGION 608 609 Docks into pockets in the proteasome
alpha-ring. {ECO:0000255|HAMAP-
Rule:MF_02112}.
COILED 20 96 {ECO:0000255|HAMAP-Rule:MF_02112}.
CROSSLNK 591 591 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-Cter in protein Pup).
{ECO:0000269|PubMed:20066036}.
MUTAGEN 120 120 R->A: Does not dramatically affect
proteasome substrate degradation.
{ECO:0000269|PubMed:19836337}.
MUTAGEN 173 173 R->E: Impairs Mpa hexamerization; when
associated with A-187 and E-235.
{ECO:0000269|PubMed:19836337}.
MUTAGEN 187 187 W->A: Impairs Mpa hexamerization; when
associated with E-173 and E-235.
{ECO:0000269|PubMed:19836337}.
MUTAGEN 225 225 K->A: Does not dramatically affect
proteasome substrate degradation.
{ECO:0000269|PubMed:19836337}.
MUTAGEN 235 235 K->E: Impairs Mpa hexamerization; when
associated with E-173 and A-187.
{ECO:0000269|PubMed:19836337}.
MUTAGEN 299 299 K->Q: Reduces both ATPase activity and
ATP affinity. Abolishes proteasome
substrate degradation and protection
against RNI.
{ECO:0000269|PubMed:15659170,
ECO:0000269|PubMed:19836337}.
MUTAGEN 341 341 F->A: Abolishes unfolding capacity.
{ECO:0000269|PubMed:20203624}.
MUTAGEN 341 341 F->Y: No effect on unfolding capacity.
{ECO:0000269|PubMed:20203624}.
MUTAGEN 342 342 V->A: Abolishes proteasome substrate
degradation.
{ECO:0000269|PubMed:19836337}.
MUTAGEN 371 371 D->A: Severely reduces ATPase activity.
Abolishes proteasome substrate
degradation and protection against RNI.
{ECO:0000269|PubMed:15659170,
ECO:0000269|PubMed:19836337}.
MUTAGEN 372 372 E->A: Severely reduces ATPase activity.
Abolishes protection against RNI.
{ECO:0000269|PubMed:15659170}.
MUTAGEN 372 372 E->Q: Abolishes protection against RNI.
{ECO:0000269|PubMed:15659170}.
MUTAGEN 608 609 Missing: Retains ATPase and unfolding
activities, yet abolishes proteasome
substrate degradation and protection
against RNI. Is also highly attenuated in
mice. {ECO:0000269|PubMed:15659170,
ECO:0000269|PubMed:17082771,
ECO:0000269|PubMed:20203624}.
MUTAGEN 608 608 Y->E,F: Abolishes proteasome substrate
degradation and protection against RNI.
{ECO:0000269|PubMed:17082771,
ECO:0000269|PubMed:19836337}.
HELIX 53 94 {ECO:0000244|PDB:3M91}.
STRAND 99 107 {ECO:0000244|PDB:3FP9}.
STRAND 109 117 {ECO:0000244|PDB:3FP9}.
STRAND 120 126 {ECO:0000244|PDB:3FP9}.
HELIX 132 134 {ECO:0000244|PDB:5KWA}.
STRAND 140 143 {ECO:0000244|PDB:3FP9}.
STRAND 149 152 {ECO:0000244|PDB:3FP9}.
STRAND 158 167 {ECO:0000244|PDB:3FP9}.
STRAND 171 177 {ECO:0000244|PDB:3FP9}.
STRAND 183 188 {ECO:0000244|PDB:3FP9}.
HELIX 190 193 {ECO:0000244|PDB:3FP9}.
HELIX 203 205 {ECO:0000244|PDB:3FP9}.
STRAND 219 223 {ECO:0000244|PDB:3FP9}.
TURN 224 227 {ECO:0000244|PDB:3FP9}.
STRAND 228 233 {ECO:0000244|PDB:3FP9}.
