ZUC_DROME
ID ZUC_DROME Reviewed; 253 AA.
AC Q9VKD7; A0AP42; A0AP43; A0AP44; A0AP47; A0AP48; A0AP51;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Mitochondrial cardiolipin hydrolase;
DE EC=3.1.4.-;
DE AltName: Full=Mitochondrial phospholipase {ECO:0000250|UniProtKB:Q8N2A8};
DE Short=MitoPLD {ECO:0000250|UniProtKB:Q8N2A8};
DE AltName: Full=Protein zucchini {ECO:0000303|PubMed:17543859};
GN Name=zuc {ECO:0000303|PubMed:17543859, ECO:0000312|FlyBase:FBgn0261266};
GN ORFNames=CG12314 {ECO:0000312|FlyBase:FBgn0261266};
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].
RC STRAIN=ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL229, ZBMEL377,
RC ZBMEL384, ZBMEL398, ZBMEL82, ZBMEL84, and ZBMEL95;
RX PubMed=16951084; DOI=10.1534/genetics.106.058008;
RA Proeschel M., Zhang Z., Parsch J.;
RT "Widespread adaptive evolution of Drosophila genes with sex-biased
RT expression.";
RL Genetics 174:893-900(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MEL01, MEL02, MEL11, MEL12, MEL13, MEL14, MEL15, MEL16, MEL17,
RC MEL18, MEL19, and MEL20;
RX PubMed=19126864; DOI=10.1093/molbev/msn297;
RA Parsch J., Zhang Z., Baines J.F.;
RT "The influence of demography and weak selection on the McDonald-Kreitman
RT test: an empirical study in Drosophila.";
RL Mol. Biol. Evol. 26:691-698(2009).
RN [3]
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 [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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [6]
RP FUNCTION, MUTAGENESIS OF ALA-47 AND HIS-169, AND DISRUPTION PHENOTYPE.
RX PubMed=17543859; DOI=10.1016/j.devcel.2007.03.022;
RA Pane A., Wehr K., Schupbach T.;
RT "zucchini and squash encode two putative nucleases required for rasiRNA
RT production in the Drosophila germline.";
RL Dev. Cell 12:851-862(2007).
RN [7]
RP FUNCTION.
RX PubMed=19812547; DOI=10.1038/nature08501;
RA Saito K., Inagaki S., Mituyama T., Kawamura Y., Ono Y., Sakota E.,
RA Kotani H., Asai K., Siomi H., Siomi M.C.;
RT "A regulatory circuit for piwi by the large Maf gene traffic jam in
RT Drosophila.";
RL Nature 461:1296-1299(2009).
RN [8]
RP FUNCTION.
RX PubMed=20818334; DOI=10.1038/emboj.2010.212;
RA Olivieri D., Sykora M.M., Sachidanandam R., Mechtler K., Brennecke J.;
RT "An in vivo RNAi assay identifies major genetic and cellular requirements
RT for primary piRNA biogenesis in Drosophila.";
RL EMBO J. 29:3301-3317(2010).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20966047; DOI=10.1101/gad.1989510;
RA Saito K., Ishizu H., Komai M., Kotani H., Kawamura Y., Nishida K.M.,
RA Siomi H., Siomi M.C.;
RT "Roles for the Yb body components Armitage and Yb in primary piRNA
RT biogenesis in Drosophila.";
RL Genes Dev. 24:2493-2498(2010).
RN [10]
RP FUNCTION.
RX PubMed=20966049; DOI=10.1101/gad.1968110;
RA Haase A.D., Fenoglio S., Muerdter F., Guzzardo P.M., Czech B., Pappin D.J.,
RA Chen C., Gordon A., Hannon G.J.;
RT "Probing the initiation and effector phases of the somatic piRNA pathway in
RT Drosophila.";
RL Genes Dev. 24:2499-2504(2010).
RN [11]
RP FUNCTION.
