MYO9A_MOUSE
ID MYO9A_MOUSE Reviewed; 2542 AA.
AC Q8C170; Q3TRT5; Q4VBD3; Q80Y92; Q8C0U0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Unconventional myosin-IXa;
DE AltName: Full=Unconventional myosin-9a;
GN Name=Myo9a; Synonyms=Myr7;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1848-2542 (ISOFORM 1/2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Skin, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2144-2542 (ISOFORM 1/2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Liver;
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 [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10409426; DOI=10.1006/geno.1999.5867;
RA Gorman S.W., Haider N.B., Grieshammer U., Swiderski R.E., Kim E.,
RA Welch J.W., Searby C., Leng S., Carmi R., Sheffield V.C., Duhl D.M.;
RT "The cloning and developmental expression of unconventional myosin IXA
RT (MYO9A) a gene in the Bardet-Biedl syndrome (BBS4) region at chromosome
RT 15q22-q23.";
RL Genomics 59:150-160(1999).
RN [5]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19828736; DOI=10.1091/mbc.e09-04-0291;
RA Abouhamed M., Grobe K., San I.V., Thelen S., Honnert U., Balda M.S.,
RA Matter K., Baehler M.;
RT "Myosin IXa regulates epithelial differentiation and its deficiency results
RT in hydrocephalus.";
RL Mol. Biol. Cell 20:5074-5085(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1243; THR-1245; SER-1950 AND
RP SER-2293, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Spleen, and Testis;
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).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27259756; DOI=10.1093/brain/aww130;
RA O'Connor E., Toepf A., Mueller J.S., Cox D., Evangelista T., Colomer J.,
RA Abicht A., Senderek J., Hasselmann O., Yaramis A., Laval S.H.,
RA Lochmueller H.;
RT "Identification of mutations in the MYO9A gene in patients with congenital
RT myasthenic syndrome.";
RL Brain 139:2143-2153(2016).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Regulates Rho
CC by stimulating it's GTPase activity in neurons. Required for the
CC regulation of neurite branching and motor neuron axon guidance
CC (PubMed:27259756). {ECO:0000250|UniProtKB:Q9Z1N3,
CC ECO:0000269|PubMed:27259756}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z1N3}.
CC Synapse {ECO:0000269|PubMed:27259756}. Cell projection, growth cone
CC {ECO:0000269|PubMed:27259756}. Note=Localized in the cytoplasm of cell
CC bodies, dendrites and axons with occasional hints of an enrichment near
CC the plasma membrane. Localized at the neuromuscular junction
CC (PubMed:27259756). {ECO:0000250|UniProtKB:Q9Z1N3,
CC ECO:0000269|PubMed:27259756}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C170-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C170-2; Sequence=VSP_035161;
CC -!- TISSUE SPECIFICITY: Expressed in the eye, lung, liver, brain, heart,
CC kidney, skeletal muscle and spleen. No detection was found in liver. In
CC the brain, expressed in the ependymal cells of the third ventricle and
CC the aqueduct (PubMed:19828736). {ECO:0000269|PubMed:10409426,
CC ECO:0000269|PubMed:19828736}.
CC -!- DEVELOPMENTAL STAGE: Detected in whole embryos at 7, 11, 15 and 17 dpc.
CC Also present in limb buds from 13.5 dpc. At 16.5 dpc, it is expressed
CC throughout the developing nervous system, eye, inner ear, kidney,
CC thyroid gland and teeth. {ECO:0000269|PubMed:10409426}.
CC -!- PTM: Phosphorylated by ALPK1 following monosodium urate monohydrate
CC (MSU)-induced inflammation. {ECO:0000250|UniProtKB:B2RTY4}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice display retarded growth, a dome-
CC shaped skull, and develop severe hydrocephalus with stenosis and
CC closure of the ventral caudal third ventricle and the aqueduct.
CC {ECO:0000269|PubMed:19828736}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-9 (MYH9). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26164.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC156795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK028873; BAC26164.1; ALT_INIT; mRNA.
DR EMBL; AK029836; BAC26639.1; -; mRNA.
DR EMBL; AK162486; BAE36942.1; -; mRNA.
DR EMBL; BC046526; AAH46526.1; -; mRNA.
DR EMBL; BC096035; AAH96035.1; -; mRNA.
DR RefSeq; XP_006511283.1; XM_006511220.2. [Q8C170-1]
DR AlphaFoldDB; Q8C170; -.
DR SMR; Q8C170; -.
DR BioGRID; 234775; 5.
DR IntAct; Q8C170; 1.
DR STRING; 10090.ENSMUSP00000122852; -.
DR iPTMnet; Q8C170; -.
DR PhosphoSitePlus; Q8C170; -.
DR EPD; Q8C170; -.
