INAD_DROME
ID INAD_DROME Reviewed; 674 AA.
AC Q24008; Q9NBV3;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Inactivation-no-after-potential D protein;
GN Name=inaD; ORFNames=CG3504;
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 {ECO:0000312|EMBL:AAO42637.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF MET-442.
RC TISSUE=Retinal photoreceptor;
RX PubMed=7826638; DOI=10.1016/0896-6273(95)90255-4;
RA Shieh B.-H., Niemeyer B.;
RT "A novel protein encoded by the InaD gene regulates recovery of visual
RT transduction in Drosophila.";
RL Neuron 14:201-210(1995).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF PRO-282;
RP 308-ARG--HIS-310; HIS-310; ASN-319 AND LYS-333, AND INTERACTION WITH INAC.
RC STRAIN=Canton-S {ECO:0000312|EMBL:AAF81203.1}, and
RC Oregon-R {ECO:0000269|PubMed:11342563};
RX PubMed=11342563; DOI=10.1074/jbc.m103570200;
RA Kumar R., Shieh B.-H.;
RT "The second PDZ domain of INAD is a type I domain involved in binding to
RT eye protein kinase C. Mutational analysis and naturally occurring
RT variants.";
RL J. Biol. Chem. 276:24971-24977(2001).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [4]
RP GENOME REANNOTATION.
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 [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000305}; TISSUE=Head {ECO:0000305};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH TRP, AND MUTAGENESIS OF MET-442.
RX PubMed=8630257; DOI=10.1016/s0896-6273(00)80122-1;
RA Shieh B.-H., Zhu M.-Y.;
RT "Regulation of the TRP Ca2+ channel by INAD in Drosophila photoreceptors.";
RL Neuron 16:991-998(1996).
RN [7]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH TRP; NORPA;
RP RHODOPSIN AND CALMODULIN.
RX PubMed=9010208; DOI=10.1016/s0896-6273(01)80049-0;
RA Chevesich J., Kreuz A.J., Montell C.;
RT "Requirement for the PDZ domain protein, INAD, for localization of the TRP
RT store-operated channel to a signaling complex.";
RL Neuron 18:95-105(1997).
RN [8]
RP PHOSPHORYLATION.
RX PubMed=10766855; DOI=10.1074/jbc.275.16.12194;
RA Liu M., Parker L.L., Wadzinski B.E., Shieh B.-H.;
RT "Reversible phosphorylation of the signal transduction complex in
RT Drosophila photoreceptors.";
RL J. Biol. Chem. 275:12194-12199(2000).
RN [9]
RP INTERACTION WITH TRP.
RX PubMed=10995445; DOI=10.1083/jcb.150.6.1411;
RA Li H.-S., Montell C.;
RT "TRP and the PDZ protein, INAD, form the core complex required for
RT retention of the signalplex in Drosophila photoreceptor cells.";
RL J. Cell Biol. 150:1411-1422(2000).
RN [10]
RP INTERACTION WITH FKBP59, AND IDENTIFICATION IN A COMPLEX WITH TRPL.
RX PubMed=11514552; DOI=10.1074/jbc.m104125200;
RA Goel M., Garcia R., Estacion M., Schilling W.P.;
RT "Regulation of Drosophila TRPL channels by immunophilin FKBP59.";
RL J. Biol. Chem. 276:38762-38773(2001).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598 AND SER-600, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [12] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 11-107 IN A COMPLEX WITH NORPA.
RX PubMed=11500369; DOI=10.1093/emboj/20.16.4414;
RA Kimple M.E., Siderovski D.P., Sondek J.;
RT "Functional relevance of the disulfide-linked complex of the N-terminal PDZ
RT domain of InaD with NorpA.";
RL EMBO J. 20:4414-4422(2001).
CC -!- FUNCTION: Involved in the negative feedback regulation of the light-
CC activated signaling cascade in photoreceptors through a calcium-
CC mediated process. Interacts with tetrapeptide ligand located in C-
CC terminal sequence of 3 key components of the visual cascade, tethering
CC them and forming a macromolecular signaling phototransduction complex.
CC {ECO:0000269|PubMed:11342563, ECO:0000269|PubMed:7826638}.
CC -!- SUBUNIT: Interacts with the C-terminus of trp, and with norpA and inaC
CC to form the inaD signaling complex. Interacts with Fkbp59, which
CC together with trpl, rhodopsin and calmodulin may also be part of the
CC inaD complex. {ECO:0000269|PubMed:10995445,
CC ECO:0000269|PubMed:11342563, ECO:0000269|PubMed:11514552,
CC ECO:0000269|PubMed:8630257, ECO:0000269|PubMed:9010208}.
