true
1994-06-01
2024-01-24
207
IDUA_HUMAN
Human alpha-L-iduronidase: cDNA isolation and expression.
Scott H.S.
Anson D.S.
Orsborn A.M.
Nelson P.V.
Clements P.R.
Morris C.P.
Hopwood J.J.
doi:10.1073/pnas.88.21.9695
1991
Proc. Natl. Acad. Sci. U.S.A.
88
9695-9699
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
VARIANT GLN-33
Liver
Structure and sequence of the human alpha-L-iduronidase gene.
Scott H.S.
Guo X.H.
Hopwood J.J.
Morris C.P.
doi:10.1016/0888-7543(92)90053-u
1992
Genomics
13
1311-1313
NUCLEOTIDE SEQUENCE [GENOMIC DNA]
VARIANT GLN-33
Complete sequencing and characterization of 21,243 full-length human cDNAs.
Ota T.
Suzuki Y.
Nishikawa T.
Otsuki T.
Sugiyama T.
Irie R.
Wakamatsu A.
Hayashi K.
Sato H.
Nagai K.
Kimura K.
Makita H.
Sekine M.
Obayashi M.
Nishi T.
Shibahara T.
Tanaka T.
Ishii S.
Yamamoto J.
Saito K.
Kawai Y.
Isono Y.
Nakamura Y.
Nagahari K.
Murakami K.
Yasuda T.
Iwayanagi T.
Wagatsuma M.
Shiratori A.
Sudo H.
Hosoiri T.
Kaku Y.
Kodaira H.
Kondo H.
Sugawara M.
Takahashi M.
Kanda K.
Yokoi T.
Furuya T.
Kikkawa E.
Omura Y.
Abe K.
Kamihara K.
Katsuta N.
Sato K.
Tanikawa M.
Yamazaki M.
Ninomiya K.
Ishibashi T.
Yamashita H.
Murakawa K.
Fujimori K.
Tanai H.
Kimata M.
Watanabe M.
Hiraoka S.
Chiba Y.
Ishida S.
Ono Y.
Takiguchi S.
Watanabe S.
Yosida M.
Hotuta T.
Kusano J.
Kanehori K.
Takahashi-Fujii A.
Hara H.
Tanase T.-O.
Nomura Y.
Togiya S.
Komai F.
Hara R.
Takeuchi K.
Arita M.
Imose N.
Musashino K.
Yuuki H.
Oshima A.
Sasaki N.
Aotsuka S.
Yoshikawa Y.
Matsunawa H.
Ichihara T.
Shiohata N.
Sano S.
Moriya S.
Momiyama H.
Satoh N.
Takami S.
Terashima Y.
Suzuki O.
Nakagawa S.
Senoh A.
Mizoguchi H.
Goto Y.
Shimizu F.
Wakebe H.
Hishigaki H.
Watanabe T.
Sugiyama A.
Takemoto M.
Kawakami B.
Yamazaki M.'
Watanabe K.
Kumagai A.
Itakura S.
Fukuzumi Y.
Fujimori Y.
Komiyama M.
Tashiro H.
Tanigami A.
Fujiwara T.
Ono T.
Yamada K.
Fujii Y.
Ozaki K.
Hirao M.
Ohmori Y.
Kawabata A.
Hikiji T.
Kobatake N.
Inagaki H.
Ikema Y.
Okamoto S.
Okitani R.
Kawakami T.
Noguchi S.
Itoh T.
Shigeta K.
Senba T.
Matsumura K.
Nakajima Y.
Mizuno T.
Morinaga M.
Sasaki M.
Togashi T.
Oyama M.
Hata H.
Watanabe M.'
Komatsu T.
Mizushima-Sugano J.
Satoh T.
Shirai Y.
Takahashi Y.
Nakagawa K.
Okumura K.
Nagase T.
Nomura N.
Kikuchi H.
Masuho Y.
Yamashita R.
Nakai K.
Yada T.
Nakamura Y.'
Ohara O.
Isogai T.
Sugano S.
doi:10.1038/ng1285
2004
Nat. Genet.
36
40-45
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)
Generation and annotation of the DNA sequences of human chromosomes 2 and 4.
Hillier L.W.
Graves T.A.
Fulton R.S.
Fulton L.A.
Pepin K.H.
Minx P.
Wagner-McPherson C.
Layman D.
Wylie K.
Sekhon M.
Becker M.C.
