PGL1_CAEEL
ID PGL1_CAEEL Reviewed; 730 AA.
AC Q9TZQ3;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Guanyl-specific ribonuclease pgl-1 {ECO:0000305};
DE EC=4.6.1.24 {ECO:0000269|PubMed:26787882};
DE AltName: Full=P granule abnormality protein 1;
GN Name=pgl-1 {ECO:0000312|WormBase:ZK381.4a};
GN ORFNames=ZK381.4 {ECO:0000312|WormBase:ZK381.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:9741628};
RX PubMed=9741628; DOI=10.1016/s0092-8674(00)81605-0;
RA Kawasaki I., Shim Y.-H., Kirchner J., Kaminker J., Wood W.B., Strome S.;
RT "pgl-1, a predicted RNA-binding component of germ granules, is essential
RT for fertility in C. elegans.";
RL Cell 94:635-645(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP INTERACTION WITH IFE-1.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:11641215};
RX PubMed=11641215; DOI=10.1242/dev.128.20.3899;
RA Amiri A., Keiper B.D., Kawasaki I., Fan Y., Kohara Y., Rhoads R.E.,
RA Strome S.;
RT "An isoform of eIF4E is a component of germ granules and is required for
RT spermatogenesis in C. elegans.";
RL Development 128:3899-3912(2001).
RN [4]
RP FUNCTION, SUBUNIT, INTERACTION WITH PGL-2 AND PGL-3, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15238518; DOI=10.1534/genetics.103.023093;
RA Kawasaki I., Amiri A., Fan Y., Meyer N., Dunkelbarger S., Motohashi T.,
RA Karashima T., Bossinger O., Strome S.;
RT "The PGL family proteins associate with germ granules and function
RT redundantly in Caenorhabditis elegans germline development.";
RL Genetics 167:645-661(2004).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=19377305; DOI=10.4161/auto.5.5.8624;
RA Tian E., Wang F., Han J., Zhang H.;
RT "epg-1 functions in autophagy-regulated processes and may encode a highly
RT divergent Atg13 homolog in C. elegans.";
RL Autophagy 5:608-615(2009).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19167332; DOI=10.1016/j.cell.2008.12.022;
RA Zhang Y., Yan L., Zhou Z., Yang P., Tian E., Zhang K., Zhao Y., Li Z.,
RA Song B., Han J., Miao L., Zhang H.;
RT "SEPA-1 mediates the specific recognition and degradation of P granule
RT components by autophagy in C. elegans.";
RL Cell 136:308-321(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=21402787; DOI=10.1083/jcb.201010106;
RA Hanazawa M., Yonetani M., Sugimoto A.;
RT "PGL proteins self associate and bind RNPs to mediate germ granule assembly
RT in C. elegans.";
RL J. Cell Biol. 192:929-937(2011).
RN [8]
RP INTERACTION WITH PRMT-1, SUBCELLULAR LOCATION, AND METHYLATION.
RX PubMed=24140420; DOI=10.1016/j.molcel.2013.09.014;
RA Li S., Yang P., Tian E., Zhang H.;
RT "Arginine methylation modulates autophagic degradation of PGL granules in
RT C. elegans.";
RL Mol. Cell 52:421-433(2013).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24746798; DOI=10.1016/j.cub.2014.03.015;
RA Updike D.L., Knutson A.K., Egelhofer T.A., Campbell A.C., Strome S.;
RT "Germ-granule components prevent somatic development in the C. elegans
RT germline.";
RL Curr. Biol. 24:970-975(2014).
RN [10]
RP INTERACTION WITH MEG-1; MEG-3 AND MEG-4.
RX PubMed=25535836; DOI=10.7554/elife.04591;
RA Wang J.T., Smith J., Chen B.C., Schmidt H., Rasoloson D., Paix A.,
RA Lambrus B.G., Calidas D., Betzig E., Seydoux G.;
RT "Regulation of RNA granule dynamics by phosphorylation of serine-rich,
RT intrinsically disordered proteins in C. elegans.";
RL Elife 3:e04591-e04591(2014).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26598553; DOI=10.1242/jcs.174201;
RA Min H., Shim Y.H., Kawasaki I.;
RT "Loss of PGL-1 and PGL-3, members of a family of constitutive germ-granule
RT components, promotes germline apoptosis in C. elegans.";
RL J. Cell Sci. 129:341-353(2016).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=27650246; DOI=10.1038/srep33884;
RA Al-Amin M., Min H., Shim Y.H., Kawasaki I.;
RT "Somatically expressed germ-granule components, PGL-1 and PGL-3, repress
RT programmed cell death in C. elegans.";
RL Sci. Rep. 6:33884-33884(2016).
