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CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase (EC 6.3.5.5); Aspartate carbamoyltransferase (EC 2.1.3.2); Dihydroorotase (EC 3.5.2.3)]

 PYR1_MESAU              Reviewed;        2225 AA.
P08955; P70108;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 4.
22-NOV-2017, entry version 156.
RecName: Full=CAD protein;
Includes:
RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase;
EC=6.3.5.5 {ECO:0000269|PubMed:9218000};
Includes:
RecName: Full=Aspartate carbamoyltransferase;
EC=2.1.3.2 {ECO:0000269|PubMed:9218000};
Includes:
RecName: Full=Dihydroorotase;
EC=3.5.2.3 {ECO:0000269|PubMed:9218000};
Name=CAD;
Mesocricetus auratus (Golden hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Mesocricetus.
NCBI_TaxID=10036;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-169.
PubMed=1671675;
Bein K., Simmer J.P., Evans D.R.;
"Molecular cloning of a cDNA encoding the amino end of the mammalian
multifunctional protein CAD and analysis of the 5'-flanking region of
the CAD gene.";
J. Biol. Chem. 266:3791-3799(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-73.
PubMed=1982061;
Farnham P.J., Kollmar R.;
"Characterization of the 5' end of the growth-regulated Syrian hamster
CAD gene.";
Cell Growth Differ. 1:179-189(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 156-1455.
PubMed=1972379;
Simmer J.P., Kelly R.E., Rinker A.G. Jr., Scully J.L., Evans D.R.;
"Mammalian carbamyl phosphate synthetase (CPS). DNA sequence and
evolution of the CPS domain of the Syrian hamster multifunctional
protein CAD.";
J. Biol. Chem. 265:10395-10402(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 246-513.
PubMed=2900634; DOI=10.1016/0006-291X(88)90246-X;
Maley J.A., Davidson J.N.;
"Identification of the junction between the glutamine amidotransferase
and carbamyl phosphate synthetase domains of the mammalian CAD
protein.";
Biochem. Biophys. Res. Commun. 154:1047-1053(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1391-1870.
PubMed=1967494; DOI=10.1073/pnas.87.1.174;
Simmer J.P., Kelly R.E., Rinker A.G. Jr., Zimmermann B.H.,
Scully J.L., Kim H., Evans D.R.;
"Mammalian dihydroorotase: nucleotide sequence, peptide sequences, and
evolution of the dihydroorotase domain of the multifunctional protein
CAD.";
Proc. Natl. Acad. Sci. U.S.A. 87:174-178(1990).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1403-2110.
PubMed=1979549; DOI=10.1016/0378-1119(90)90399-C;
Williams N.K., Simpson R.J., Moritz R.L., Peide Y., Crofts L.,
Minasian E., Leach S.J., Wake R.G., Christopherson R.I.;
"Location of the dihydroorotase domain within trifunctional hamster
dihydroorotate synthetase.";
Gene 94:283-288(1990).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1774-2225.
PubMed=2543974; DOI=10.1073/pnas.86.12.4382;
Simmer J.P., Kelly R.E., Scully J.L., Grayson D.R., Rinker A.G. Jr.,
Bergh S.T., Evans D.R.;
"Mammalian aspartate transcarbamylase (ATCase): sequence of the ATCase
domain and interdomain linker in the CAD multifunctional polypeptide
and properties of the isolated domain.";
Proc. Natl. Acad. Sci. U.S.A. 86:4382-4386(1989).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 2074-2225.
PubMed=2862577; DOI=10.1128/MCB.5.7.1735;
Shigesada K., Stark G.R., Maley J.A., Niswander L.A., Davidson J.N.;
"Construction of a cDNA to the hamster CAD gene and its application
toward defining the domain for aspartate transcarbamylase.";
Mol. Cell. Biol. 5:1735-1742(1985).
[9]
SUBUNIT.
PubMed=2995985; DOI=10.1073/pnas.82.20.6802;
Lee L., Kelly R.E., Pastra-Landis S.C., Evans D.R.;
"Oligomeric structure of the multifunctional protein CAD that
initiates pyrimidine biosynthesis in mammalian cells.";
Proc. Natl. Acad. Sci. U.S.A. 82:6802-6806(1985).