Fewell G.A.
Delehaunty K.D.
Miner T.L.
Nash W.E.
Kremitzki C.
Oddy L.
Du H.
Sun H.
Bradshaw-Cordum H.
Ali J.
Carter J.
Cordes M.
Harris A.
Isak A.
van Brunt A.
Nguyen C.
Du F.
Courtney L.
Kalicki J.
Ozersky P.
Abbott S.
Armstrong J.
Belter E.A.
Caruso L.
Cedroni M.
Cotton M.
Davidson T.
Desai A.
Elliott G.
Erb T.
Fronick C.
Gaige T.
Haakenson W.
Haglund K.
Holmes A.
Harkins R.
Kim K.
Kruchowski S.S.
Strong C.M.
Grewal N.
Goyea E.
Hou S.
Levy A.
Martinka S.
Mead K.
McLellan M.D.
Meyer R.
Randall-Maher J.
Tomlinson C.
Dauphin-Kohlberg S.
Kozlowicz-Reilly A.
Shah N.
Swearengen-Shahid S.
Snider J.
Strong J.T.
Thompson J.
Yoakum M.
Leonard S.
Pearman C.
Trani L.
Radionenko M.
Waligorski J.E.
Wang C.
Rock S.M.
Tin-Wollam A.-M.
Maupin R.
Latreille P.
Wendl M.C.
Yang S.-P.
Pohl C.
Wallis J.W.
Spieth J.
Bieri T.A.
Berkowicz N.
Nelson J.O.
Osborne J.
Ding L.
Meyer R.'
Sabo A.
Shotland Y.
Sinha P.
Wohldmann P.E.
Cook L.L.
Hickenbotham M.T.
Eldred J.
Williams D.
Jones T.A.
She X.
Ciccarelli F.D.
Izaurralde E.
Taylor J.
Schmutz J.
Myers R.M.
Cox D.R.
Huang X.
McPherson J.D.
Mardis E.R.
Clifton S.W.
Warren W.C.
Chinwalla A.T.
Eddy S.R.
Marra M.A.
Ovcharenko I.
Furey T.S.
Miller W.
Eichler E.E.
Bork P.
Suyama M.
Torrents D.
Waterston R.H.
Wilson R.K.
doi:10.1038/nature03466
2005
Nature
434
724-731
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
Molecular genetics of mucopolysaccharidosis type I: diagnostic, clinical, and biological implications.
Scott H.S.
Bunge S.
Gal A.
Clarke L.A.
Morris C.P.
Hopwood J.J.
doi:10.1002/humu.1380060403
1995
Hum. Mutat.
6
288-302
REVIEW ON VARIANTS
Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.
Chen R.
Jiang X.
Sun D.
Han G.
Wang F.
Ye M.
Wang L.
Zou H.
doi:10.1021/pr8008012
2009
J. Proteome Res.
8
651-661
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110
Insights into mucopolysaccharidosis I from the structure and action of alpha-L-iduronidase.
Bie H.
Yin J.
He X.
Kermode A.R.
Goddard-Borger E.D.
Withers S.G.
James M.N.
doi:10.1038/nchembio.1357
2013
Nat. Chem. Biol.
9
739-745
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-653 IN COMPLEX WITH IDURONATE ANALOGS
CATALYTIC ACTIVITY
ACTIVE SITE
CHARACTERIZATION OF VARIANT MPS1H ARG-533
DISULFIDE BOND
GLYCOSYLATION AT ASN-110; ASN-372 AND ASN-415
Human alpha-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module.
Maita N.
Tsukimura T.
Taniguchi T.
Saito S.
Ohno K.
Taniguchi H.
Sakuraba H.
doi:10.1073/pnas.1306939110
2013
Proc. Natl. Acad. Sci. U.S.A.
110
14628-14633
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 27-653 IN COMPLEX WITH IDURONATE
CATALYTIC ACTIVITY
DISULFIDE BOND
SUBUNIT
GLYCOSYLATION AT ASN-110; ASN-190; ASN-372; ASN-415 AND ASN-451
IDENTIFICATION BY MASS SPECTROMETRY
Mutation analysis of 19 North American mucopolysaccharidosis type I patients: identification of two additional frequent mutations.
Clarke L.A.
Nelson P.V.
Warrington C.L.
Morris C.P.
Hopwood J.J.
Scott H.S.
doi:10.1002/humu.1380030316
1994
Hum. Mutat.
