NINAC_DROME
ID NINAC_DROME Reviewed; 1501 AA.
AC P10676; P10677; Q8MRP1; Q9VM23; Q9VM24;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Neither inactivation nor afterpotential protein C;
DE EC=2.7.11.1;
GN Name=ninaC; ORFNames=CG5125;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B), AND FUNCTION.
RX PubMed=2449973; DOI=10.1016/0092-8674(88)90413-8;
RA Montell C., Rubin G.M.;
RT "The Drosophila ninaC locus encodes two photoreceptor cell specific
RT proteins with domains homologous to protein kinases and the myosin heavy
RT chain head.";
RL Cell 52:757-772(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP FUNCTION.
RX PubMed=20107052; DOI=10.1523/jneurosci.4464-09.2010;
RA Mecklenburg K.L., Takemori N., Komori N., Chu B., Hardie R.C.,
RA Matsumoto H., O'Tousa J.E.;
RT "Retinophilin is a light-regulated phosphoprotein required to suppress
RT photoreceptor dark noise in Drosophila.";
RL J. Neurosci. 30:1238-1249(2010).
RN [7]
RP FUNCTION, AND INTERACTION WITH RTP.
RX PubMed=20739554; DOI=10.1523/jneurosci.2709-10.2010;
RA Venkatachalam K., Wasserman D., Wang X., Li R., Mills E., Elsaesser R.,
RA Li H.S., Montell C.;
RT "Dependence on a retinophilin/myosin complex for stability of PKC and INAD
RT and termination of phototransduction.";
RL J. Neurosci. 30:11337-11345(2010).
RN [8]
RP INTERACTION WITH RTP, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25822849; DOI=10.1371/journal.pone.0122502;
RA Mecklenburg K.L., Freed S.A., Raval M., Quintero O.A., Yengo C.M.,
RA O'Tousa J.E.;
RT "Invertebrate and vertebrate class III myosins interact with MORN repeat-
RT containing adaptor proteins.";
RL PLoS ONE 10:E0122502-E0122502(2015).
CC -!- FUNCTION: Required for photoreceptor cell function. The ninaC proteins
CC combines putative serine/threonine-protein kinase and myosin activities
CC (PubMed:2449973). Essential for the expression and stability of the rtp
CC protein in the photoreceptors (PubMed:20107052). The rtp/ninaC complex
CC is required for stability of inad and inac and the normal termination
CC of phototransduction in the retina (PubMed:20739554).
CC {ECO:0000269|PubMed:20107052, ECO:0000269|PubMed:20739554,
CC ECO:0000269|PubMed:2449973}.
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 -!- 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;
CC -!- SUBUNIT: Interacts with rtp. {ECO:0000269|PubMed:25822849}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25822849}.
CC Cytoplasm, cytoskeleton. Nucleus {ECO:0000269|PubMed:25822849}.
CC Membrane {ECO:0000269|PubMed:25822849}. Note=Localizes in the cytoplasm
CC or punctate structures within the nuclei in the absence of rtp. Co-
CC localizes with rtp in the rhabdomere membrane.
CC {ECO:0000269|PubMed:25822849}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=Long;
CC IsoId=P10676-1; Sequence=Displayed;
CC Name=A; Synonyms=Short;
CC IsoId=P10676-2; Sequence=VSP_004940, VSP_004941;
CC -!- TISSUE SPECIFICITY: Expressed in the phototransducing compartment of
CC photoreceptor cells, the rhabdomeres (at protein level).
CC {ECO:0000269|PubMed:25822849}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAFAC class
CC myosin-kinesin ATPase superfamily. Myosin family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
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DR EMBL; J03131; AAA28718.1; -; Genomic_DNA.
DR EMBL; J03131; AAA28719.1; -; Genomic_DNA.
DR EMBL; M20230; AAA28721.1; -; mRNA.
DR EMBL; M20231; AAA28720.1; -; mRNA.
DR EMBL; AE014134; AAF52504.3; -; Genomic_DNA.
DR EMBL; AE014134; AAF52505.1; -; Genomic_DNA.
DR EMBL; AY119496; AAM50150.1; -; mRNA.
DR PIR; A29813; A29813.
DR PIR; B29813; B29813.
