MYO16_MOUSE
ID MYO16_MOUSE Reviewed; 1919 AA.
AC Q5DU14; B2RX94; E1CB68; Q6GQW7; Q8BUV4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Unconventional myosin-XVI;
DE AltName: Full=Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3;
DE AltName: Full=Unconventional myosin-16;
GN Name=Myo16 {ECO:0000312|MGI:MGI:2685951};
GN Synonyms=Kiaa0865 {ECO:0000312|EMBL:BAD90419.1}, Nyap3;
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 [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH ACOT9;
RP ARHGAP26; CYFIP1; NCKAP1 AND PIK3R2, SUBUNIT, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, PHOSPHORYLATION, AND MUTAGENESIS
RP OF TYR-1416 AND TYR-1441.
RC TISSUE=Brain;
RX PubMed=21946561; DOI=10.1038/emboj.2011.348;
RA Yokoyama K., Tezuka T., Kotani M., Nakazawa T., Hoshina N., Shimoda Y.,
RA Kakuta S., Sudo K., Watanabe K., Iwakura Y., Yamamoto T.;
RT "NYAP: a phosphoprotein family that links PI3K to WAVE1 signalling in
RT neurons.";
RL EMBO J. 30:4739-4754(2011).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH72580.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH72580.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH72580.1}, and Testis;
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:BAC38475.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-992 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC38475.1};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAC38475.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAD90419.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 736-1919.
RC TISSUE=Fetal brain {ECO:0000312|EMBL:BAD90419.1};
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails are presumed to bind to membranous compartments, which
CC would be moved relative to actin filaments. May be involved in
CC targeting of the catalytic subunit of protein phosphatase 1 during
CC brain development (By similarity). Activates PI3K and concomitantly
CC recruits the WAVE1 complex to the close vicinity of PI3K and regulates
CC neuronal morphogenesis. {ECO:0000250, ECO:0000269|PubMed:21946561}.
CC -!- SUBUNIT: Binds PPP1CA and/or PPP1CC. Binds F-actin in an ATP-sensitive
CC manner (By similarity). Interacts with ACOT9, ARHGAP26 and PIK3R2.
CC Interacts with components of the WAVE1 complex, CYFIP1 and NCKAP1; this
CC interaction mediates PI3K-WAVE1 association and actin cytoskeleton
CC remodeling (PubMed:21946561). Interacts with KIRREL3 (By similarity).
CC {ECO:0000250|UniProtKB:Q9ERC1, ECO:0000250|UniProtKB:Q9Y6X6,
CC ECO:0000269|PubMed:21946561}.
CC -!- INTERACTION:
CC Q5DU14; P28660: Nckap1; NbExp=2; IntAct=EBI-7448308, EBI-771576;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ERC1}.
CC Note=Found in puncta in soma and processes of astrocytes and
CC dissociated cerebellar cells with the morphology of migrating granule
CC cells. {ECO:0000250|UniProtKB:Q9ERC1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:16141072, ECO:0000269|Ref.4};
CC IsoId=Q5DU14-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q5DU14-2; Sequence=VSP_052446;
CC Name=3;
CC IsoId=Q5DU14-3; Sequence=VSP_042365, VSP_042366;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain where it is
CC present in the neurons, but not in astrocytes or oligodendrites.
CC {ECO:0000269|PubMed:21946561}.
CC -!- DEVELOPMENTAL STAGE: At postnatal day 1, highly expressed in upper
CC neocortex and also detected in the olfactory bulb, but not in the
CC striatum. {ECO:0000269|PubMed:21946561}.
CC -!- PTM: Phosphorylated on tyrosine residues by FYN upon stimulation with
CC CNTN5. Phosphorylation begins at 14 dpc, reaches a peak during
CC perinatal days in brain, then gradually decreases.
CC {ECO:0000269|PubMed:21946561}.
CC -!- DISRUPTION PHENOTYPE: Triple knockout mice NYAP1/NYAP2/MYO16 are
CC fertile and appear healthy. However, compared to wild-type mice they
CC show a clear reduction in brain size, exhibiting a reduction in the
CC size of the cortex and striatum, but not the olfactory bulb or corpus
CC callosum. The total neurite length of neurons in these mice is also
CC significantly shorter. {ECO:0000269|PubMed:21946561}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TRAFAC class
CC myosin-kinesin ATPase superfamily. Myosin family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NYAP family.
CC {ECO:0000305}.
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DR EMBL; AB429291; BAJ19140.1; -; mRNA.
DR EMBL; BC072580; AAH72580.1; -; mRNA.
DR EMBL; BC151049; AAI51050.1; -; mRNA.
DR EMBL; BC151051; AAI51052.1; -; mRNA.
DR EMBL; BC157966; AAI57967.1; -; mRNA.