3
275-282
VARIANT MPS1H THR-75
Two novel mutations causing mucopolysaccharidosis type I detected by single strand conformational analysis of the alpha-L-iduronidase gene.
Clark L.A.
Scott H.S.
doi:10.1093/hmg/2.8.1311
1993
Hum. Mol. Genet.
2
1311-1312
VARIANT MPS1H/S PRO-82
Identification of mutations in the alpha-L-iduronidase gene (IDUA) that cause Hurler and Scheie syndromes.
Scott H.S.
Litjens T.
Nelson P.V.
Thompson P.R.
Brooks D.A.
Hopwood J.J.
Morris C.P.
1993
Am. J. Hum. Genet.
53
973-986
VARIANT MPS1S GLN-89
Molecular analysis of Hurler syndrome in Druze and Muslim Arab patients in Israel: multiple allelic mutations of the IDUA gene in a small geographic area.
Bach G.
Moskowitz S.M.
Tieu P.T.
Matynia A.
Neufeld E.F.
1993
Am. J. Hum. Genet.
53
330-338
VARIANTS MPS1H PRO-366 AND ARG-409
Alpha-L-iduronidase mutations (Q70X and P533R) associate with a severe Hurler phenotype.
Scott H.S.
Litjens T.
Nelson P.V.
Brooks D.A.
Hopwood J.J.
Morris C.P.
doi:10.1002/humu.1380010412
1992
Hum. Mutat.
1
333-339
VARIANT MPS1H ARG-533
Mucopolysaccharidosis type I: identification of 8 novel mutations and determination of the frequency of the two common alpha-L-iduronidase mutations (W402X and Q70X) among European patients.
Bunge S.
Kleijer W.J.
Steglich C.
Beck M.
Zuther C.
Morris C.P.
Schwinger E.
Hopwood J.J.
Scott H.S.
Gal A.
doi:10.1093/hmg/3.6.861
1994
Hum. Mol. Genet.
3
861-866
VARIANTS MPS1H ASP-51; THR-75; PRO-218; PRO-327; PRO-489 AND 16-SER--ALA-19 DEL
PCR detection of two RFLPs in exon I of the alpha-L-iduronidase (IDUA) gene.
Scott H.S.
Litjens T.
Hopwood J.J.
Morris C.P.
doi:10.1007/bf00220095
1992
Hum. Genet.
90
327
VARIANT GLN-33
Multiple polymorphisms within the alpha-L-iduronidase gene (IDUA): implications for a role in modification of MPS-I disease phenotype.
Scott H.S.
Nelson P.V.
Litjens T.
Hopwood J.J.
Morris C.P.
doi:10.1093/hmg/2.9.1471
1993
Hum. Mol. Genet.
2
1471-1473
VARIANT THR-361
Four novel mutations underlying mild or intermediate forms of alpha-L-iduronidase deficiency (MPS IS and MPS IH/S).
Tieu P.T.
Bach G.
Matynia A.
Hwang M.
Neufeld E.F.
doi:10.1002/humu.1380060111
1995
Hum. Mutat.
6
55-59
VARIANTS MPS1H/S PRO-490 AND LEU-496
VARIANT MPS1S PRO-492
Mucopolysaccharidosis type I: identification of 13 novel mutations of the alpha-L-iduronidase gene.
Bunge S.
Kleijer W.J.
Steglich C.
Beck M.
Schwinger E.
Gal A.
doi:10.1002/humu.1380060119
1995
Hum. Mutat.
6
91-94
VARIANTS MPS1S TRP-89 AND HIS-383
VARIANT MPS1H 349-ASP-ASN-350 DEL
VARIANTS MPS1H/S THR-504 AND ARG-626
Molecular genetic defect underlying alpha-L-iduronidase pseudodeficiency.
Aronovich E.L.
Pan D.
Whitley C.B.
1996
Am. J. Hum. Genet.
58
75-85
VARIANT IDUA PSEUDODEFICIENCY THR-300
A novel missense mutation in the human IDUA gene associated with a severe Hurler's phenotype.
Bartholomew D.W.
McClellan J.M.
1998
Hum. Mutat.
12
291
VARIANT MPS1H ARG-388
Mucopolysaccharidosis type I: characterization of novel mutations affecting alpha-L-iduronidase activity.
Lee-Chen G.J.
Lin S.P.
Tang Y.F.