[10]
DOMAINS, AND PARTIAL PROTEIN SEQUENCE.
PubMed=1348059;
Kim H., Kelly R.E., Evans D.R.;
"The structural organization of the hamster multifunctional protein
CAD. Controlled proteolysis, domains, and linkers.";
J. Biol. Chem. 267:7177-7184(1992).
[11]
FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-1406, AND
MUTAGENESIS OF SER-1406.
PubMed=9218000; DOI=10.1007/BF02679954;
Banerjei L.C., Davidson J.N.;
"Site-directed substitution of Ser1406 of hamster CAD with glutamic
acid alters allosteric regulation of carbamyl phosphate synthetase
II.";
Somat. Cell Mol. Genet. 23:37-49(1997).
[12]
3D-STRUCTURE MODELING OF ATCASE DOMAIN.
PubMed=2006137; DOI=10.1002/prot.340090305;
Scully J.L., Evans D.R.;
"Comparative modeling of mammalian aspartate transcarbamylase.";
Proteins 9:191-206(1991).
-!- FUNCTION: This protein is a "fusion" protein encoding four
enzymatic activities of the pyrimidine pathway (GATase, CPSase,
ATCase and DHOase). {ECO:0000269|PubMed:9218000}.
-!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
ADP + phosphate + L-glutamate + carbamoyl phosphate.
{ECO:0000269|PubMed:9218000}.
-!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate
+ N-carbamoyl-L-aspartate. {ECO:0000269|PubMed:9218000}.
-!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
aspartate. {ECO:0000269|PubMed:9218000}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P27708};
Note=Binds 3 Zn(2+) ions per subunit (for dihydroorotase
activity). {ECO:0000250|UniProtKB:P27708};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
Note=Binds 4 magnesium or manganese ions per subunit.
{ECO:0000255|PROSITE-ProRule:PRU00409};
-!- ENZYME REGULATION: Allosterically regulated and controlled by
phosphorylation. 5-phosphoribose 1-diphosphate (PRPP) is an
activator while UMP and UTP are inhibitors of the CPSase reaction.
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
-!- SUBUNIT: Homohexamer (PubMed:2995985). Interacts with CIPC (By
similarity). {ECO:0000250|UniProtKB:P27708,
ECO:0000269|PubMed:2995985}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
Note=Cytosolic and unphosphorylated in resting cells, translocates
to the nucleus in response to EGF stimulation, nuclear import
promotes optimal cell growth. {ECO:0000250}.
-!- PTM: Activated by MAP kinase (Erk1/2) phosphorylation just prior
to the S phase of the cell cycle, when the demand for pyrimidine
nucleotides is greatest, and down-regulated as the cells emerge
from S phase by protein kinase A (PKA) phosphorylation.
Phosphorylation at Ser-1859 by RPS6KB1 downstream of MTOR promotes
oligomerization and stimulates dihydroorotase activity (By
similarity). Phosphorylation at Ser-1406 reduces sensitivy to
feedback inhibition by UTP. {ECO:0000250,
ECO:0000269|PubMed:9218000}.
-!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
(carbamoyl phosphate synthase) form together the glutamine-
dependent CPSase (GD-CPSase) (EC 6.3.5.5).
-!- SIMILARITY: In the central section; belongs to the metallo-
dependent hydrolases superfamily. DHOase family. CAD subfamily.
{ECO:0000305}.
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EMBL; J05503; AAA37062.1; -; mRNA.
EMBL; M28866; AAA37073.1; -; mRNA.
EMBL; M60078; AAA63617.1; -; mRNA.
EMBL; M11242; AAA37061.1; -; mRNA.
EMBL; M23652; AAA37064.1; -; mRNA.
EMBL; M21927; AAA37063.1; -; mRNA.
PIR; A38653; A23443.
ProteinModelPortal; P08955; -.
SMR; P08955; -.
MEROPS; M38.972; -.
iPTMnet; P08955; -.