DR EMBL; BC172122; AAI72122.1; -; mRNA.
DR EMBL; AK082350; BAC38475.1; -; mRNA.
DR EMBL; AK220356; BAD90419.1; -; Transcribed_RNA.
DR CCDS; CCDS40218.2; -. [Q5DU14-1]
DR RefSeq; NP_001306080.1; NM_001319151.1. [Q5DU14-1]
DR RefSeq; XP_006508842.1; XM_006508779.3. [Q5DU14-1]
DR AlphaFoldDB; Q5DU14; -.
DR SMR; Q5DU14; -.
DR BioGRID; 232633; 6.
DR IntAct; Q5DU14; 4.
DR MINT; Q5DU14; -.
DR STRING; 10090.ENSMUSP00000049345; -.
DR iPTMnet; Q5DU14; -.
DR PhosphoSitePlus; Q5DU14; -.
DR PaxDb; Q5DU14; -.
DR PRIDE; Q5DU14; -.
DR ProteomicsDB; 286121; -. [Q5DU14-1]
DR ProteomicsDB; 286122; -. [Q5DU14-2]
DR ProteomicsDB; 286123; -. [Q5DU14-3]
DR Antibodypedia; 42542; 79 antibodies from 20 providers.
DR Ensembl; ENSMUST00000207204; ENSMUSP00000146796; ENSMUSG00000039057. [Q5DU14-3]
DR Ensembl; ENSMUST00000207477; ENSMUSP00000146677; ENSMUSG00000039057. [Q5DU14-1]
DR GeneID; 244281; -.
DR KEGG; mmu:244281; -.
DR UCSC; uc009kus.2; mouse. [Q5DU14-1]
DR UCSC; uc012fzh.1; mouse. [Q5DU14-3]
DR CTD; 23026; -.
DR MGI; MGI:2685951; Myo16.
DR VEuPathDB; HostDB:ENSMUSG00000039057; -.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG1082; Eukaryota.
DR GeneTree; ENSGT00940000158920; -.
DR InParanoid; Q5DU14; -.
DR OMA; CSPHFIH; -.
DR OrthoDB; 59940at2759; -.
DR PhylomeDB; Q5DU14; -.
DR BioGRID-ORCS; 244281; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Myo16; mouse.
DR PRO; PR:Q5DU14; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q5DU14; protein.
DR Bgee; ENSMUSG00000039057; Expressed in habenula and 87 other tissues.
DR ExpressionAtlas; Q5DU14; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0016459; C:myosin complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:HGNC-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:HGNC-UCL.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISS:HGNC-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0021549; P:cerebellum development; ISS:HGNC-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:HGNC-UCL.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:HGNC.
DR GO; GO:0048812; P:neuron projection morphogenesis; IDA:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR CDD; cd14878; MYSc_Myo16; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036042; MYSc_Myo16.
DR InterPro; IPR039482; NYAP_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF15439; NYAP_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ANK repeat; ATP-binding; Cytoplasm;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1919
FT /note="Unconventional myosin-XVI"
FT /id="PRO_0000289137"
FT REPEAT 59..88
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 92..121
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 125..154
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 158..189
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 191..217
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 221..250
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 254..283
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 287..316
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT DOMAIN 400..1143
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1145..1174
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 371..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1365
FT /note="Involved in CYFIP1- and NCKAP1-binding"
FT REGION 1218..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1672..1818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1633
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1883..1897
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 496..503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT VAR_SEQ 431..452
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:21946561"
FT /id="VSP_042365"
FT VAR_SEQ 620..629
FT /note="YVSQGMREDV -> NMSSRCGQTP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052446"
FT VAR_SEQ 657..695
FT /note="EVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQ -> LCLIS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:21946561"
FT /id="VSP_042366"
FT MUTAGEN 1416
FT /note="Y->F: Slight reduction of phosphorylation in HEK293T
FT cells. Abolishes phosphorylation in HEK293T cells and
FT neurons; when associated with F-1441."
FT /evidence="ECO:0000269|PubMed:21946561"
FT MUTAGEN 1441
FT /note="Y->F: Slight reduction of phosphorylation in HEK293T
FT cells. Abolishes phosphorylation in HEK293T cells and in
FT neurons; when associated with F-1416."