Chin Y.W.
doi:10.1034/j.1399-0004.1999.560109.x
1999
Clin. Genet.
56
66-70
VARIANT MPS1H/S GLY-619
Identification and characterization of -3c-g acceptor splice site mutation in human alpha-L-iduronidase associated with mucopolysaccharidosis type IH/S.
Teng Y.N.
Wang T.R.
Hwu W.L.
Lin S.P.
Lee-Chen G.J.
doi:10.1034/j.1399-0004.2000.570207.x
2000
Clin. Genet.
57
131-136
VARIANT MPS1H/S ARG-346
Identification and characterization of 13 new mutations in mucopolysaccharidosis type I patients.
Matte U.
Yogalingam G.
Brooks D.
Leistner S.
Schwartz I.
Lima L.
Norato D.Y.
Brum J.M.
Beesley C.
Winchester B.
Giugliani R.
Hopwood J.J.
doi:10.1016/s1096-7192(02)00200-7
2003
Mol. Genet. Metab.
78
37-43
VARIANTS MPS1H ILE-133; LYS-182; ASP-208; TYR-349 AND ARG-533
VARIANTS MPS1H/S PHE-260; PRO-327; ARG-380 AND PRO-628
VARIANTS MPS1S GLN-89; ILE-350; HIS-383 AND ASP-445 DEL
Identification and molecular characterization of alpha-L-iduronidase mutations present in mucopolysaccharidosis type I patients undergoing enzyme replacement therapy.
Yogalingam G.
Guo X.H.
Muller V.J.
Brooks D.A.
Clements P.R.
Kakkis E.D.
Hopwood J.J.
doi:10.1002/humu.20081
2004
Hum. Mutat.
24
199-207
VARIANTS MPS1H/S VAL-79; GLN-238; PRO-327; CYS-363; ARG-380; ARG-533 AND ILE-602
VARIANT MPS1S ARG-423
VARIANTS GLN-82; GLN-105; THR-361 AND ILE-454
CHARACTERIZATION OF VARIANTS MPS1H/S VAL-79; GLN-238; CYS-363 AND ILE-602
CHARACTERIZATION OF VARIANT MPS1S ARG-423
CHARACTERIZATION OF VARIANT GLN-82
Mucopolysaccharidosis type I in 21 Czech and Slovak patients: mutation analysis suggests a functional importance of C-terminus of the IDUA protein.
Vazna A.
Beesley C.
Berna L.
Stolnaja L.
Myskova H.
Bouckova M.
Vlaskova H.
Poupetova H.
Zeman J.
Magner M.
Hlavata A.
Winchester B.
Hrebicek M.
Dvorakova L.
doi:10.1002/ajmg.a.32812
2009
Am. J. Med. Genet. A
149A
965-974
VARIANTS MPS1H TYR-315; PRO-327 AND PHE-620
CHARACTERIZATION OF VARIANTS MPS1H TYR-315 AND PHE-620
VARIANT MPS1S ARG-380
VARIANTS GLN-33; GLN-105; THR-361 AND ILE-454
IDUA mutational profiling of a cohort of 102 European patients with mucopolysaccharidosis type I: identification and characterization of 35 novel alpha-L-iduronidase (IDUA) alleles.
Bertola F.
Filocamo M.
Casati G.
Mort M.
Rosano C.
Tylki-Szymanska A.
Tuysuz B.
Gabrielli O.
Grossi S.
Scarpa M.
Parenti G.
Antuzzi D.
Dalmau J.
Di Rocco M.
Vici C.D.
Okur I.
Rosell J.
Rovelli A.
Furlan F.
Rigoldi M.
Biondi A.
Cooper D.N.
Parini R.
doi:10.1002/humu.21479
2011
Hum. Mutat.
32
E2189-E2210
VARIANTS MPS1H/S ARG-84; LYS-178; LEU-188; ARG-265; LYS-276; PRO-396; ARG-423; PRO-436; ARG-496; ARG-533 AND PHE-535
VARIANTS MPS1H ASP-51; PRO-103; PRO-327 AND ARG-385
VARIANTS MPS1S CYS-76; TRP-89; GLU-219; LYS-276; LEU-306; LYS-348; PRO-490 AND PRO-492
VARIANTS GLN-33; GLN-105; THR-361; ASN-449; ILE-454 AND THR-591
p.L18P: a novel IDUA mutation that causes a distinct attenuated phenotype in mucopolysaccharidosis type I patients.
