LRRK1_MOUSE
ID LRRK1_MOUSE Reviewed; 2014 AA.
AC Q3UHC2; Q3U476; Q66JQ4; Q6GQR9; Q6NZF5; Q6ZPI4; Q8BKP3; Q8BU93; Q8BUY0;
AC Q8BVV2; Q8R085;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Leucine-rich repeat serine/threonine-protein kinase 1;
DE EC=2.7.11.1;
GN Name=Lrrk1 {ECO:0000312|MGI:MGI:2142227}; Synonyms=Kiaa1790;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAE27935.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE27935.1}, and
RC NOD {ECO:0000312|EMBL:BAE32558.1};
RC TISSUE=Dendritic cell {ECO:0000312|EMBL:BAE32558.1},
RC Fetal head {ECO:0000312|EMBL:BAC38349.1},
RC Head {ECO:0000312|EMBL:BAC36341.1}, Lung {ECO:0000312|EMBL:BAC39743.1}, and
RC Spinal ganglion {ECO:0000312|EMBL:BAC34581.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH27199.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1632-2014 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH66159.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH27199.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH72664.1},
RC Colon {ECO:0000312|EMBL:AAH27199.1}, Jaw {ECO:0000312|EMBL:AAH80819.1}, and
RC Kidney {ECO:0000312|EMBL:AAH66159.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC98251.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 117-2014 (ISOFORM 1).
RC TISSUE=Embryonic tail {ECO:0000312|EMBL:BAC98251.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q38SD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q38SD2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q38SD2};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q38SD2};
CC -!- ACTIVITY REGULATION: Binding of GTP stimulates kinase activity.
CC {ECO:0000250|UniProtKB:Q38SD2}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q38SD2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:14621295, ECO:0000269|PubMed:16141072};
CC IsoId=Q3UHC2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q3UHC2-2; Sequence=VSP_052014;
CC Name=3 {ECO:0000269|PubMed:15489334};
CC IsoId=Q3UHC2-3; Sequence=VSP_052013, VSP_052015, VSP_052016;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. ROCO subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27199.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC36341.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC39743.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK051264; BAC34581.1; -; mRNA.
DR EMBL; AK076432; BAC36341.1; ALT_INIT; mRNA.
DR EMBL; AK081849; BAC38349.1; -; mRNA.
DR EMBL; AK086795; BAC39743.1; ALT_INIT; mRNA.
DR EMBL; AK147469; BAE27935.1; -; mRNA.
DR EMBL; AK154395; BAE32558.1; -; mRNA.
DR EMBL; BC027199; AAH27199.1; ALT_INIT; mRNA.
DR EMBL; BC066159; AAH66159.1; -; mRNA.
DR EMBL; BC072664; AAH72664.1; -; mRNA.
DR EMBL; BC080819; AAH80819.1; -; mRNA.
DR EMBL; AK129441; BAC98251.1; -; mRNA.
DR CCDS; CCDS21344.1; -. [Q3UHC2-1]
DR RefSeq; NP_666303.3; NM_146191.3. [Q3UHC2-1]
DR AlphaFoldDB; Q3UHC2; -.
DR SMR; Q3UHC2; -.
DR BioGRID; 231403; 6.
DR IntAct; Q3UHC2; 2.
DR STRING; 10090.ENSMUSP00000015277; -.
DR iPTMnet; Q3UHC2; -.
DR PhosphoSitePlus; Q3UHC2; -.
DR EPD; Q3UHC2; -.
DR MaxQB; Q3UHC2; -.
DR PaxDb; Q3UHC2; -.
DR PeptideAtlas; Q3UHC2; -.
DR PRIDE; Q3UHC2; -.
DR ProteomicsDB; 252527; -. [Q3UHC2-1]
DR ProteomicsDB; 252528; -. [Q3UHC2-2]
DR ProteomicsDB; 252529; -. [Q3UHC2-3]
DR ABCD; Q3UHC2; 2 sequenced antibodies.
DR Antibodypedia; 2085; 202 antibodies from 29 providers.
DR DNASU; 233328; -.
DR Ensembl; ENSMUST00000015277; ENSMUSP00000015277; ENSMUSG00000015133. [Q3UHC2-1]
DR GeneID; 233328; -.