RX PubMed=20559422; DOI=10.1371/journal.pone.0011032;
RA Todeschini A.L., Teysset L., Delmarre V., Ronsseray S.;
RT "The epigenetic trans-silencing effect in Drosophila involves maternally-
RT transmitted small RNAs whose production depends on the piRNA pathway and
RT HP1.";
RL PLoS ONE 5:E11032-E11032(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-169.
RX PubMed=21397848; DOI=10.1016/j.devcel.2011.01.004;
RA Huang H., Gao Q., Peng X., Choi S.Y., Sarma K., Ren H., Morris A.J.,
RA Frohman M.A.;
RT "piRNA-associated germline nuage formation and spermatogenesis require
RT MitoPLD profusogenic mitochondrial-surface lipid signaling.";
RL Dev. Cell 20:376-387(2011).
RN [13]
RP INTERACTION WITH MIGA.
RX PubMed=26711011; DOI=10.1016/j.molcel.2015.11.017;
RA Zhang Y., Liu X., Bai J., Tian X., Zhao X., Liu W., Duan X., Shang W.,
RA Fan H.Y., Tong C.;
RT "Mitoguardin regulates mitochondrial fusion through MitoPLD and is required
RT for neuronal homeostasis.";
RL Mol. Cell 61:111-124(2016).
CC -!- FUNCTION: Cardiolipin hydrolase present at the mitochondrial outer
CC membrane required for piRNA metabolic process. Acts by catalyzing the
CC hydrolysis of cardiolipin (diphosphatidylglycerol) to form
CC phosphatidate (phosphatidic acid or PA) at the mitochondrial outer
CC membrane surface, promoting the piRNA metabolic process. Plays a key
CC role in primary biogenesis of piRNAs and is required during oogenesis
CC to repress transposable elements and prevent their mobilization. piRNAs
CC mediate the repression of transposable elements during meiosis by
CC forming complexes composed of piRNAs and Piwi proteins and govern the
CC methylation and subsequent repression of transposons. Involved in
CC trans-silencing effect (TSE), a homology-dependent repression mechanism
CC by which a P-transgene inserted in subtelomeric heterochromatin via its
CC role in piRNA biogenesis. {ECO:0000269|PubMed:17543859,
CC ECO:0000269|PubMed:19812547, ECO:0000269|PubMed:20559422,
CC ECO:0000269|PubMed:20818334, ECO:0000269|PubMed:20966047,
CC ECO:0000269|PubMed:20966049, ECO:0000269|PubMed:21397848}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with miga/CG12125
CC (PubMed:26711011). {ECO:0000250|UniProtKB:Q5SWZ9,
CC ECO:0000269|PubMed:26711011}.
CC -!- INTERACTION:
CC Q9VKD7; Q9W3F7: Miga; NbExp=2; IntAct=EBI-9943000, EBI-184365;
CC Q9VKD7; Q9VKD7: zuc; NbExp=3; IntAct=EBI-9943000, EBI-9943000;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:20966047, ECO:0000269|PubMed:21397848}; Single-pass
CC membrane protein {ECO:0000269|PubMed:20966047,
CC ECO:0000269|PubMed:21397848}. Note=Was initially reported to localize
CC to the meiotic nuage, also named P granule (PubMed:17543859). However,
CC it was later shown that the EGFP tag at N-terminus used in initial
CC experiments interfered with mitochondrial localization (PubMed:21397848
CC and PubMed:20966047). {ECO:0000269|PubMed:17543859}.
CC -!- DOMAIN: In contrast to other members of the phospholipase D family,
CC contains only one PLD phosphodiesterase domain, suggesting that it has
CC a single half-catalytic and requires homodimerization to form a
CC complete active site. {ECO:0000250|UniProtKB:Q8N2A8}.
CC -!- DISRUPTION PHENOTYPE: Defects in mid oogenesis. Females are viable but
CC produce eggs with a range of dorso-ventral patterning defects. Flies
CC lay few eggs, all of which are completely ventralized and often
CC collapsed. Effects are due to defects in piRNA biogenesis and
CC derepression of retrotransposons. Defects are not only present in germ
CC cells but also in somatic cells of the ovary.