Pasqualim G.
Ribeiro M.G.
da Fonseca G.G.
Szlago M.
Schenone A.
Lemes A.
Rojas M.V.
Matte U.
Giugliani R.
doi:10.1111/cge.12507
2015
Clin. Genet.
88
376-380
VARIANT MPS1S PRO-18
Genotype-phenotype relationships in mucopolysaccharidosis type I (MPS I): Insights from the International MPS I Registry.
Clarke L.A.
Giugliani R.
Guffon N.
Jones S.A.
Keenan H.A.
Munoz-Rojas M.V.
Okuyama T.
Viskochil D.
Whitley C.B.
Wijburg F.A.
Muenzer J.
doi:10.1111/cge.13583
2019
Clin. Genet.
96
281-289
VARIANT MPS1H ASN-349
REVIEW
2.30
A/B=27-653
2.76
A/B=27-653
2.99
A/B=27-653
2.70
A/B=27-653
2.36
A/B=27-653
2.10
A/B=1-653
2.17
A=1-653
2.46
A/B=27-653
2.26
A=27-653
2.02
A/B=27-653
2.39
A/B=27-653
90
2
Chondroitin sulfate
Glycoside Hydrolase Family 39
5 N-Linked glycans (2 sites)
6 sites, 5 glycans
6 sites, 5 N-linked glycans (2 sites)
250 antibodies from 26 providers
human
IDUA
Low tissue specificity
gene
phenotype
phenotype
phenotype
Hurler syndrome
Hurler-Scheie syndrome
Scheie syndrome
Eukaryota
2681
HS-GAG degradation
CS/DS degradation
MPS I - Hurler syndrome
12 hits in 1156 CRISPR screens
human
Tbio
Protein
Expressed in right hemisphere of cerebellum and 130 other cell types or tissues
baseline and differential
Glycosidases
Immunoglobulins
GH39_as
GH39_C
GH39_cat
Glyco_hydro_39
Glycoside_hydrolase_SF
Ig-like_fold
ALPHA-L-IDURONIDASE
ALPHA-L-IDURONIDASE
Glyco_hydro_39
Glyco_hydro_39_C
GLHYDRLASE39
(Trans)glycosidases
Glycosyl hydrolase domain
GLYCOSYL_HYDROL_F39
HS
Alpha-L-iduronidase
3.2.1.76
IDUA
Monomer.
Ubiquitous.
N-glycosylation at Asn-372 contributes to substrate binding and is required for full enzymatic activity.
The disease is caused by variants affecting the gene represented in this entry.
The disease is caused by variants affecting the gene represented in this entry.
The disease is caused by variants affecting the gene represented in this entry.
Belongs to the glycosyl hydrolase 39 family.
1
27
Alpha-L-iduronidase
69908
28
653
Proton donor
182
Nucleophile
299
54
56
58
91
181
264
305
306
349
363
488
492
N-linked (GlcNAc...) asparagine
110
N-linked (GlcNAc...) asparagine
190
N-linked (GlcNAc...) asparagine
336
N-linked (GlcNAc...) asparagine
372
N-linked (GlcNAc...) asparagine
415
N-linked (GlcNAc...) asparagine
451
541
577
In isoform 2.
W
53
100
In isoform 2.
VRPAPPSAPVFCALSRCAPGRADPGGAEAAPPAGCAQLHLHPGAGEGRRAADPAALPQVRGHPHLQRRGGPAGGLVPATAVEGGRDLRGHGGEGGPAQRPARPPATFLPRRDRRAVAAPPGPSCPGHPQ
265
324
In MPS1H.
16
19
In MPS1S.
P
18
Q
33
In MPS1H.
D
51
In MPS1H.
T
75
In MPS1S.
C
76
In MPS1H/S; reduction of activity and protein levels.
V
79
In MPS1H/S.
P
82
Reduction of protein levels.
Q
In MPS1H/S.
R
84
In MPS1S.
Q
89
In MPS1S.
W
In MPS1H; uncertain significance.
P
103
Q
105
R
116
In MPS1H.
I
133
In MPS1H/S.
K
178
In MPS1H.
K
In MPS1H/S; associated in cis with R-423.
L
188
In MPS1H.
D
208
In MPS1H.
P
218
In MPS1S.
E
219
In MPS1H/S.
Q
238
In MPS1H/S.