DR RefSeq; NP_001260189.1; NM_001273260.1. [P10676-2]
DR RefSeq; NP_001260190.1; NM_001273261.1. [P10676-2]
DR RefSeq; NP_523503.2; NM_078779.3. [P10676-1]
DR RefSeq; NP_723271.1; NM_164747.1. [P10676-2]
DR AlphaFoldDB; P10676; -.
DR SMR; P10676; -.
DR BioGRID; 60158; 6.
DR IntAct; P10676; 9.
DR MINT; P10676; -.
DR STRING; 7227.FBpp0079064; -.
DR iPTMnet; P10676; -.
DR PaxDb; P10676; -.
DR PRIDE; P10676; -.
DR EnsemblMetazoa; FBtr0079436; FBpp0079064; FBgn0002938. [P10676-1]
DR EnsemblMetazoa; FBtr0079437; FBpp0079065; FBgn0002938. [P10676-2]
DR EnsemblMetazoa; FBtr0334835; FBpp0306863; FBgn0002938. [P10676-2]
DR EnsemblMetazoa; FBtr0334836; FBpp0306864; FBgn0002938. [P10676-2]
DR GeneID; 34012; -.
DR KEGG; dme:Dmel_CG5125; -.
DR CTD; 34012; -.
DR FlyBase; FBgn0002938; ninaC.
DR VEuPathDB; VectorBase:FBgn0002938; -.
DR eggNOG; KOG0587; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR InParanoid; P10676; -.
DR OMA; FECFHRN; -.
DR PhylomeDB; P10676; -.
DR SignaLink; P10676; -.
DR BioGRID-ORCS; 34012; 0 hits in 3 CRISPR screens.
DR ChiTaRS; ninaC; fly.
DR GenomeRNAi; 34012; -.
DR PRO; PR:P10676; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0002938; Expressed in head capsule and 10 other tissues.
DR ExpressionAtlas; P10676; baseline and differential.
DR Genevisible; P10676; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016027; C:inaD signaling complex; IPI:FlyBase.
DR GO; GO:0042385; C:myosin III complex; NAS:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0033583; C:rhabdomere membrane; IDA:UniProtKB.
DR GO; GO:0016461; C:unconventional myosin complex; ISS:FlyBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IMP:FlyBase.
DR GO; GO:0000146; F:microfilament motor activity; ISS:FlyBase.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0016062; P:adaptation of rhodopsin mediated signaling; IMP:FlyBase.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IMP:FlyBase.
DR GO; GO:0033227; P:dsRNA transport; IMP:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IMP:FlyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:FlyBase.
DR GO; GO:0007602; P:phototransduction; IMP:UniProtKB.
DR GO; GO:0007604; P:phototransduction, UV; IMP:FlyBase.
DR GO; GO:0007603; P:phototransduction, visible light; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:FlyBase.
DR GO; GO:1990146; P:protein localization to rhabdomere; IMP:FlyBase.
DR GO; GO:0030832; P:regulation of actin filament length; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton;
KW Kinase; Membrane; Motor protein; Myosin; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Sensory transduction;
KW Serine/threonine-protein kinase; Transferase; Vision.