CC {ECO:0000269|PubMed:17543859}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. MitoPLD/Zucchini
CC subfamily. {ECO:0000305}.
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DR EMBL; AM294430; CAL26369.1; -; Genomic_DNA.
DR EMBL; AM294431; CAL26370.1; -; Genomic_DNA.
DR EMBL; AM294432; CAL26371.1; -; Genomic_DNA.
DR EMBL; AM294433; CAL26372.1; -; Genomic_DNA.
DR EMBL; AM294434; CAL26373.1; -; Genomic_DNA.
DR EMBL; AM294435; CAL26374.1; -; Genomic_DNA.
DR EMBL; AM294436; CAL26375.1; -; Genomic_DNA.
DR EMBL; AM294437; CAL26377.1; -; Genomic_DNA.
DR EMBL; AM294438; CAL26381.1; -; Genomic_DNA.
DR EMBL; AM294439; CAL26382.1; -; Genomic_DNA.
DR EMBL; AM294440; CAL26383.1; -; Genomic_DNA.
DR EMBL; FM245502; CAR93428.1; -; Genomic_DNA.
DR EMBL; FM245503; CAR93429.1; -; Genomic_DNA.
DR EMBL; FM245504; CAR93430.1; -; Genomic_DNA.
DR EMBL; FM245505; CAR93431.1; -; Genomic_DNA.
DR EMBL; FM245506; CAR93432.1; -; Genomic_DNA.
DR EMBL; FM245507; CAR93433.1; -; Genomic_DNA.
DR EMBL; FM245508; CAR93434.1; -; Genomic_DNA.
DR EMBL; FM245509; CAR93435.1; -; Genomic_DNA.
DR EMBL; FM245510; CAR93436.1; -; Genomic_DNA.
DR EMBL; FM245511; CAR93437.1; -; Genomic_DNA.
DR EMBL; FM245512; CAR93438.1; -; Genomic_DNA.
DR EMBL; FM245513; CAR93439.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53139.1; -; Genomic_DNA.
DR EMBL; AY118493; AAM49862.1; -; mRNA.
DR RefSeq; NP_609530.1; NM_135686.3.
DR PDB; 4GEL; X-ray; 1.76 A; A/B=41-253.
DR PDB; 4GEM; X-ray; 2.21 A; A/B=41-253.
DR PDB; 4GEN; X-ray; 2.20 A; A=89-250.
DR PDB; 4H4A; X-ray; 2.20 A; A=89-253.
DR PDBsum; 4GEL; -.
DR PDBsum; 4GEM; -.
DR PDBsum; 4GEN; -.
DR PDBsum; 4H4A; -.
DR AlphaFoldDB; Q9VKD7; -.
DR SMR; Q9VKD7; -.
DR BioGRID; 60662; 7.
DR DIP; DIP-59983N; -.
DR IntAct; Q9VKD7; 2.
DR STRING; 7227.FBpp0079900; -.
DR PaxDb; Q9VKD7; -.
DR DNASU; 34609; -.
DR EnsemblMetazoa; FBtr0080316; FBpp0079900; FBgn0261266.
DR GeneID; 34609; -.
DR KEGG; dme:Dmel_CG12314; -.
DR UCSC; CG12314-RA; d. melanogaster.
DR CTD; 34609; -.
DR FlyBase; FBgn0261266; zuc.
DR VEuPathDB; VectorBase:FBgn0261266; -.
DR eggNOG; ENOG502RXG9; Eukaryota.
DR GeneTree; ENSGT00390000004368; -.
DR HOGENOM; CLU_080814_0_1_1; -.
DR InParanoid; Q9VKD7; -.
DR OMA; QPFIKEF; -.
DR OrthoDB; 1489926at2759; -.
DR PhylomeDB; Q9VKD7; -.
DR Reactome; R-DME-1483166; Synthesis of PA.
DR BioGRID-ORCS; 34609; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34609; -.