FT /evidence="ECO:0000269|PubMed:21946561"
FT CONFLICT 736..737
FT /note="RD -> VN (in Ref. 4; BAD90419)"
FT /evidence="ECO:0000305"
FT CONFLICT 920
FT /note="Missing (in Ref. 4; BAD90419)"
FT /evidence="ECO:0000305"
FT CONFLICT 1605
FT /note="P -> H (in Ref. 1; BAJ19140)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1919 AA; 211383 MW; 9F3899BB2035BD48 CRC64;
MEIDQCLLES LPLGQRQRLV KRMRCEQIKA YYEREKVFQK QEGPLKRSKP GKRQKVRFGL
ADMIQDAVIH HHDKEVLQLL KEGADPHTLV SSGGSLLHLC ARYDNVFIAE VLIDRGVNVN
HQDEDFWTPM HIACACDNPD IVLLLILAGA NVFLQDVNGN IPLDYAVEGT ESSAILLAYL
DEKGVDLSSL RQIKLQRPLS MLTDVRHFLS SGGDVNEKND DGVTLLHMAC ASGYKEVVLL
LLEHGGDLNG TDDRYWTPLH LAAKYGQTTL VKLLLAHQAN PHLVNCNGEK PSDIAASESI
EEMLLKAEIA WEEKMKESPS APSLAQEELY EILHDLPDLS SKLSPLVLPI AKQDSLLEKD
IMFKDTTKGL CKQESQDGPP ETSMTSNCGK PEQVQVMPPA PSDDLATLSE LNDSSLLYEI
QKRFGNDQIH TFIGDIFLLV NPFKELPIYS TMVSQMYLSP TGQRSPSLPP HLFSCAERAF
HRLFQERKPQ NIILSGERGS GKTQASKQIM KYLTSRASSS CTMFDSRLRH AIYIVEAFGH
AKTTLNNVSS CLIQYWELQC CQRRKHITGA RISTYMLEKS RVVAQPPGQG TFLIFSWLMD
GLSSEEKCGL HLNNFCAHRY VSQGMREDVS TAEHSLNKER LAALKHALNV IGFSTLEVEN
LFVILSAILH IGDIQFTALT EADSAFVSDL QLLEQVAGML QVSTDELASA LTTDIQYFKG
DVIIRRHTIQ MAAFYRDLLA KSLYSRLFGF LINTVNCCLQ NQDEYKSLQT LDIGILDIFG
FEEFQKNEFE QLCVNLTNEK MHHYIQEVLF LQEQTECVQE GVAMETACSP GNQAGVLDFF
FQKPSGFFSL LDEESQVIWS GEPNLPRKLQ GLLESSNTNA VYSPVKDGNG NVAFKGQGAA
FTVMHYAGRV MYEMGGAVER NKDSLSQNLL FVMKTSENVV ISHLFQSKLS QTGSLISSYP
SFKFGGHKST LLSKRTASSM VGVNKNYLEL SKLLKKKGTS TFLQRLERGE PATAASQLTK
SLADITAKLQ RGSPHFILCI KPNTSQLPGV FDHFYVSAQL QYLGVLGLVR LFRSGYPVRP
SFEDFLSRYE PLASVLLGET KGQAAEERCR LVLQRCKLQG WQIGVHKVFL KYWHVDQLSD
LWLQLQRKIV TCQKVIRGFL ARQHLLQRMS IKQQEVTSIK SFLQSTEDMA LKTYDALVIQ
NASDIAREHD RLRKEVHTAY HRNRQEEGTK RAEDQGGCRH VHSNSVPVPM VVDSLAQALT
GPSTRPPSLH SVFSMDDSTG LPSPRKQPPP KPKRDPNTRL SASYEAVSAC LSAAKDAAGE
ALTRPRPHSD DYSTMKKIPP RKPKRSPHTK LSGSYEEIWG PPRPSGTMGQ GGRHQAPGTL
SVQWARPDSV PQCTPQLPLH LPLPQGDYDD DAEPVYIEMV GNAARAGGSE TDSPDQGESV
YEEMKYILPE EGCGLGMLTF LPASPPLFLE TRKAIILEAA EGNCQPSKDT CDIPPPFPNL
LPHRPPLLVF PPTPVTRSPA SDESPLTPLE VKKLPVLETN LKYPVQSEGS SPLSPQYSKA
QKGDNDQLAS PGFPVFNGPS RISPPATPPP PPGPPPAPCG PPPAPCGPPP APCGPPPAPC
GPPPAPCGPP PAPCGAASAS CGVAPAPCRP PTHFAFPPES VLVTAAKALT NSDLPRTQPK
PSSAPVPGPC SSFVKAPYSP GKTARADLRK TSSTFSPPSP YSPPNSRPLS SPLDELASLF
NSGRSVLRRS AVGRRIREAE GFETNMNLSS RDEPSSSEMA SETQDRNANN HGTQLSSSLS
SDVTAENGNP VTNGLAEDDG CSRLCLSGMG TSSFQRNRES HTTQVIHQLR LSENESVALQ
ELLDWRRKLC EAREGWQEAL QHPEPRAPPP PPCKKPTLLK KPEGGSCTRL PSQLWDSSM
