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Information on EC 3.4.11.9 - Xaa-Pro aminopeptidase and Organism(s) Homo sapiens and UniProt Accession Q9NQH7
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3.4.11.9 Xaa-Pro aminopeptidaseSpecify your search results
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
Synonyms
xpnpep2, xpnpep3, membrane-bound app, xpnpep1, appro, tgapp, tvmp50, x-prolyl-dipeptidyl aminopeptidase, aminopeptidase p1, x-prolyl aminopeptidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminoacylproline aminopeptidase
-
-
-
-
aminopeptidase P
aminopeptidase, aminoacylproline
-
-
-
-
AP-P
APP
mAmP
-
-
-
-
Membrane-bound AmP
-
-
-
-
Membrane-bound APP
-
-
-
-
proline aminopeptidase
-
-
-
-
X-Pro aminopeptidase
Xaa-Pro aminopeptidase
-
-
-
-
XPNPEP1
additional information
aminopeptidase P
-
-
-
-
AP-P
-
-
-
-
APP
-
-
-
-
X-Pro aminopeptidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37288-66-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
bradykinin + H2O
des-Arg-bradykinin + Arg
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
?
L-prolyl-peptide + H2O
L-proline + peptide
-
X-prolyl aminopeptidase catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides
-
-
?
Lys(epsilon-dinitrophenol)-Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl + H2O
Lys(epsilon-dinitrophenol) + Pro-Pro-NH-CH3-CH2-NH-2-aminobenzoyl
-
-
-
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
hydrolysis of the N-terminal Arg1-Pro bond
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
hydrolysis of the N-terminal Arg1-Pro2 bond
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
enzyme activity in plasma of humans with previous angio-oedema, a rare but potentially life-threatening side-effect of angiotensin-converting enzyme inhibitor treatment, is low compared to humans without this sensitivity and might be a predisposing factor for development of angio-oedema
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
the enzyme contributes to the degradation of bradykinin in human skin, especially in case of angiotensin-converting enzyme inhibition
-
?
additional information
?
-
no activity with Gly-Pro-hydroxyPro
-
?
additional information
?
-
aminopeptidase P targets Xaa-Proline peptides for cleavage. Roles of active site residues Tyr527 and Arg535, both residues make significant contributions to the catalytic efficiency, overview
-
-
?
additional information
?
-
-
aminopeptidase P targets Xaa-Proline peptides for cleavage. Roles of active site residues Tyr527 and Arg535, both residues make significant contributions to the catalytic efficiency, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
bradykinin + H2O
Arg + des-Arg-bradykinin
-
enzyme activity in plasma of humans with previous angio-oedema, a rare but potentially life-threatening side-effect of angiotensin-converting enzyme inhibitor treatment, is low compared to humans without this sensitivity and might be a predisposing factor for development of angio-oedema
-
?
bradykinin + H2O
Arg + des-Arg-bradykinin
-
the enzyme contributes to the degradation of bradykinin in human skin, especially in case of angiotensin-converting enzyme inhibition
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
in a metal:protein ratio of 0.11:1, slightly activates the enzyme at 0.01-0.1 mM, 2.8fold activation at 1 mM in presence of 1 mM glutathione
Mn2+
NaCl
activates the wild-type enzyme at 160 mM, inhibits the enzyme mutant R353A at 160 mM
additional information
Mn2+
in a metal:protein ratio of 1:1, activates the enzyme 2.80fold at 0.1 mM with substrate substance P, maximal at 0.3 mM, 4.6fold activation at 1 mM in presence of 1 mM glutathione
Mn2+
-
using the QM/MM method it is shown that XPNPEP1 employs two divalent manganese atoms (Mn(II)-Mn(II)) in the active site. The possibility of a single Mn(II) atom or other combination of divalent metal ions: Ca(II), Fe(II), Mg(II) is excluded
Mn2+
activates, required, Km values for Mn2+ are 0.0022 mM for the wild-type enzyme, 0.004 mM for mutant Y527F, and 0.0018 mM for mutant R535A. Kinetic analysis of MnCl2 activation of wild-type, Y527F and R535A hcAMPPs
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
activates the wild-type enzyme at 160 mM, inhibits the enzyme mutant R353A at 160 mM
additional information
no significant inhibition by amastatin and enalaprilat
-
additional information
-
no significant inhibition by amastatin and enalaprilat
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutathione
activates the enzyme in presence of Mn2+ or Co2+, and slightly in presence of Zn2+
guanidine hydrochloride
strongly reactivates enzyme mutant R353 at 0.1-10 mM, approximately 90% of the activity lost in theR535A hcAMPP mutant is regained in the presence of 30 mM guanidine hydrochloride. It has neither an observable rescue effect on wild-type hcAMPP nor on the Y527F mutant
progesterone
-
exposure of HepG2 cells to 0.001 mM progesterone results in a significant increase in the AP-P activity of cell lysates
additional information
-
women on the oral contraceptive pill have higher age-adjusted plasma AP-P compared to women not on the oral contraceptive pill or males