HELIX 238 245 {ECO:0000244|PDB:3FP9}.
TURN 251 253 {ECO:0000244|PDB:5KWA}.
HELIX 258 268 {ECO:0000244|PDB:5KWA}.
HELIX 270 273 {ECO:0000244|PDB:5KWA}.
HELIX 275 280 {ECO:0000244|PDB:5KWA}.
STRAND 288 294 {ECO:0000244|PDB:5KWA}.
HELIX 299 312 {ECO:0000244|PDB:5KWA}.
STRAND 328 333 {ECO:0000244|PDB:5KWA}.
HELIX 334 338 {ECO:0000244|PDB:5KWA}.
HELIX 345 360 {ECO:0000244|PDB:5KWA}.
TURN 361 363 {ECO:0000244|PDB:5KWA}.
STRAND 366 371 {ECO:0000244|PDB:5KWA}.
HELIX 393 403 {ECO:0000244|PDB:5KWA}.
STRAND 409 416 {ECO:0000244|PDB:5KWA}.
HELIX 418 420 {ECO:0000244|PDB:5KWA}.
HELIX 423 426 {ECO:0000244|PDB:5KWA}.
STRAND 433 436 {ECO:0000244|PDB:5KWA}.
HELIX 442 449 {ECO:0000244|PDB:5KWA}.
TURN 450 452 {ECO:0000244|PDB:5KWA}.
HELIX 461 465 {ECO:0000244|PDB:5KWA}.
TURN 466 469 {ECO:0000244|PDB:5KWA}.
HELIX 471 486 {ECO:0000244|PDB:5KWA}.
HELIX 491 493 {ECO:0000244|PDB:5KWA}.
STRAND 494 500 {ECO:0000244|PDB:5KWA}.
STRAND 505 509 {ECO:0000244|PDB:5KWA}.
HELIX 510 513 {ECO:0000244|PDB:5KWA}.
HELIX 516 537 {ECO:0000244|PDB:5KWA}.
HELIX 544 559 {ECO:0000244|PDB:5KWA}.
HELIX 567 577 {ECO:0000244|PDB:5KWA}.
STRAND 581 586 {ECO:0000244|PDB:5KWA}.
STRAND 597 599 {ECO:0000244|PDB:5KWA}.
SEQUENCE 609 AA; 67401 MW; 4D5F4E630614C58D CRC64;
MGESERSEAF GIPRDSPLSS GDAAELEQLR REAAVLREQL ENAVGSHAPT RSARDIHQLE
ARIDSLAARN SKLMETLKEA RQQLLALREE VDRLGQPPSG YGVLLATHDD DTVDVFTSGR
KMRLTCSPNI DAASLKKGQT VRLNEALTVV EAGTFEAVGE ISTLREILAD GHRALVVGHA
DEERVVWLAD PLIAEDLPDG LPEALNDDTR PRKLRPGDSL LVDTKAGYAF ERIPKAEVED
LVLEEVPDVS YADIGGLSRQ IEQIRDAVEL PFLHKELYRE YSLRPPKGVL LYGPPGCGKT
LIAKAVANSL AKKMAEVRGD DAHEAKSYFL NIKGPELLNK FVGETERHIR LIFQRAREKA
SEGTPVIVFF DEMDSIFRTR GTGVSSDVET TVVPQLLSEI DGVEGLENVI VIGASNREDM
IDPAILRPGR LDVKIKIERP DAEAAQDIYS KYLTEFLPVH ADDLAEFDGD RSACIKAMIE
KVVDRMYAEI DDNRFLEVTY ANGDKEVMYF KDFNSGAMIQ NVVDRAKKNA IKSVLETGQP
GLRIQHLLDS IVDEFAENED LPNTTNPDDW ARISGKKGER IVYIRTLVTG KSSSASRAID
TESNLGQYL


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EIAAB32668 26S protease regulatory subunit 8,26S proteasome AAA-ATPase subunit RPT6,Bos taurus,Bovine,p45_SUG,Proteasome 26S subunit ATPase 5,Proteasome subunit p45,PSMC5,SUG1
EIAAB32594 26S protease regulatory subunit 10B,26S proteasome AAA-ATPase subunit RPT4,Mouse,Mus musculus,Proteasome 26S subunit ATPase 6,Proteasome subunit p42,Psmc6,Sug2
EIAAB32656 26S protease regulatory subunit 6A,26S proteasome AAA-ATPase subunit RPT5,Proteasome 26S subunit ATPase 3,Psmc3,Rat,Rattus norvegicus,Spermatogenic cell_sperm-associated Tat-binding protein homolog SA