PRIDE; P08955; -.
HOVERGEN; HBG000279; -.
BRENDA; 3.5.2.3; 3239.
SABIO-RK; P08955; -.
UniPathway; UPA00070; UER00115.
UniPathway; UPA00070; UER00116.
UniPathway; UPA00070; UER00117.
Proteomes; UP000189706; Genome assembly.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0070335; F:aspartate binding; IDA:BHF-UCL.
GO; GO:0004070; F:aspartate carbamoyltransferase activity; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IDA:BHF-UCL.
GO; GO:0004151; F:dihydroorotase activity; IDA:BHF-UCL.
GO; GO:0004672; F:protein kinase activity; IDA:BHF-UCL.
GO; GO:0002134; F:UTP binding; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IDA:BHF-UCL.
GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006541; P:glutamine metabolic process; IDA:BHF-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:BHF-UCL.
CDD; cd01744; GATase1_CPSase; 1.
Gene3D; 1.10.1030.10; -; 1.
Gene3D; 2.30.40.10; -; 1.
Gene3D; 3.40.50.1370; -; 2.
Gene3D; 3.40.50.1380; -; 1.
Gene3D; 3.40.50.880; -; 1.
Gene3D; 3.50.30.20; -; 1.
HAMAP; MF_00001; Asp_carb_tr; 1.
HAMAP; MF_01209; CPSase_S_chain; 1.
InterPro; IPR006680; Amidohydro-rel.
InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
InterPro; IPR002082; Asp_carbamoyltransf.
InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR006275; CarbamoylP_synth_lsu.
InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
InterPro; IPR006274; CarbamoylP_synth_ssu.
InterPro; IPR002474; CarbamoylP_synth_ssu_N.
InterPro; IPR036480; CarbP_synth_ssu_N_sf.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR035686; CPSase_GATase1.
InterPro; IPR002195; Dihydroorotase_CS.
InterPro; IPR017926; GATASE.
InterPro; IPR011059; Metal-dep_hydrolase_composite.
InterPro; IPR032466; Metal_Hydrolase.
InterPro; IPR011607; MGS-like_dom.
InterPro; IPR036914; MGS-like_dom_sf.
InterPro; IPR016185; PreATP-grasp_dom_sf.
Pfam; PF01979; Amidohydro_1; 1.
Pfam; PF02786; CPSase_L_D2; 2.
Pfam; PF02787; CPSase_L_D3; 1.
Pfam; PF00988; CPSase_sm_chain; 1.
Pfam; PF00117; GATase; 1.
Pfam; PF02142; MGS; 1.
Pfam; PF00185; OTCace; 1.
Pfam; PF02729; OTCace_N; 1.
PRINTS; PR00100; AOTCASE.
PRINTS; PR00101; ATCASE.
PRINTS; PR00098; CPSASE.
SMART; SM01096; CPSase_L_D3; 1.
SMART; SM01097; CPSase_sm_chain; 1.
SMART; SM00851; MGS; 1.
SUPFAM; SSF48108; SSF48108; 1.
SUPFAM; SSF51338; SSF51338; 1.
SUPFAM; SSF51556; SSF51556; 1.
SUPFAM; SSF52021; SSF52021; 1.
SUPFAM; SSF52317; SSF52317; 1.
SUPFAM; SSF52335; SSF52335; 1.
SUPFAM; SSF52440; SSF52440; 2.
SUPFAM; SSF53671; SSF53671; 1.
TIGRFAMs; TIGR00670; asp_carb_tr; 1.
TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
PROSITE; PS50975; ATP_GRASP; 2.
PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PROSITE; PS00866; CPSASE_1; 2.
PROSITE; PS00867; CPSASE_2; 2.
PROSITE; PS00482; DIHYDROOROTASE_1; 1.
PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PROSITE; PS51273; GATASE_TYPE_1; 1.
1: Evidence at protein level;
Acetylation; Allosteric enzyme; ATP-binding; Complete proteome;
Cytoplasm; Direct protein sequencing; Glutamine amidotransferase;
Hydrolase; Ligase; Magnesium; Manganese; Metal-binding;
Multifunctional enzyme; Nucleotide-binding; Nucleus; Phosphoprotein;
Pyrimidine biosynthesis; Reference proteome; Repeat; Transferase;
Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P27708}.