DR PRO; PR:Q9VKD7; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0261266; Expressed in gastrula and 21 other tissues.
DR ExpressionAtlas; Q9VKD7; baseline and differential.
DR Genevisible; Q9VKD7; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:0035755; F:cardiolipin hydrolase activity; IDA:UniProtKB.
DR GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046843; P:dorsal appendage formation; HMP:FlyBase.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:FlyBase.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; HMP:FlyBase.
DR GO; GO:1990511; P:piRNA biosynthetic process; IMP:FlyBase.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:FlyBase.
DR InterPro; IPR025202; PLD-like_dom.
DR Pfam; PF13091; PLDc_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Differentiation; Hydrolase; Lipid degradation;
KW Lipid metabolism; Meiosis; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Oogenesis; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..253
FT /note="Mitochondrial cardiolipin hydrolase"
FT /id="PRO_0000408335"
FT TOPO_DOM 1..13
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 164..211
FT /note="PLD phosphodiesterase"
FT ACT_SITE 169
FT /evidence="ECO:0000305"
FT ACT_SITE 171
FT /evidence="ECO:0000255"
FT ACT_SITE 176
FT /evidence="ECO:0000255"
FT VARIANT 2
FT /note="L -> V (in strain: MEL20, ZBMEL131, ZBMEL186,
FT ZBMEL384 and ZBMEL398)"
FT VARIANT 225
FT /note="D -> E (in strain: =MEL01, MEL02, MEL11, MEL12,
FT MEL14, MEL15, MEL16, MEL17, MEL18, MEL19, MEL20, ZBMEL82,
FT ZBMEL95, ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191,
FT ZBMEL229, ZBMEL377, ZBMEL384 and ZBMEL398)"
FT VARIANT 252
FT /note="L -> V (in strain: ZBMEL191, ZBMEL229, ZBMEL377 and
FT ZBMEL384)"
FT MUTAGEN 47
FT /note="A->D: In zuc(RS49); produce some eggs with a more
FT normal eggshell phenotype in addition to the ventralized
FT eggs compared to null mutants."
FT /evidence="ECO:0000269|PubMed:17543859"
FT MUTAGEN 169
FT /note="H->N: Abolishes cardiolipin hydrolase activity."
FT /evidence="ECO:0000269|PubMed:17543859,
FT ECO:0000269|PubMed:21397848"
FT MUTAGEN 169
FT /note="H->Y: In zuc(SG63); produce some eggs with a more
FT normal eggshell phenotype in addition to the ventralized
FT eggs compared to null mutants."
FT /evidence="ECO:0000269|PubMed:17543859,
FT ECO:0000269|PubMed:21397848"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:4GEL"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4GEL"
FT TURN 58..63
FT /evidence="ECO:0007829|PDB:4GEL"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:4GEL"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:4GEL"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:4GEL"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:4GEL"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:4GEL"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:4GEL"
FT TURN 139..143
FT /evidence="ECO:0007829|PDB:4GEL"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:4GEL"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:4GEL"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4GEL"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:4GEL"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:4GEL"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:4GEL"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:4GEL"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:4GEL"
FT HELIX 225..241
FT /evidence="ECO:0007829|PDB:4GEL"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:4GEL"
SQ SEQUENCE 253 AA; 28520 MW; 4488BEA6DFF9E092 CRC64;
MLITQIIMKQ IRDYPIVSTI SIAVSTVLAS EVIWKLVQCS RSKREKASRV HEVIIFNELG
EICAAVHMRN SSMGSQKPQV SPCCNTHCSL RNVAKIVEQI DRAVYSIDLA IYTFTSLFLA
DSIKRALQRG VIIRIISDGE MVYSKGSQIS MLAQLGVPVR VPITTNLMHN KFCIIDGFER
VEEIRLLRKL KFMRPCYSIV ISGSVNWTAL GLGGNWENCI ITADDKLTAT FQAEFQRMWR
AFAKTEGSQI QLK
