IMD_DROME
ID IMD_DROME Reviewed; 273 AA.
AC Q7K4Z4; Q9NHG0;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein immune deficiency {ECO:0000303|PubMed:7568155};
GN Name=imd {ECO:0000303|PubMed:7568155, ECO:0000312|FlyBase:FBgn0013983};
GN ORFNames=CG5576 {ECO:0000312|FlyBase:FBgn0013983};
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] {ECO:0000312|EMBL:AAF44326.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhou L., Steller H.;
RT "BG5_Drosophila death-domain containing protein similar to cell death
RT protein RIP.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAK92982.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK92982.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAK92982.1};
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] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ALA-31.
RX PubMed=7568155; DOI=10.1073/pnas.92.21.9465;
RA Lemaitre B., Kromer-Metzger E., Michaut L., Nicolas E., Meister M.,
RA Georgel P., Reichhart J.M., Hoffmann J.A.;
RT "A recessive mutation, immune deficiency (imd), defines two distinct
RT control pathways in the Drosophila host defense.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9465-9469(1995).
RN [6] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ALA-31.
RX PubMed=8808632; DOI=10.1016/s0092-8674(00)80172-5;
RA Lemaitre B., Nicolas E., Michaut L., Reichhart J.-M., Hoffmann J.A.;
RT "The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the
RT potent antifungal response in Drosophila adults.";
RL Cell 86:973-983(1996).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=11269502; DOI=10.1093/embo-reports/kvd073;
RA Leulier F., Rodriguez A., Khush R.S., Abrams J.M., Lemaitre B.;
RT "The Drosophila caspase Dredd is required to resist Gram-negative bacterial
RT infection.";
RL EMBO Rep. 1:353-358(2000).
RN [8] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ALA-31.
RX PubMed=11703941; DOI=10.1016/s1534-5807(01)00059-4;
RA Georgel P., Naitza S., Kappler C., Ferrandon D., Zachary D., Swimmer C.,
RA Kopczynski C., Duyk G., Reichhart J.M., Hoffmann J.A.;
RT "Drosophila immune deficiency (IMD) is a death domain protein that
RT activates antibacterial defense and can promote apoptosis.";
RL Dev. Cell 1:503-514(2001).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=11266367; DOI=10.1093/embo-reports/kve048;
RA Onfelt Tingvall T., Roos E., Engstroem Y.;
RT "The imd gene is required for local Cecropin expression in Drosophila
RT barrier epithelia.";
RL EMBO Rep. 2:239-243(2001).
RN [10] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH FADD.
RX PubMed=12433364; DOI=10.1016/s1074-7613(02)00454-5;
RA Naitza S., Rosse C., Kappler C., Georgel P., Belvin M., Gubb D.,
RA Camonis J., Hoffmann J.A., Reichhart J.-M.;
RT "The Drosophila immune defense against Gram-negative infection requires the
RT death protein dFADD.";
RL Immunity 17:575-581(2002).
RN [11] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SCNY, DEUBIQUITINATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19837371; DOI=10.1016/j.chom.2009.09.007;
RA Thevenon D., Engel E., Avet-Rochex A., Gottar M., Bergeret E., Tricoire H.,
RA Benaud C., Baudier J., Taillebourg E., Fauvarque M.O.;
RT "The Drosophila ubiquitin-specific protease dUSP36/Scny targets IMD to
RT prevent constitutive immune signaling.";
RL Cell Host Microbe 6:309-320(2009).
RN [12] {ECO:0000305}
RP FUNCTION.
RX PubMed=19763182; DOI=10.1371/journal.ppat.1000582;
RA Avadhanula V., Weasner B.P., Hardy G.G., Kumar J.P., Hardy R.W.;
RT "A novel system for the launch of alphavirus RNA synthesis reveals a role
RT for the Imd pathway in arthropod antiviral response.";
RL PLoS Pathog. 5:E1000582-E1000582(2009).