DR jPOST; Q8C170; -.
DR MaxQB; Q8C170; -.
DR PRIDE; Q8C170; -.
DR ProteomicsDB; 287592; -. [Q8C170-1]
DR ProteomicsDB; 287593; -. [Q8C170-2]
DR Antibodypedia; 26536; 32 antibodies from 14 providers.
DR Ensembl; ENSMUST00000128341; ENSMUSP00000119401; ENSMUSG00000039585. [Q8C170-1]
DR Ensembl; ENSMUST00000135298; ENSMUSP00000117432; ENSMUSG00000039585. [Q8C170-2]
DR GeneID; 270163; -.
DR CTD; 4649; -.
DR MGI; MGI:107735; Myo9a.
DR VEuPathDB; HostDB:ENSMUSG00000039585; -.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000154905; -.
DR HOGENOM; CLU_000192_2_1_1; -.
DR InParanoid; Q8C170; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR BioGRID-ORCS; 270163; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Myo9a; mouse.
DR PRO; PR:Q8C170; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8C170; protein.
DR Bgee; ENSMUSG00000039585; Expressed in spermatocyte and 225 other tissues.
DR ExpressionAtlas; Q8C170; baseline and differential.
DR Genevisible; Q8C170; MM.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0150011; P:regulation of neuron projection arborization; IMP:UniProtKB.
DR CDD; cd00029; C1; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.850.10; -; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR028558; MYO9A.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036023; MYSc_Myo9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF3; PTHR46184:SF3; 2.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Cell projection;
KW Coiled coil; Cytoplasm; GTPase activation; Membrane; Metal-binding;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Transmembrane; Transmembrane helix;
KW Zinc; Zinc-finger.
FT CHAIN 1..2542
FT /note="Unconventional myosin-IXa"
FT /id="PRO_0000348441"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 14..112
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 146..1017
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1021..1041
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1043..1072
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1075..1104
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1116..1145
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1139..1168
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2065..2253
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 2001..2050
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 2068..2119
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 908..919
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1022..1163
FT /note="Neck or regulatory domain"
FT /evidence="ECO:0000250"
FT REGION 1164..2505
FT /note="Tail"
FT /evidence="ECO:0000250"
FT REGION 1221..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1650..1675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1693..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1767..1793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1806..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2361..2443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2465..2530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1265..1292
FT /evidence="ECO:0000255"
FT COILED 1492..1539
FT /evidence="ECO:0000255"
FT COILED 2324..2360
FT /evidence="ECO:0000255"
FT COMPBIAS 1357..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1820..1834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2370..2392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2419..2443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2490..2504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2505..2530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N3"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1245