EIAAB32655 26S protease regulatory subunit 6A,26S proteasome AAA-ATPase subunit RPT5,Mouse,Mus musculus,Proteasome 26S subunit ATPase 3,Psmc3,Tat-binding protein 1,Tbp1,TBP-1
EIAAB32621 26S protease regulatory subunit 4,26S proteasome AAA-ATPase subunit RPT2,Homo sapiens,Human,P26s4,Proteasome 26S subunit ATPase 1,PSMC1
EIAAB32619 26S protease regulatory subunit 4,26S proteasome AAA-ATPase subunit RPT2,Mouse,Mus musculus,P26s4,Proteasome 26S subunit ATPase 1,Psmc1
EIAAB32620 26S protease regulatory subunit 4,26S proteasome AAA-ATPase subunit RPT2,P26s4,Proteasome 26S subunit ATPase 1,Psmc1,Rat,Rattus norvegicus
EIAAB32663 26S protease regulatory subunit 7,26S proteasome AAA-ATPase subunit RPT1,Bos taurus,Bovine,Proteasome 26S subunit ATPase 2,PSMC2
EIAAB32658 26S protease regulatory subunit 6B,26S proteasome AAA-ATPase subunit RPT3,Bos taurus,Bovine,Proteasome 26S subunit ATPase 4,PSMC4
EIAAB32592 26S protease regulatory subunit 10B,26S proteasome AAA-ATPase subunit RPT4,Bos taurus,Bovine,Proteasome 26S subunit ATPase 6,PSMC6
EIAAB32657 26S protease regulatory subunit 6B,26S proteasome AAA-ATPase subunit RPT3,CIP21,MB67-interacting protein,MIP224,Mouse,Mus musculus,Proteasome 26S subunit ATPase 4,Psmc4,Tat-binding protein 7,Tbp7,TBP-
EIAAB32661 26S protease regulatory subunit 7,26S proteasome AAA-ATPase subunit RPT1,Homo sapiens,Human,MSS1,Proteasome 26S subunit ATPase 2,Protein MSS1,PSMC2
EIAAB32662 26S protease regulatory subunit 7,26S proteasome AAA-ATPase subunit RPT1,Mouse,Mss1,Mus musculus,Proteasome 26S subunit ATPase 2,Protein MSS1,Psmc2
EIAAB32664 26S protease regulatory subunit 7,26S proteasome AAA-ATPase subunit RPT1,Mss1,Proteasome 26S subunit ATPase 2,Protein MSS1,Psmc2,Rat,Rattus norvegicus
EIAAB32622 26S protease regulatory subunit 4,26S proteasome AAA-ATPase subunit RPT2,Chicken,Gallus gallus,P26s4,Proteasome 26S subunit ATPase 1,PSMC1
EIAAB32659 26S protease regulatory subunit 6B,26S proteasome AAA-ATPase subunit RPT3,Homo sapiens,Human,MB67-interacting protein,MIP224,MIP224,Proteasome 26S subunit ATPase 4,PSMC4,Tat-binding protein 7,TBP7,TBP
orb41644 V ATPase C2 antibody Polyclonal Rabbit polyclonal to V ATPase C2. This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracell 100
orb41647 V ATPase H antibody Polyclonal Rabbit polyclonal to V ATPase H. This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellul 100


 

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