RN [13] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DIAP2, PHOSPHORYLATION, PROTEOLYTIC CLEAVAGE,
RP UBIQUITINATION, AND MUTAGENESIS OF ASP-30.
RX PubMed=20122400; DOI=10.1016/j.molcel.2009.12.036;
RA Paquette N., Broemer M., Aggarwal K., Chen L., Husson M.,
RA Ertuerk-Hasdemir D., Reichhart J.M., Meier P., Silverman N.;
RT "Caspase-mediated cleavage, IAP binding, and ubiquitination: linking three
RT mechanisms crucial for Drosophila NF-kappaB signaling.";
RL Mol. Cell 37:172-182(2010).
RN [14] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH FAF.
RX PubMed=23919485; DOI=10.1111/gtc.12085;
RA Yagi Y., Lim Y.M., Tsuda L., Nishida Y.;
RT "fat facets induces polyubiquitination of Imd and inhibits the innate
RT immune response in Drosophila.";
RL Genes Cells 18:934-945(2013).
RN [15] {ECO:0000305}
RP INTERACTION WITH USP2 AND RPT6, AND DEUBIQUITINATION.
RX PubMed=25027767; DOI=10.1186/s12964-014-0041-2;
RA Engel E., Viargues P., Mortier M., Taillebourg E., Coute Y., Thevenon D.,
RA Fauvarque M.O.;
RT "Identifying USPs regulating immune signals in Drosophila: USP2
RT deubiquitinates Imd and promotes its degradation by interacting with the
RT proteasome.";
RL Cell Commun. Signal. 12:41-41(2014).
CC -!- FUNCTION: Essential for the imd/NF-kappa-B (Imd) humoral and epithelial
CC immune response to Gram-negative bacteria (PubMed:7568155,
CC PubMed:8808632, PubMed:11266367, PubMed:12433364). Functions as an
CC adapter protein that transduces immunity signals from the activation of
CC pathogen recognition receptors (PRRs) by bacterial infection to the Imd
CC signaling pathway (PubMed:7568155, PubMed:11269502, PubMed:11703941,
CC PubMed:12433364, PubMed:20122400). Binding of diaminopimelic acid-type
CC (DAP-type) bacterial peptidoglycans (PGN) causes multimerization or
CC clustering of PGRP receptors which activate the Imd cascade probably by
CC recruiting imd, Fadd and Dredd to the receptor complex
CC (PubMed:11269502, PubMed:12433364, PubMed:20122400). Once in proximity,
CC Dredd cleaves imd in a Fadd-dependent manner to enable its association
CC and activation by the ubiquitin E3-ligase DIAP2 (PubMed:20122400). The
CC activated form of imd recruits and activates the Tab2/Tak1 complex thus
CC acting upstream of the IKK complex (ird5 and key) to activate Rel and
CC induce the expression of antimicrobial peptides such as Def, Dpt and
CC Cecropin (PubMed:7568155, PubMed:8808632, PubMed:11703941,
CC PubMed:12433364, PubMed:19837371, PubMed:20122400, PubMed:11266367).
CC Also able to inhibit the viral replication of the Sindbis virus
CC (PubMed:19763182). Involved in promoting the polyubiquitination and
CC stability of faf which in turn, regulates the Imd pathway by
CC controlling imd polyubiquitination and/or stability; they may therefore
CC form a regulatory feedback mechanism within the Imd pathway
CC (PubMed:23919485). Not required for the cuticle melanization immune
CC response to bacterial challenge (PubMed:11266367).
CC {ECO:0000269|PubMed:11266367, ECO:0000269|PubMed:11269502,
CC ECO:0000269|PubMed:11703941, ECO:0000269|PubMed:12433364,
CC ECO:0000269|PubMed:19763182, ECO:0000269|PubMed:19837371,
CC ECO:0000269|PubMed:20122400, ECO:0000269|PubMed:23919485,
CC ECO:0000269|PubMed:7568155, ECO:0000269|PubMed:8808632}.