FT CHAIN 1..1501
FT /note="Neither inactivation nor afterpotential protein C"
FT /id="PRO_0000086444"
FT DOMAIN 16..282
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 332..1037
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1036..1065
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1072..1101
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 913..934
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1043..1271
FT /note="Interaction with rtp"
FT /evidence="ECO:0000269|PubMed:25822849"
FT REGION 1066..1501
FT /note="Non alpha-helical, C-terminal domain"
FT REGION 1308..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1082..1135
FT /note="AFRGFRDRVRLPPLVNEKSGQLNENTADFIRPFAKKWREKSIFQVLLHYRAA
FT RF -> GKKTQVDRLREYDEEHIDISETPSEAEEMFLEARMDEALAAVRIAKIEQASAE
FT E (in isoform A)"
FT /evidence="ECO:0000303|PubMed:2449973"
FT /id="VSP_004940"
FT VAR_SEQ 1136..1501
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:2449973"
FT /id="VSP_004941"
FT CONFLICT 253
FT /note="Q -> K (in Ref. 1; AAA28718/AAA28719)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="E -> D (in Ref. 4; AAM50150)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="D -> N (in Ref. 1; AAA28718/AAA28719/AAA28721/
FT AAA28720)"
FT /evidence="ECO:0000305"
FT CONFLICT 986
FT /note="A -> P (in Ref. 4; AAM50150)"
FT /evidence="ECO:0000305"
FT CONFLICT 1089
FT /note="R -> P (in Ref. 1; AAA28718)"
FT /evidence="ECO:0000305"
FT CONFLICT 1311
FT /note="V -> E (in Ref. 1; AAA28718/AAA28721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1501 AA; 174300 MW; 164DF87DDA7EB3D1 CRC64;
MMYLPYAQLP DPTDKFEIYE EIAQGVNAKV FRAKELDNDR IVALKIQHYD EEHQVSIEEE
YRTLRDYCDH PNLPEFYGVY KLSKPNGPDE IWFVMEYCAG GTAVDMVNKL LKLDRRMREE
HIAYIIRETC RAAIELNRNH VLHRDIRGDN ILLTKNGRVK LCDFGLSRQV DSTLGKRGTC
IGSPCWMAPE VVSAMESREP DITVRADVWA LGITTIELAD GKPPFADMHP TRAMFQIIRN
PPPTLMRPTN WSQQINDFIS ESLEKNAENR PMMVEMVEHP FLTELIENED EMRSDIAEML
ELSRDVKTLY KEPELFVDRG YVKRFDEKPE KMYPEDLAAL ENPVDENIIE SLRHRILMGE
SYSFIGDILL SLNSNEIKQE FPQEFHAKYR FKSRSENQPH IFSVADIAYQ DMLHHKEPQH
IVLSGESYSG KSTNARLLIK HLCYLGDGNR GATGRVESSI KAILMLVNAG TPVNNDSTRC
VLQYCLTFGK TGKMSGAVFN MYMLEKLRVA TTDGTQHNFH IFYYFYDFIN QQNQLKEYNL
KADRNYRYLR VPPEVPPSKL KYRRDDPEGN VERYREFENI LRDIDFNHKQ LETVRKVLAA
ILNIGNIRFR QNGKYAEVEN TDIVSRIAEL LRVDEKKFMW SLTNFIMVKG GIAERRQYTT
EEARDARDAV ASTLYSRLVD FIINRINMNM SFPRAVFGDT NAIIIHDMFG FECFNRNGLE
QLMINTLNEQ MQYHYNQRIF ISEMLEMEAE DIDTINLNFY DNKTALDNLL TKPDGLFYII
DDASRSCQDQ DLIMDRVSEK HSQFVKKHTA TEISVAHYTG RIIYDTRAFT DINRDFVPPE
MIETFRSSLD ESIMLMFTNQ LTKAGNLTMP FEAVQHKDES ERKSYALNTL SAGCISQVNN
LRTLAANFRF TCLTLLKMLS QNANLGVHFV RCIRADLEYK PRSFHSDVVQ QQMKALGVLD
TVIARQKGFS SRLPFDEFLR RYQFLAFDFD EPVEMTKDNC RLLFLRLKME GWALGKTKVF
LRYYNDEFLA RLYELQVKKV IKVQSMMRAL LARKRVKGGK VFKLGKKGPE HHDVAASKIQ
KAFRGFRDRV RLPPLVNEKS GQLNENTADF IRPFAKKWRE KSIFQVLLHY RAARFQDFVN
LSQQVHIYNQ RMVAGLNKCT RAVPFERINM REVNSSQLGP LPVPIKKMPF RLDQIPFYDT
QYMVDPANSI SRQAFPNQLL TQHMEDDEPW DSPLQRNPSM TSCALTYNAY KKEQACQTNW
DRMGESDNIY NQGYFRDPQQ LRRNQMQMNM NAYNNAYNSY NSNYNNQNWG VHRSGSRRNS
LKGYAAPPPP PPPMPSSNYY RNNPNQQQRN YQQRSSYPPS DPVRELQNMA RNEGDNSEDP
PFNFKAMLRK TNYPRGSETN TYDFNNRRGS DSGDQHTFQP PKLRSTGRRY QDDEGYNSSS
GNYGVSRKFG QQQRAPTLRQ SPASVGRSFE DSNARSFEEA GSYVEEEIAP GITLSGYAVD
I