F
260
In MPS1H/S.
R
In MPS1H/S and MPS1S.
K
276
A
279
In IDUA pseudodeficiency.
T
300
In MPS1S.
L
In MPS1H; loss of function; undetectable enzyme activity.
Y
315
In MPS1H; MPS1H/S.
P
327
In MPS1H/S; 0.4% of normal activity.
R
346
In MPS1S.
K
348
In MPS1H.
350
In MPS1H.
N
In MPS1H.
Y
In MPS1S.
I
T
361
In MPS1H/S; loss of activity.
C
In MPS1H.
P
366
In MPS1H/S and MPS1S.
R
380
In MPS1S; 2-3% of normal activity.
H
383
In MPS1H.
R
385
In MPS1H.
R
388
In MPS1H.
LALL
396
In MPS1H/S.
P
In MPS1H.
R
409
In MPS1S and MPS1H/S; associated in cis with L-188 in a patient with MPS1H/S; significant reduction of activity and protein levels.
R
423
In MPS1H/S.
P
436
In MPS1S.
445
N
449
I
454
In MPS1H.
P
489
In MPS1H/S and MPS1S.
P
490
In MPS1S.
P
In MPS1H/S.
L
496
In MPS1H/S.
R
In MPS1H/S.
T
504
In MPS1H and MPS1H/S; in 3% of the MPS1H patients; reduces catalytic activity and protein stability.
R
533
In MPS1H/S.
F
535
T
591
In MPS1H/S; reduction of activity and protein levels.
I
602
In MPS1H/S; 1.5% of normal activity.
G
619
In MPS1H; loss of function; undetectable enzyme activity.
F
620
In MPS1H/S.
R
626
In MPS1H/S.
P
628
T
622
30
42
49
52
60
64
66
68
78
81
83
87
90
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2006-04-04
2
true
72670
7893ae3987ecc754a0cfcc486d423ce9
1
MRPLRPRAALLALLASLLAAPPVAPAEAPHLVHVDAARALWPLRRFWRSTGFCPPLPHSQADQYVLSWDQQLNLAYVGAVPHRGIKQVRTHWLLELVTTRGSTGRGLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISLHRKGARSSISILEQEKVVAQQIRQLFPKFADTPIYNDEADPLVGWSLPQPWRADVTYAAMVVKVIAQHQNLLLANTTSAFPYALLSNDNAFLSYHPHPFAQRTLTARFQVNNTRPPHVQLLRKPVLTAMGLLALLDEEQLWAEVSQAGTVLDSNHTVGVLASAHRPQGPADAWRAAVLIYASDDTRAHPNRSVAVTLRLRGVPPGPGLVYVTRYLDNGLCSPDGEWRRLGRPVFPTAEQFRRMRAAEDPVAAAPRPLPAGGRLTLRPALRLPSLLLVHVCARPEKPPGQVTRLRALPLTQGQLVLVWSDEHVGSKCLWTYEIQFSQDGKAYTPVSRKPSTFNLFVFSPDTGAVSGSYRVRALDYWARPGPFSDPVPYLEVPVPRGPPSPGNP
2
MRPLRPRAALLALLASLLAAPPVAPAEAPHLVHVDAARALWPLRRFWRSTGFWGSTGRGLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISLHRKVRPAPPSAPVFCALSRCAPGRADPGGAEAAPPAGCAQLHLHPGAGEGRRAADPAALPQVRGHPHLQRRGGPAGGLVPATAVEGGRDLRGHGGEGGPAQRPARPPATFLPRRDRRAVAAPPGPSCPGHPQVIAQHQNLLLANTTSAFPYALLSNDNAFLSYHPHPFAQRTLTARFQVNNTRPPHVQLLRKPVLTAMGLLALLDEEQLWAEVSQAGTVLDSNHTVGVLASAHRPQGPADAWRAAVLIYASDDTRAHPNRSVAVTLRLRGVPPGPGLVYVTRYLDNGLCSPDGEWRRLGRPVFPTAEQFRRMRAAEDPVAAAPRPLPAGGRLTLRPALRLPSLLLVHVCARPEKPPGQVTRLRALPLTQGQLVLVWSDEHVGSKCLWTYEIQFSQDGKAYTPVSRKPSTFNLFVFSPDTGAVSGSYRVRALDYWARPGPFSDPVPYLEVPVPRGPPSPGNP
true
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true