CC -!- SUBUNIT: Interacts with Fadd (PubMed:12433364). Interacts with faf
CC (PubMed:23919485). Interacts with Rpt6 (PubMed:25027767). Interacts
CC (via N-terminus) with Usp2 (via N-terminus) (PubMed:25027767).
CC Interacts (via N-terminus) with scny (via C-terminus)
CC (PubMed:19837371). The N-terminally cleaved form interacts (via IAP-
CC Binding motif) with Diap2 (via the BIR2 and BIR3 domains); the
CC interaction promotes ubiquitination by Diap2 and the E2 ligases Uev1A,
CC ben and Ubc5 (PubMed:20122400). {ECO:0000269|PubMed:12433364,
CC ECO:0000269|PubMed:19837371, ECO:0000269|PubMed:20122400,
CC ECO:0000269|PubMed:23919485, ECO:0000269|PubMed:25027767}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:20122400}.
CC -!- PTM: Caspase-mediated cleavage is required for activation and function;
CC upon immune stimulation, peptidoglycans (PGN) induce proteolytic
CC cleavage by caspases such as Dredd leading to its ubiquitination.
CC {ECO:0000269|PubMed:20122400}.
CC -!- PTM: Ubiquitination is essential for function; after PGN-induced
CC caspase-mediated cleavage the N-terminally cleaved imd interacts with
CC the E3 ligase Diap2 leading to polyubiquitination of 'Lys-63'-linked
CC chains involving the E2 complex members Uev1A, ben and Ubc5
CC (PubMed:20122400). These 'Lys-63' chains stabilize imd and may serve as
CC scaffolds to recruit and activate the key kinases TAK1 and IKK
CC (PubMed:20122400). Under normal unchallenged conditions, scny
CC deubiquitinates the activating 'Lys-63'-linked chains to prevent signal
CC transduction and this is also likely to promote the polyubiquitination
CC of 'Lys-48'-linked chains which act as 'tags' for proteosomal
CC degradation (PubMed:19837371). Usp2 then deubiquitinates the 'Lys-48'-
CC linked chains and this promotes degradation of imd probably by allowing
CC interaction between imd and the proteasome (PubMed:25027767).
CC {ECO:0000269|PubMed:19837371, ECO:0000269|PubMed:20122400,
CC ECO:0000269|PubMed:25027767}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the fat body results
CC in reduced expression of the antimicrobial peptide gene Dpt following
CC infection with E.coli. {ECO:0000269|PubMed:19837371}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF44326.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF44326.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF222006; AAF44326.1; ALT_SEQ; mRNA.
DR EMBL; AE013599; AAF57692.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56367.1; -; Genomic_DNA.
DR EMBL; AY051558; AAK92982.1; -; mRNA.
DR RefSeq; NP_001286572.1; NM_001299643.1.
DR RefSeq; NP_573394.1; NM_133166.4.
DR AlphaFoldDB; Q7K4Z4; -.
DR SMR; Q7K4Z4; -.
DR ELM; Q7K4Z4; -.
DR IntAct; Q7K4Z4; 4.
DR STRING; 7227.FBpp0085904; -.
DR PaxDb; Q7K4Z4; -.
DR PRIDE; Q7K4Z4; -.
DR DNASU; 44339; -.
DR EnsemblMetazoa; FBtr0086725; FBpp0085904; FBgn0013983.
DR EnsemblMetazoa; FBtr0345891; FBpp0311815; FBgn0013983.
DR GeneID; 44339; -.
DR KEGG; dme:Dmel_CG5576; -.
DR UCSC; CG5576-RA; d. melanogaster.
DR CTD; 44339; -.
DR FlyBase; FBgn0013983; imd.
DR VEuPathDB; VectorBase:FBgn0013983; -.
DR eggNOG; ENOG502S6XJ; Eukaryota.
DR HOGENOM; CLU_991335_0_0_1; -.
DR InParanoid; Q7K4Z4; -.
DR OMA; DPNYNSM; -.
DR OrthoDB; 1460301at2759; -.
DR PhylomeDB; Q7K4Z4; -.