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N3"
FT MOD_RES 1300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RTY4"
FT MOD_RES 1318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RTY4"
FT MOD_RES 1950
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RTY4"
FT MOD_RES 2458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RTY4"
FT VAR_SEQ 1717
FT /note="E -> EVARPAHKKKARMARTRSDFLTRGTFAEGEGDTEEDDYDDIIEPLLS
FT LDQASHSELGPVSSLGQASHSDSEM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035161"
FT CONFLICT 2434
FT /note="N -> Y (in Ref. 3; AAH96035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2542 AA; 292119 MW; 9371996D5B3D72E0 CRC64;
MNVSDGGRRR FEDNEHTLRI YPGTISEGTI YCPIPARKNS TAAEVIDSLI NRLHLDKTKC
YVLAEVKEFG GEEWILNPTD CPVQRMMLWP RMALENRLSG EDYRFLLREK NLDGSIHYGS
LQSWLRVTEE RRRMMERGFL PQPQQKDFDD LCSLPDLNEK TLLENLRNRF KHEKIYTYVG
SILIAINPFK FLPIYNPKYV KMYDNHQLGK LEPHIYAVAD VAYHAMLQRK KNQCIVISGE
SGSGKTQSTN FLIHHLTALS QKGFASGVEQ IILGAGPVLE AFGNAKTAHN NNSSRFGKFI
QVNYQETGTV LGAYVEKYLL EKSRLVYQEH NERNYHVFYY LLAGASEEER LAFHLKQPEE
YHFLNQITKK PLRQSWDDYC YDSEPDCFTV EGEDLRHDFE RLQLAMEMVG FLPKTRRQIF
SLLSAILHLG NISYKKKTYR DDSIDICNPE VLPIVSELLE VKEEMLFEAL VTRKTVTVGE
KLILPYKLAE AVTVRNSMAK SLYSALFDWI VFRINHALLN SKDLEQDTKT LSIGVLDIFG
FEDYENNSFE QFCINFANER LQHYFNQHIF KLEQEEYRTE GISWHNIDYI DNTCCINLIS
KKPTGLLHLL DEESNFPQAT NQTLLDKFKH QHEENSYIEF PAVMEPAFII KHYAGKVKYG
VKDFREKNTD HMRPDIVALL RSSRNAFVSG MTGIDPVAVF RWAVLRAFFR AVVAFREAGK
RHIQRKSGHD DTTPCAILKS MDSFSFLQHP VHQRSLEILQ RCKEEKYSIT RKNPRTPLSD
LQGMNTLNEK NQHDTFDIAW NVRTGIRQSR LPASNTSLLD KDGIFAHSAS SKLLERAHGI
LTRNKNFRSK PVLPKHLLEV NSLKHLTRLT LQDRITKSLL HLHKKKKPPS ISAQFQASLS
KLMETLGQAE PYFVKCIRSN AEKLPLRFSD ALVLRQLRYT GMLETVRIRQ SGYSSKYSFQ
DFVSHFHVLL PQHIIPSKFN IQDFFRKINI NSDNYQVGKT MVFLKEHERQ HLQDLLHQEV
LRRIVLLQRW FRVLLSRQQF LHLRQASIII QRFWRNYLNQ KQVRNAAVEK DAFIMASAAS
LLQASWRAHL ERQRYLELRA AAVIIQQRWR ELYRCRHKAA TCIQSRWRGY RQRKKYKEQR
NKIILLQSIY RGFRARQRCN ALKEEKLREA KLEHGLVHVK ACGPLEIQGS DPSEWEDRSF
DNRVKAIEEC KYVIESNRIS RESSMDFSKE SPDKQQERGR RQSGTDLQED VIVRQRPKSL
EDLHQKKVGR AKRESRRMRE LEQAIFSLEL LKVRSLGGMS PSEERRWSTE LMPEGLQSPH
GTPDSESSQG SLELLTCDEN QKSKPESLIL DEGELKISSP NTFTNPKSQD NALSASSETS
STLAGKGASS DSEHLKNGTA KEKLVCSSEP ITCKPQLRDS FVSSSLPTFF YIPHQEALKT
SSHLDTSIQR NKLPEREAIL KTTLTQDINR EARKCQFSGD QMTPLNTDSS CTVLKKLEKL
NIEKEKRQKQ LQQQNEKEMM EQIRQQTDIL EKERKAFKTI EQSRTEASVL APSFYQPRQK
VERPCSLYIQ NTPSKGEAGV LGSPSAVTKR DAALATKDSP SIHLPPKDRP VTLFFEKKGS
PCQSRTVKEL PKTERTGTQH DAAYKLSNNR STERDHFKST HFYSHRSDDP SREGSSRAIF
FTPKDNITPL VHSGNPQAHK QDESAWKPKL AGPGQQETSQ RFSSVDEQAK LHKAMSQGEI
TKLAVRQKAS DLDIRPQRAK MRFWAKGKQG EKKTTRVKPA SQSEISSFFP GPDVTPAHPF
SDELTQYHPT PPLSPELPGS CRKEFKENKE PSPKAKRKRG VKISSVALDS MHWQNDSVQI
IASASDLKSM DEFLLKKMND LDNEDSKKDT LVDVVFKKAL KEFRQNIFSS YSSALAMDDG
KSIRYKDLYA LFEQILEKTM RLEQRDWNES PVRVWVNTFK VFLDEYMNEF KTLDSTAPKV
LKTERKKRRK KETDLVEEHN GHIFKATQYS IPTYCEYCSS LIWIMDRASV CKLCKYACHK
KCCLKTTAKC SKKYDPELSS RQFGVELSRL TSEDRAVPLV VEKLINYIEM HGLYTEGIYR
KSGSTNKIKE LRQGLDTDAE SVNLDDYNIH VIASVFKQWL RDLPNPLMTF ELYEEFLRAM
GLQERKETIR GVYSVIDQLS RTHLNTLERL IFHLVRIALQ EDTNRMSANA LAIVFAPCIL
RCPDTTDPLQ SVQDISKTTT CVELIVVEQM NKYKARLKDI SSLEFAENKA KTRLSLIRRS
MGKGRIHRGN YPSPSSPVIV RLPSMSDVPE ETLSSETAME TDLTDQQQAA MQQEEKVLTE
QIENLQKEKE ELTFEMLVLE PRASDDETLE SEASIGTADS SENLNMDSEE RSLALSSLKA
AGKSEPSSKS RKQLRKQPDS LDSVSSSVSS CLSNTTSSHG TRKRFQIYSK SPFYRAASAC
EAQGTEGPLG QAKSLEDRPQ FISRGTFNPE KGKQKLKNVK NSPQKTKETP EGTVTSGRKK
TVDSDCSSTQ QLPLFGNNEF MV