CHAIN 2 2225 CAD protein.
/FTId=PRO_0000199507.
DOMAIN 177 363 Glutamine amidotransferase type-1.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
DOMAIN 519 711 ATP-grasp 1. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 1052 1243 ATP-grasp 2. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
NP_BIND 545 600 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
NP_BIND 1078 1135 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 2 365 GATase (Glutamine amidotransferase).
{ECO:0000303|PubMed:1348059}.
REGION 366 394 Linker. {ECO:0000303|PubMed:1348059}.
REGION 395 1455 CPSase (Carbamoyl-phosphate synthase).
{ECO:0000303|PubMed:1348059}.
REGION 395 933 CPSase A. {ECO:0000303|PubMed:1348059}.
REGION 934 1455 CPSase B. {ECO:0000303|PubMed:1348059}.
REGION 1456 1788 DHOase (dihydroorotase).
{ECO:0000303|PubMed:1348059}.
REGION 1789 1917 Linker. {ECO:0000303|PubMed:1348059}.
REGION 1918 2225 ATCase (Aspartate transcarbamylase).
{ECO:0000303|PubMed:1348059}.
ACT_SITE 252 252 Nucleophile; for GATase activity.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
ACT_SITE 336 336 For GATase activity.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
ACT_SITE 338 338 For GATase activity.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
METAL 668 668 Magnesium or manganese 1.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 682 682 Magnesium or manganese 1.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 682 682 Magnesium or manganese 2.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 684 684 Magnesium or manganese 2.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 1202 1202 Magnesium or manganese 3.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 1214 1214 Magnesium or manganese 3.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 1214 1214 Magnesium or manganese 4.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 1216 1216 Magnesium or manganese 4.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 1471 1471 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P27708}.
METAL 1471 1471 Zinc 2; via pros nitrogen.
{ECO:0000250|UniProtKB:P27708}.
METAL 1473 1473 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P27708}.
METAL 1556 1556 Zinc 1; via carbamate group.
{ECO:0000250|UniProtKB:P27708}.
METAL 1556 1556 Zinc 3; via carbamate group.
{ECO:0000250|UniProtKB:P27708}.
METAL 1590 1590 Zinc 3; via pros nitrogen.
{ECO:0000250|UniProtKB:P27708}.
METAL 1613 1613 Zinc 2. {ECO:0000250|UniProtKB:P27708}.
METAL 1614 1614 Zinc 3; via tele nitrogen.
{ECO:0000250|UniProtKB:P27708}.
METAL 1637 1637 Zinc 2. {ECO:0000250|UniProtKB:P27708}.
METAL 1686 1686 Zinc 1. {ECO:0000250|UniProtKB:P27708}.
BINDING 1475 1475 N-carbamoyl-L-aspartate.
{ECO:0000250|UniProtKB:P27708}.
BINDING 1505 1505 N-carbamoyl-L-aspartate.
{ECO:0000250|UniProtKB:P27708}.
BINDING 1661 1661 N-carbamoyl-L-aspartate; via amide
nitrogen and carbonyl oxygen.
{ECO:0000250|UniProtKB:P27708}.
BINDING 1686 1686 N-carbamoyl-L-aspartate.
{ECO:0000250|UniProtKB:P27708}.
BINDING 1690 1690 N-carbamoyl-L-aspartate.
{ECO:0000250|UniProtKB:P27708}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P27708}.
MOD_RES 456 456 Phosphothreonine; by MAPK1.
{ECO:0000250|UniProtKB:P27708}.
MOD_RES 747 747 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27708}.
MOD_RES 1038 1038 Phosphoserine.
{ECO:0000250|UniProtKB:P27708}.
MOD_RES 1406 1406 Phosphoserine; by PKA.
{ECO:0000269|PubMed:9218000}.
MOD_RES 1411 1411 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27708}.
MOD_RES 1556 1556 N6-carboxylysine.