CC -!- INTERACTION:
CC Q24008; P13677: inaC; NbExp=2; IntAct=EBI-195326, EBI-130595;
CC Q24008; A8WH76: inaF-B; NbExp=2; IntAct=EBI-195326, EBI-15668597;
CC Q24008; A3RLX3: Kon; NbExp=3; IntAct=EBI-195326, EBI-4306640;
CC Q24008; P13217: norpA; NbExp=4; IntAct=EBI-195326, EBI-101510;
CC Q24008; P19334: trp; NbExp=10; IntAct=EBI-195326, EBI-165136;
CC Q24008; Q9W2S5: X11Lbeta; NbExp=2; IntAct=EBI-195326, EBI-121784;
CC Q24008; P17252: PRKCA; Xeno; NbExp=2; IntAct=EBI-195326, EBI-1383528;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9010208};
CC Peripheral membrane protein {ECO:0000269|PubMed:9010208}.
CC -!- TISSUE SPECIFICITY: Expressed in rhabdomeres of the compound eyes and
CC ocelli. {ECO:0000269|PubMed:7826638}.
CC -!- DOMAIN: Second PDZ domain is a type I PDZ domain that tethers type I
CC PDZ ligand inaC by interaction with its C-terminus.
CC {ECO:0000269|PubMed:11342563}.
CC -!- PTM: Phosphorylated by inaC. {ECO:0000269|PubMed:10766855,
CC ECO:0000269|PubMed:17372656}.
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DR EMBL; U15803; AAC36490.1; -; mRNA.
DR EMBL; AF245280; AAF81203.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF46915.1; -; Genomic_DNA.
DR EMBL; BT004473; AAO42637.1; -; mRNA.
DR RefSeq; NP_726260.1; NM_166566.1.
DR PDB; 1IHJ; X-ray; 1.80 A; A/B=11-107.
DR PDB; 2LA8; NMR; -; A=580-665.
DR PDB; 2QKT; X-ray; 2.05 A; A/B=580-665.
DR PDB; 2QKU; X-ray; 2.20 A; A/B/C=580-665.
DR PDB; 2QKV; X-ray; 1.55 A; A/B=580-665.
DR PDB; 3R0H; X-ray; 2.60 A; A/B/C/D/E/F/G/H=473-674.
DR PDB; 5F67; X-ray; 1.76 A; A/B=345-448.
DR PDB; 6IRE; X-ray; 3.25 A; B=478-671.
DR PDBsum; 1IHJ; -.
DR PDBsum; 2LA8; -.
DR PDBsum; 2QKT; -.
DR PDBsum; 2QKU; -.
DR PDBsum; 2QKV; -.
DR PDBsum; 3R0H; -.
DR PDBsum; 5F67; -.
DR PDBsum; 6IRE; -.
DR AlphaFoldDB; Q24008; -.
DR BMRB; Q24008; -.
DR SMR; Q24008; -.
DR BioGRID; 63241; 22.
DR DIP; DIP-18621N; -.
DR IntAct; Q24008; 10.
DR MINT; Q24008; -.
DR STRING; 7227.FBpp0293662; -.
DR iPTMnet; Q24008; -.
DR PaxDb; Q24008; -.
DR PRIDE; Q24008; -.
DR DNASU; 37629; -.
DR EnsemblMetazoa; FBtr0071909; FBpp0071820; FBgn0001263.
DR GeneID; 37629; -.
DR KEGG; dme:Dmel_CG3504; -.
DR CTD; 37629; -.
DR FlyBase; FBgn0001263; inaD.
DR VEuPathDB; VectorBase:FBgn0001263; -.
DR eggNOG; KOG3528; Eukaryota.
DR HOGENOM; CLU_025815_0_0_1; -.
DR InParanoid; Q24008; -.
DR OMA; HIHMVTL; -.
DR PhylomeDB; Q24008; -.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q24008; -.
DR BioGRID-ORCS; 37629; 0 hits in 3 CRISPR screens.
DR ChiTaRS; inaD; fly.
DR EvolutionaryTrace; Q24008; -.
DR GenomeRNAi; 37629; -.
DR PRO; PR:Q24008; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0001263; Expressed in head capsule and 8 other tissues.
DR ExpressionAtlas; Q24008; baseline and differential.
DR Genevisible; Q24008; DM.
DR GO; GO:0016027; C:inaD signaling complex; IPI:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0005516; F:calmodulin binding; TAS:FlyBase.
DR GO; GO:0017022; F:myosin binding; TAS:FlyBase.
DR GO; GO:0031473; F:myosin III binding; IPI:FlyBase.
DR GO; GO:0009881; F:photoreceptor activity; IMP:FlyBase.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IDA:FlyBase.
DR GO; GO:0071482; P:cellular response to light stimulus; IMP:FlyBase.
DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IMP:FlyBase.
DR GO; GO:0050962; P:detection of light stimulus involved in sensory perception; IMP:FlyBase.
DR GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; TAS:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 5.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 5.
DR SMART; SM00228; PDZ; 5.
DR SUPFAM; SSF50156; SSF50156; 5.
DR PROSITE; PS50106; PDZ; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Sensory transduction; Vision.