DR KEGG; mmu:233328; -.
DR UCSC; uc009hhc.1; mouse. [Q3UHC2-2]
DR UCSC; uc009hhd.1; mouse. [Q3UHC2-1]
DR CTD; 79705; -.
DR MGI; MGI:2142227; Lrrk1.
DR VEuPathDB; HostDB:ENSMUSG00000015133; -.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160363; -.
DR HOGENOM; CLU_001731_0_0_1; -.
DR InParanoid; Q3UHC2; -.
DR OMA; CHICAAA; -.
DR OrthoDB; 14978at2759; -.
DR PhylomeDB; Q3UHC2; -.
DR TreeFam; TF313679; -.
DR BioGRID-ORCS; 233328; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Lrrk1; mouse.
DR PRO; PR:Q3UHC2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3UHC2; protein.
DR Bgee; ENSMUSG00000015133; Expressed in right lung lobe and 194 other tissues.
DR ExpressionAtlas; Q3UHC2; baseline and differential.
DR Genevisible; Q3UHC2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0045453; P:bone resorption; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IGI:MGI.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0036035; P:osteoclast development; IMP:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IGI:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR032171; COR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR020859; ROC_dom.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS51450; LRR; 11.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS51424; ROC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; ATP-binding; Cytoplasm; GTP-binding;
KW Kinase; Leucine-rich repeat; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2014
FT /note="Leucine-rich repeat serine/threonine-protein kinase
FT 1"
FT /id="PRO_0000233378"
FT REPEAT 86..116
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 119..148
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 152..182
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 193..222
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 279..300
FT /note="LRR 1"
FT REPEAT 303..324
FT /note="LRR 2"
FT REPEAT 330..351
FT /note="LRR 3"
FT REPEAT 353..374
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 381..402
FT /note="LRR 5"
FT REPEAT 405..426
FT /note="LRR 6"
FT REPEAT 427..447
FT /note="LRR 7"
FT REPEAT 451..472
FT /note="LRR 8"
FT REPEAT 474..495
FT /note="LRR 9"
FT REPEAT 498..519
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 549..570
FT /note="LRR 11"
FT REPEAT 572..594
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 596..617
FT /note="LRR 13"
FT DOMAIN 632..826
FT /note="Roc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT DOMAIN 1242..1525
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1839..1895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1839..1880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1881..1895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1386
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q5S007,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1248..1256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5S007,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q38SD2,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..1610
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052014"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052013"
FT VAR_SEQ 1153..1979
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052015"