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.078
bradykinin
-
wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C
0.144
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 1.0 mM guanidine hydrochloride
0.163
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 10 mM guanidine hydrochloride
0.327
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 0.1 mM guanidine hydrochloride
0.308
L-Arg-L-Pro-L-Pro
-
wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C
additional information
additional information
Michaelis-Menten steady-state kinetics. Kinetic parameters for R535A hcAMPP measured in the presence and absence of guanidine hydrochloride, overview
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics. Kinetic parameters for R535A hcAMPP measured in the presence and absence of guanidine hydrochloride, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.7
L-Arg-L-Pro-L-Pro
-
wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C
2
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 0.1 mM guanidine hydrochloride
3.2
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 1.0 mM guanidine hydrochloride
3.8
bradykinin
-
wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C
8.3
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 10 mM guanidine hydrochloride
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.12
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 0.1 mM guanidine hydrochloride
22.22
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 1.0 mM guanidine hydrochloride
50.92
bradykinin
pH 7.5, 37°C, recombinant mutant R535A, with 10 mM guanidine hydrochloride
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.016
-
humans with previous angiotensin-converting enzyme-inhibitor treatment-associated angio-oedema
0.022 - 0.023
-
humans without angiotensin-converting enzyme-inhibitor treatment-associated angio-oedema
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
upregulation of Xaa-Pro aminopeptidase-1, XPNPEP-1, in renal cell carcinoma from von Hippel-Lindau patients, and a strong decrease of XPNPEP-2, quantitative proteomic analysis, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
XPNPEP2 is glycophosphatidylinositol (GPI) anchored on the cytosolic side of the plasma membrane
additional information
additional information
isoforms of the human enzyme include the cytosolic (hcAMPP) and membrane-bound (hmAMPP) aminopeptidase P, encoded by XPNPEP1 and XPNPEP2 genes, and a third hypothetical isoform thought to be present in mitochondrial and cytosolic localizations
-
additional information
-
isoforms of the human enzyme include the cytosolic (hcAMPP) and membrane-bound (hmAMPP) aminopeptidase P, encoded by XPNPEP1 and XPNPEP2 genes, and a third hypothetical isoform thought to be present in mitochondrial and cytosolic localizations
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
in 2 families with an nephronophthisis-like phenotype, homozygous frameshift and splice-site mutations, respectively, are detected in the X-prolyl aminopeptidase 3 gene
physiological function
Xaa-Pro aminopeptidase-1 is an anti-proliferative and anti-migratory exoprotease. Differential expression of Xaa-Pro aminopeptidases 1 and 2 in renal cancer, overview
additional information
additional information
isozymes XPNPEP1 and -2 have comparable structural properties and similar substrate specificities
additional information
isozymes XPNPEP1 and -2 have comparable structural properties and similar substrate specificities
additional information
-
isozymes XPNPEP1 and -2 have comparable structural properties and similar substrate specificities
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). XPP3_HUMAN
507
0
57034
Swiss-Prot
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
interaction of the subunits can not be disrupted by 2-mercaptoethanol, 1 M NaCl, 1% Triton X-100, and 4 mM CHAPS
additional information
-
interaction of the subunits can not be disrupted by 2-mercaptoethanol, 1 M NaCl, 1% Triton X-100, and 4 mM CHAPS
additional information
the reported X-ray structure of hcAMPP depicts a homodimer with each subunit containing an N-terminal domain, a middle domain, and a C-terminal catalytic domain, two active site divalent metal ions. Dimerization is mediated by the N-terminal domain and Trp477, and conservation of the key active site residues including Asp415, Asp426, His489, Glu523, Glu537, His395, His485, and His498
additional information
-
the reported X-ray structure of hcAMPP depicts a homodimer with each subunit containing an N-terminal domain, a middle domain, and a C-terminal catalytic domain, two active site divalent metal ions. Dimerization is mediated by the N-terminal domain and Trp477, and conservation of the key active site residues including Asp415, Asp426, His489, Glu523, Glu537, His395, His485, and His498
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
secreted enzyme mutant with translational stop codon at position 658, N-glycosylated
side-chain modification
-
the enzyme is anchored to the membrane via a covalently attached glycosyl-phosphatidylinositol moiety