DR Reactome; R-DME-214397; Assembly of the PGN:PGRP-LC/LE receptor 'signalling complex'.
DR Reactome; R-DME-214399; Activated IkappaB kinase (IKK) complex, Phospho IRD5:KEY dimer, phosphorylates REL in the PGN:PGRP-LC/LE receptor 'signalling complex'.
DR Reactome; R-DME-214411; REL binds to DREDD in the PGN:PGRP-LC/LE receptor 'signalling complex'.
DR Reactome; R-DME-214416; Phosphorylated REL is cleaved by and dissociates from DREDD.
DR SignaLink; Q7K4Z4; -.
DR BioGRID-ORCS; 44339; 0 hits in 1 CRISPR screen.
DR ChiTaRS; imd; fly.
DR GenomeRNAi; 44339; -.
DR PRO; PR:Q7K4Z4; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0013983; Expressed in saliva-secreting gland and 25 other tissues.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070513; F:death domain binding; IPI:FlyBase.
DR GO; GO:0019731; P:antibacterial humoral response; IMP:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; TAS:FlyBase.
DR GO; GO:0006959; P:humoral immune response; IMP:FlyBase.
DR GO; GO:0006955; P:immune response; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:UniProtKB.
DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
DR GO; GO:0002803; P:positive regulation of antibacterial peptide production; IGI:FlyBase.
DR GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; HMP:FlyBase.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:FlyBase.
DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:FlyBase.
DR GO; GO:0009617; P:response to bacterium; NAS:FlyBase.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR Pfam; PF00531; Death; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Immunity; Innate immunity; Reference proteome; Ubl conjugation.
FT CHAIN 1..273
FT /note="Protein immune deficiency"
FT /id="PRO_0000445481"
FT DOMAIN 176..260
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..178
FT /note="May be required for interaction with Fadd"
FT /evidence="ECO:0000269|PubMed:12433364"
FT REGION 134..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..177
FT /note="Essential for ubiquitination and the induction of
FT Dpt"
FT /evidence="ECO:0000269|PubMed:20122400"
FT MOTIF 31..34
FT /note="IAP-binding motif"
FT /evidence="ECO:0000269|PubMed:20122400"
FT COMPBIAS 37..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 30..31
FT /note="Cleavage; by Dredd"
FT /evidence="ECO:0000269|PubMed:20122400"
FT MUTAGEN 30
FT /note="D->A: Loss of function. Abolishes caspase-mediated
FT cleavage and ubiquitination. Blocks expression of Dpt in
FT response to E.coli peptidoglycans (PGN)."
FT /evidence="ECO:0000269|PubMed:20122400"
FT MUTAGEN 31
FT /note="A->V: In imd-1; immune response defective. Reduced
FT survival and decreased induction of various antibacterial
FT peptides after bacterial challenge. Abolishes
FT ubiquitination and reduces binding to Diap2 but has no
FT effect on caspase-mediated cleavage. Increased resistance
FT to UV radiation. No effect on survival after infection with
FT the fungus A.fumigatus. No effect on up-regulation of Drs
FT after bacterial challenge."
FT /evidence="ECO:0000269|PubMed:11703941,
FT ECO:0000269|PubMed:20122400, ECO:0000269|PubMed:7568155,
FT ECO:0000269|PubMed:8808632"
SQ SEQUENCE 273 AA; 29899 MW; 7247CA4B46F5545B CRC64;
MSKLRNLLPT IFGGKEAQNP TPVEGRLEKD AAPVDDNEPD NNNSGALALP STAGTPTASS
DLTESVLREL SDPNYNSMDV VHSANIPGTL SNVQTNNTMN VHSAQQQVVM NFSNANNLHF
GSVYNFNQNL SACSSRKGST STAEESVASP DGKPRASATR KTVSIVAMMQ SQEEPDVRLL
DVVSTHLGEG WKQVMRDLGM SEGQIDQAII DHQMHGNIRE VIYQLLLQWI RSSADGVATV
GRLTTLLWES QHRDCVQRMK LVWKALEKRK TNS