FT VAR_SEQ 1999..2014
FT /note="SYEELGRLEACTRKRR -> LPHQLFQCAFLCQL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052016"
FT CONFLICT 66
FT /note="N -> D (in Ref. 1; BAC34581)"
FT /evidence="ECO:0000305"
FT CONFLICT 950
FT /note="Q -> R (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1539
FT /note="A -> T (in Ref. 1; BAE32558 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1751
FT /note="V -> L (in Ref. 2; AAH27199)"
FT /evidence="ECO:0000305"
FT CONFLICT 1806
FT /note="G -> E (in Ref. 1; BAE32558, 2; AAH80819 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1903
FT /note="S -> N (in Ref. 1; BAE32558, 2; AAH80819 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1931
FT /note="G -> S (in Ref. 1; BAE32558, 2; AAH80819 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1972
FT /note="S -> G (in Ref. 1; BAE32558, 2; AAH27199/AAH80819
FT and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2014 AA; 225470 MW; EE33100F581779D0 CRC64;
MAGTSQRPPS MYWCVGTEGL AVCPGPAMET HNGAEDMGSK LSLPGGSSTV QCPSMEEIHT
AYKQRNLSRA RDLLRGVCEE SESSQEKGQL LSIAAAHGDL ETVQFLLTEK RVELPTEPTD
DNPAVVAAHF GHAEVVRELL ESLPGPCTPQ RLLNWMLALA CQRGHLEVVK LLVLTHGADP
ENYAVRKNEF PVIVRLPLYA AIKAGNEDIA IFLLRHGAYF CSYILLDSPE PSKHLLRKYF
IEASALPSSY PGKIALRVKW SHLKLPWVDL DWLLDISCQI TELDLSANCL PSLPSIIPWG
LINLKKLNLS NNQLGELPCV QSSDEIICSR LLEIDISSNK LSHLPPGFLH LSKLQKLTAS
KNYLERLFEE ENATNWIGLR KLQELDLADN RLTELPVQFM HSFKSLTSLN VSRNNLKSFP
DPWSCPLKCC KASKNALESL PDKMAVFWKS HLRDADFSEN SLKEVPLGLF QLDALMFLRL
QGNQLLSLPP QEKWTCTQLK TLDLSRNQLG KNEDGLKTKR ISLFTTRGRQ RSGTETASML
EFPAFLSESL EVLCLNDNHL DAVPPSVCLL KNLSELYLGN NPGLRELPPE LGQLGNLWQL
DIEDLNISNV PAEVRKEGPK ATLSFLRAQL RKAEKCKLMK MILVGPPRQG KSTLLEILQT
GKAPQLAHSE ATIRTTKWEL QRPAGSKAKV ESVEFNVWDI GGPASMATVN QCFFTDKALY
VVVWNLALGE EAVANLQFWL LNIEAKAPNA VVLVVGTHLD LIEAKFRVER IATLRAYVLA
LCRSPSGSRA TGFPDITFKH LHEISCKNLE GQEGLRQLIF HVTCNMKDVG STIGCQKLAG
RLIPRSYISL QEAVLAEQQR RSLGDQVQYL TDRQLDQLVE QTPGNDIKDY EDLQSAISFL
IETGTLLHFP DTSHGLRNLY FLDPIWLSEC LQRIFNIKGS RSVAKNGVIQ AEDLRMLLVG
TGFTQQTEEQ YFQFLAKFEI ALPVANDSYL LPHLLPSKPG LDTHSMRHPM ANTIQRVFKM
SFVPVGFWQR FIARMLISLA EMDLQLFENK KNTKSRNRKV TIYSFTGSQR NRCSTFRVRR
NQTIYWQEGL LVTFDGGYLS VESSDVNWKK KKSGGIKIIC QSEMRDFSAM AFITDHVNSL
IDQWFPALTA TESDGTPLME QYVPCPVCEA SWAQHADPNE RSESVQYFDM EDCVLTAIER
DFISCPRHPD LPVPLQELVP ELFMTDFPAR LFLENSKLEH TEGENSILGQ GGSGTVIYQA
RYQGQPVAVK RFHIKKFKNS ANAPADTMLR HLRAMDAMKN FSDFRQEASM LHALQHPCIV
SLIGISIHPL CFALELAPLG SLNTVLSENA KDSSFMPLGH MLTQKIAYQI ASGLAYLHKK
NIIFCDLKSD NILVWSLSAK EHINIKLSDY GISRQSFHEG ALGVEGTPGY QAPEIRPRIV
YDEKVDMFSY GMVLYELLSG QRPALGHHQL QIVKKLSKGI RPVLGQPEEV QFHRLQALMM
ECWDTKPEKR PLALSVVSQM KDPTFATFMY MLPCGKQSAF FSSQSQEYTV VFWDGKEESR
NYTVVNTEKG LLEVQRMTCP GMKLSCQLKV QSSVWIATED QKIYIYSLKG MCPLSVPQQA
LDTPAVVTCF LAVPVIKKNS FLVLAGLADG LVAVFPVARG TPKESCSYLC SHTANRSKFC
IPDEDARQNP YPVKAMEVVN SGSEVWYSNG PGLLVIDCTI LDISRRLEPY AAPSMVTSLV
CSSDCRGEEM VWCLDDKANC LVMYHSATYQ LCARYFCGDP NPLRDTFSVQ PSVLETPGSH
KTTSKGPVEE CIADVSIMYS EELGTQILTH QDSLTDYCSM SSYSSSPPHQ DPRSPSSLPS
SLTSYSSVPF SANYEDSDRL QEPSVTSDRT EHDLSPMDGE TFSQHLQAVK VLAVKDLIWV
PRHGGDIIVI GLEKDSGAQR GRVIAVLKAR ELNRHGVLVD AAVVAKDTVV CSFANENTEW
CLAVWRGWGA REFDIFYQSY EELGRLEACT RKRR