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, using 20% (v/v) polyethylene glycol 400, 0.15 M CaCl2, and 100 mM HEPES (pH 7.5)
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E41A
-
the mutant maintains 91% of the wild type activity and demonstrates that the acidic residue, which is considered as a stabilizing factor in the protonation of catalytic residue His498, plays only a marginal role in catalysis
R535A
site-directed mutagenesis, the mutant enzyme shows reduced kcat and Km compared to the wild-type enzyme. The respective levels of activity restoration are determined to be 86%, 31%, 16%, and 10% for guanidine hydrochloride, methylguanidine, aminoguanidine and N-ethyl-guanidine
W477E
-
the mutant, designed to block dimer formation, shows only 6% of the wild type activity
Y527F
site-directed mutagenesis, the mutant enzyme shows reduced kcat and Km compared to the wild-type enzyme
additional information
additional information
design of an aminopeptidase P (APaseP) targeting tissue-specific construct conjugated to a homing peptide for selective binding to human breast-derived cancer cells. Homing peptides are short amino acid sequences derived from phage display libraries that have the unique property of localizing to specific organs. The molecular construct allows for tissue-specific drug delivery, by binding to APaseP in the vascular endothelium. The breast homing peptide is a cyclic nine-amino-acid peptide with the sequence CPGPEGAGC, referred to as PEGA. The PEGA peptide and similar peptide conjugates distribute to human breast tissue xenograft specifically and evaluate the interaction with the membrane-bound proline-specific APaseP by binding studies. In vivo localization of the breast tissue specific conjugate in a breast cancer xenograft mouse model, established by implanting enzyme-expressing human breast adenocarcinoma cell line MCF-7 in nude mice with estrogen supplementation
additional information
-
design of an aminopeptidase P (APaseP) targeting tissue-specific construct conjugated to a homing peptide for selective binding to human breast-derived cancer cells. Homing peptides are short amino acid sequences derived from phage display libraries that have the unique property of localizing to specific organs. The molecular construct allows for tissue-specific drug delivery, by binding to APaseP in the vascular endothelium. The breast homing peptide is a cyclic nine-amino-acid peptide with the sequence CPGPEGAGC, referred to as PEGA. The PEGA peptide and similar peptide conjugates distribute to human breast tissue xenograft specifically and evaluate the interaction with the membrane-bound proline-specific APaseP by binding studies. In vivo localization of the breast tissue specific conjugate in a breast cancer xenograft mouse model, established by implanting enzyme-expressing human breast adenocarcinoma cell line MCF-7 in nude mice with estrogen supplementation
additional information
downregulation of XPNPEP1 in 786-O cells by stable transduction with small-hairpin (sh)RNAs
additional information
downregulation of XPNPEP1 in 786-O cells by stable transduction with small-hairpin (sh)RNAs
additional information
-
downregulation of XPNPEP1 in 786-O cells by stable transduction with small-hairpin (sh)RNAs
additional information
kinetic analysis of MnCl2 activation of wild-type, Y527F and R535A hcAMPPs
additional information
-
kinetic analysis of MnCl2 activation of wild-type, Y527F and R535A hcAMPPs
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
human cytosolic APP1 is unstable and forms a high molecular weight aggregate at acidic pH
709048
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
thermal stability of wild-type and mutant hcAMPPs, overview
additional information
-
thermal stability of wild-type and mutant hcAMPPs, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography and Hitrap Q HP affinity column chromatography
-
recombinant His-tagged wild-type and mutant cytosolic isozymes from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli BL21(DE3) as His-tagged enzyme, and in COS-1 cells
gene XPNPEP1, recombinant expression of wild-type and mutant cytosolic aminopeptidases P (hcAMPP, residues M1 to H623), with a thrombin-cleavable N-terminal His-tag in Escherichia coli strain Rosetta (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hooper, N.M.; Turner, A.J.
Ectoenzymes of the kidney microvillar membrane. Aminopeptidase P is anchored by a glycosyl-phosphatidylinositol moiety
FEBS Lett.
229
340-344
1988
Homo sapiens, Sus scrofa
Holtzman, E.J.; Pillay, G.; Rosenthal, T.; Yaron, A.
Aminopeptidase P activity in rat organs and human serum
Anal. Biochem.
162
476-481
1987
Homo sapiens, Rattus norvegicus
Fleminger, G.; Carmel, A.; Goldenberg, D.; Yaron, A.
Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and calf lung
Eur. J. Biochem.
125
609-615
1982
Bos taurus, Escherichia coli, Homo sapiens
Cottrell, G.S.; Hooper, N.M.; Turner, A.J.
Cloning, expression, and characterization of human cytosolic aminopeptidase P: a single manganese(II)-dependent enzyme
Biochemistry
39
15121-15128
2000
Homo sapiens (Q9NQW7), Homo sapiens
Kim, K.S.; Kumar, S.; Simmons, W.H.; Brown, N.J.