FT CHAIN 1..674
FT /note="Inactivation-no-after-potential D protein"
FT /id="PRO_0000084194"
FT DOMAIN 17..106
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143,
FT ECO:0000305"
FT DOMAIN 249..332
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143,
FT ECO:0000305"
FT DOMAIN 364..448
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143,
FT ECO:0000305"
FT DOMAIN 489..577
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143,
FT ECO:0000305"
FT DOMAIN 584..664
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143,
FT ECO:0000305"
FT REGION 133..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MUTAGEN 282
FT /note="P->L: Nearly 2-fold increase in interaction with
FT inaC."
FT /evidence="ECO:0000269|PubMed:11342563"
FT MUTAGEN 308..310
FT /note="RCH->GCL: 75% reduced interaction with inaC."
FT /evidence="ECO:0000269|PubMed:11342563"
FT MUTAGEN 310
FT /note="H->L: 100% increased interaction with inaC."
FT /evidence="ECO:0000269|PubMed:11342563"
FT MUTAGEN 310
FT /note="H->R: 50% reduced interaction with inaC."
FT /evidence="ECO:0000269|PubMed:11342563"
FT MUTAGEN 319
FT /note="N->S: Over 3-fold increase in interaction with
FT inaC."
FT /evidence="ECO:0000269|PubMed:11342563"
FT MUTAGEN 333
FT /note="K->Q: Slight reduction in interaction with inaC."
FT /evidence="ECO:0000269|PubMed:11342563"
FT MUTAGEN 442
FT /note="M->K: In allele inaD-P215; slow recovery of light-
FT induced responses and altered light sensitivity. Abolishes
FT interaction with trp."
FT /evidence="ECO:0000269|PubMed:7826638,
FT ECO:0000269|PubMed:8630257"
FT CONFLICT 319
FT /note="N -> S (in Ref. 2; AAF81203)"
FT /evidence="ECO:0000305"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:1IHJ"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1IHJ"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1IHJ"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1IHJ"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:1IHJ"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:1IHJ"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1IHJ"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:1IHJ"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:1IHJ"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:5F67"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:5F67"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:5F67"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:5F67"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:5F67"
FT STRAND 388..397
FT /evidence="ECO:0007829|PDB:5F67"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:5F67"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:5F67"
FT HELIX 426..435
FT /evidence="ECO:0007829|PDB:5F67"
FT STRAND 438..445
FT /evidence="ECO:0007829|PDB:5F67"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:3R0H"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:3R0H"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:3R0H"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:3R0H"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:3R0H"
FT HELIX 525..529
FT /evidence="ECO:0007829|PDB:3R0H"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:3R0H"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:3R0H"
FT HELIX 553..561
FT /evidence="ECO:0007829|PDB:3R0H"
FT STRAND 565..573
FT /evidence="ECO:0007829|PDB:3R0H"
FT STRAND 583..588
FT /evidence="ECO:0007829|PDB:2QKV"
FT STRAND 590..593
FT /evidence="ECO:0007829|PDB:2LA8"
FT STRAND 597..601
FT /evidence="ECO:0007829|PDB:2QKV"
FT STRAND 603..611
FT /evidence="ECO:0007829|PDB:2QKV"
FT HELIX 617..622
FT /evidence="ECO:0007829|PDB:2QKV"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:2QKV"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:2LA8"
FT HELIX 642..650
FT /evidence="ECO:0007829|PDB:2QKV"
FT STRAND 653..661
FT /evidence="ECO:0007829|PDB:2QKV"
SQ SEQUENCE 674 AA; 74332 MW; D4C24091D99EA7F3 CRC64;
MVQFLGKQGT AGELIHMVTL DKTGKKSFGI CIVRGEVKDS PNTKTTGIFI KGIVPDSPAH
LCGRLKVGDR ILSLNGKDVR NSTEQAVIDL IKEADFKIEL EIQTFDKSDE QQAKSDPRSN
GYMQAKNKFN QEQTTNNNAS GGQGMGQGQG QGQGMAGMNR QQSMQKRNTT FTASMRQKHS
NYADEDDEDT RDMTGRIRTE AGYEIDRASA GNCKLNKQEK DRDKEQEDEF GYTMAKINKR
YNMMKDLRRI EVQRDASKPL GLALAGHKDR QKMACFVAGV DPNGALGSVD IKPGDEIVEV
NGNVLKNRCH LNASAVFKNV DGDKLVMITS RRKPNDEGMC VKPIKKFPTA SDETKFIFDQ
FPKARTVQVR KEGFLGIMVI YGKHAEVGSG IFISDLREGS NAELAGVKVG DMLLAVNQDV
TLESNYDDAT GLLKRAEGVV TMILLTLKSE EAIKAEKAAE EKKKEEAKKE EEKPQEPATA
EIKPNKKILI ELKVEKKPMG VIVCGGKNNH VTTGCVITHV YPEGQVAADK RLKIFDHICD
INGTPIHVGS MTTLKVHQLF HTTYEKAVTL TVFRADPPEL EKFNVDLMKK AGKELGLSLS
PNEIGCTIAD LIQGQYPEID SKLQRGDIIT KFNGDALEGL PFQVCYALFK GANGKVSMEV
TRPKPTLRTE APKA