{ECO:0000250|UniProtKB:P27708}.
MOD_RES 1859 1859 Phosphoserine; by RPS6KB1 and PKA.
{ECO:0000250|UniProtKB:P27708}.
MOD_RES 1873 1873 Phosphoserine; by PKC; in vitro.
{ECO:0000250|UniProtKB:P27708}.
MOD_RES 1884 1884 Phosphothreonine.
{ECO:0000250|UniProtKB:P27708}.
MOD_RES 1900 1900 Phosphoserine.
{ECO:0000250|UniProtKB:P27708}.
MOD_RES 1938 1938 Phosphoserine.
{ECO:0000250|UniProtKB:P27708}.
MUTAGEN 1406 1406 S->A: No effect on enzyme kinetics.
{ECO:0000269|PubMed:9218000}.
MUTAGEN 1406 1406 S->D: Increases CPSase activity and
reduces sensitivy to feedback inhibition
by UTP. {ECO:0000269|PubMed:9218000}.
SEQUENCE 2225 AA; 243128 MW; 9F6EBA9BD4C6EC5A CRC64;
MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY
GIPSDEEDEF GLSKWFESSE NHVAGLVVGE CCPTPSHWSA TCTLHEWLQQ HGIPGLQGVD
TRELTKKLRE QGSLLGKLVQ SGTEPSTLPF VDPNARPLAP EVSIKTPRVF NAGGAPRICA
LDCGLKYNQI RCLCQLGAEV TVVPWNHELD SQKYDGLFLS NGPGDPASYP GVVATLNRVL
SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD
ADSLPAGWTP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF DVFLETVREA
VAGNPGGQTV KERLVQRLCP PGLLIPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI
KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITPHYV TQVIRNERPD GVLLTFGGQT
ALNCGVELTK AGVLARYGVR VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ
AQAAAERLGY PVLVRAAFAL GGLGSGFAST KEELSALVAP AFAHTSQVLI DKSLKGWKEI
EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRR TAIKVTQHLG
IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA LGIPLPELRN
SVTGGTAAFE PSLDYCVVKI PRWDLSKFLR VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL
RMVDENCVGF DHTVKPVSDV ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM
KRIVTHAQLL EQHRGQPLSQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RTPHVLVLGS GVYRIGSSVE FDWCAVGCIQ
QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM DIYELENPDG VILSMGGQLP
NNMAMALHRQ QCRVLGTSPE AIDSAENRFK FSRLLDTIGI SQPQWRELSD LESARQFCQT
VGYPCVVRPS YVLSGAAMNV AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV
ACDGVVSAIA ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPI GLMTGSGVVG
VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL KAMLSTGFKI PKKNILLTIG
SYKNKSELLP TVRLLESLGY SLYASLGTAD FYTEHGVKVT AVDWHFEEAV DGECPPQRSI
LDQLAENHFE LVINLSMRGA GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL
GQIGPAPPLK VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGVTMV
CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGAVAG SAAGLKLYLN
ETFSELRLDS VAQWMEHFET WPSHLPIVAH AERQSVAAVL MVAQLTQRPV HICHVARKEE
ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL ERLGPGRGEV RPELGSREDM EALWENMAVI
DCFASDHAPH TLEEKCGPKP PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF
HLPLQEDTYV EVDLEHEWTI PSHMPFSKAR WTPFEGQKVK GTIRRVVLRG EVAYIDGQVL
VPPGYGQDVR KWPQGAVPQP PPSAPATTEI TTTPERPRRV IPGLPDGRFH LPPRIHRASD
PGLPAEEPKE KPSRKVVEPE LMGTPDGPCY PAPPVPRQAS PQNLGSSGLL HPQTSPLLHS
LVGQHILSVK QFTKDQMSHL FNVAHTLRMM VQKERSLDIL KGKVMASMFY EVSTRTSSSF
AAAMARLGGA VLSFSEATSS VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR
PVINAGDGVG EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
LRYVAPPSLR MPPSVWDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE RFGSTQEYEA
CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR AAYFRQAENG MYIRMALLAT
VLGRF


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