Inhibition of aminopeptidase P potentiates wheal response to bradykinin in angiotensin-converting enzyme inhibitor-treated humans
J. Pharmacol. Exp. Ther.
292
295-298
2000
Homo sapiens
Adam, A.; Cugno, M.; Molinaro, G.; Perez, M.; Lepage, Y.; Agostoni, A.
Aminopeptidase P in individuals with a history of angio-oedema on ACE inhibitors
Lancet
359
2088-2089
2002
Homo sapiens
Molinaro, G.; Carmona, A.K.; Juliano, M.A.; Juliano, L.; Malitskaya, E.; Yessine, M.A.; Chagnon, M.; Lepage, Y.; Simmons, W.H.; Boileau, G.; Adam, A.
Human recombinant membrane-bound aminopeptidase P: production of a soluble form and characterization using novel, internally quenched fluorescent substrates
Biochem. J.
385
389-397
2005
Homo sapiens
Duan, Q.L.; Binkley, K.; Rouleau, G.A.
Genetic analysis of Factor XII and bradykinin catabolic enzymes in a family with estrogen-dependent inherited angioedema
J. Allergy Clin. Immunol.
123
906-910
2009
Homo sapiens
Li, X.; Lou, Z.; Li, X.; Zhou, W.; Ma, M.; Cao, Y.; Geng, Y.; Bartlam, M.; Zhang, X.C.; Rao, Z.
Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit
J. Biol. Chem.
283
22858-22866
2008
Homo sapiens
La Corte, A.L.; Carter, A.M.; Turner, A.J.; Grant, P.J.; Hooper, N.M.
The bradykinin-degrading aminopeptidase P is increased in women taking the oral contraceptive pill
J. Renin Angiotensin Aldosterone Syst.
9
221-225
2008
Homo sapiens
Doria, C.; Elia, E.S.; Kang, Y.; Adam, A.; Desormeaux, A.; Ramirez, C.; Frank, A.; di Francesco, F.; Herman, J.H.
Acute hypotensive transfusion reaction during liver transplantation in a patient on angiotensin converting enzyme inhibitors from low aminopeptidase P activity
Liver Transpl.
14
684-687
2008
Homo sapiens
Ragheb, D.; Bompiani, K.; Dalal, S.; Klemba, M.
Evidence for catalytic roles for Plasmodium falciparum aminopeptidase P in the food vacuole and cytosol
J. Biol. Chem.
284
24806-24815
2009
Homo sapiens, Plasmodium falciparum
OToole, J.F.; Liu, Y.; Davis, E.E.; Westlake, C.J.; Attanasio, M.; Otto, E.A.; Seelow, D.; Nurnberg, G.; Becker, C.; Nuutinen, M.; Kaerppae, M.; Ignatius, J.; Uusimaa, J.; Pakanen, S.; Jaakkola, E.; van den Heuvel, L.P.; Fehrenbach, H.; Wiggins, R.; Goyal, M.; Zhou, W.; Wolf, M.T.; Wise, E.; Helou, J.; A, A.l.
Individuals with mutations in XPNPEP3, which encodes a mitochondrial protein, develop a nephronophthisis-like nephropathy
J. Clin. Invest.
120
791-802
2010
Danio rerio, Escherichia coli, Homo sapiens (Q9NQH7), Homo sapiens
Wu, S.; Liu, S.; Sim, S.; Pedersen, L.G.
Weakly antiferromagentic coupling via superexchange interaction between Mn(II)-Mn(II) atoms: A QM/MM study of the active site of human cytosolic X-propyl aminopeptidase P
J. Phys. Chem. Lett.
3
2293-2297
2012
Homo sapiens
Cordova, A.; Woodrick, J.; Grindrod, S.; Zhang, L.; Saygideger-Kont, Y.; Wang, K.; DeVito, S.; Daniele, S.G.; Paige, M.; Brown, M.L.
Aminopeptidase P mediated targeting for breast tissue specific conjugate delivery
Bioconjug. Chem.
27
1981-1990
2016
Homo sapiens (O43895), Homo sapiens
Drendel, V.; Heckelmann, B.; Chen, C.Y.; Weisser, J.; Espadas, G.; Schell, C.; Sabido, E.; Werner, M.; Jilg, C.A.; Schilling, O.
Proteome profiling of clear cell renal cell carcinoma in von Hippel-Lindau patients highlights upregulation of Xaa-Pro aminopeptidase-1, an anti-proliferative and anti-migratory exoprotease
Oncotarget
8
100066-100078
2017
Homo sapiens (O43895), Homo sapiens (Q9NQW7), Homo sapiens
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