RN [13]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=28806108; DOI=10.1080/15548627.2017.1339843;
RA Zhang G., Lin L., Qi D., Zhang H.;
RT "The composition of a protein aggregate modulates the specificity and
RT efficiency of its autophagic degradation.";
RL Autophagy 13:1487-1495(2017).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 205-447, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVE SITE, COFACTOR, ACTIVITY REGULATION, SUBUNIT, DOMAIN,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLN-301; GLU-401 AND HIS-437.
RX PubMed=26787882; DOI=10.1073/pnas.1524400113;
RA Aoki S.T., Kershner A.M., Bingman C.A., Wickens M., Kimble J.;
RT "PGL germ granule assembly protein is a base-specific, single-stranded
RT RNase.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:1279-1284(2016).
RN [15]
RP INTERACTION WITH NMAD-1.
RX PubMed=31283754; DOI=10.1371/journal.pgen.1008252;
RA Wang S.Y., Mao H., Shibuya H., Uzawa S., O'Brown Z.K., Wesenberg S.,
RA Shin N., Saito T.T., Gao J., Meyer B.J., Colaiacovo M.P., Greer E.L.;
RT "The demethylase NMAD-1 regulates DNA replication and repair in the
RT Caenorhabditis elegans germline.";
RL PLoS Genet. 15:E1008252-E1008252(2019).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=32843637; DOI=10.1038/s41467-020-18089-1;
RA Suen K.M., Braukmann F., Butler R., Bensaddek D., Akay A., Lin C.C.,
RA Milonaityte D., Doshi N., Sapetschnig A., Lamond A., Ladbury J.E.,
RA Miska E.A.;
RT "DEPS-1 is required for piRNA-dependent silencing and PIWI condensate
RT organisation in Caenorhabditis elegans.";
RL Nat. Commun. 11:4242-4242(2020).
CC -!- FUNCTION: Guanyl-specific endoribonuclease which cleaves the
CC phosphodiester bond in single-stranded RNA between the 3'-guanylic
CC residue and the 5'-OH residue of adjacent nucleotide, resulting in the
CC formation of a corresponding 2',3'-cyclic phosphate intermediate
CC (PubMed:26787882). Together with the P-granule component pgl-3, is
CC involved in the formation of P-granules (PubMed:21402787,
CC PubMed:24746798). Together with pgl-3, probably recruits other granule
CC components such as pos-1, mex-3 and glh-1 to P-granules
CC (PubMed:21402787). In addition, may act redundantly with pgl-3 to
CC protect germ cells from excessive germline apoptosis during normal
CC oogenesis and development of the two gonadal arms (PubMed:26598553).
CC This may in part be through regulating the localization of sir-2.1
CC which is involved in germ cell apoptosis (PubMed:26598553). May protect
CC somatic cells from excessive apoptosis during normal development
CC (PubMed:27650246). Essential role in male and female postembryonic
CC germline development; maternally provided protein maintains a
CC population of proliferating germ cells and zygotic expression is
CC required for correct oogenesis (PubMed:9741628, PubMed:15238518,
CC PubMed:24746798). {ECO:0000269|PubMed:15238518,
CC ECO:0000269|PubMed:21402787, ECO:0000269|PubMed:24746798,
CC ECO:0000269|PubMed:26598553, ECO:0000269|PubMed:26787882,
CC ECO:0000269|PubMed:27650246, ECO:0000269|PubMed:9741628}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[RNA] containing guanosine + H2O = an [RNA fragment]-3'-
CC guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA
CC fragment].; EC=4.6.1.24; Evidence={ECO:0000269|PubMed:26787882};
CC -!- COFACTOR:
CC Note=Does not require metal ions for catalytic activity.
CC {ECO:0000269|PubMed:26787882};
CC -!- ACTIVITY REGULATION: Not inhibited by RNase inhibitor RNasin.
CC {ECO:0000269|PubMed:26787882}.
CC -!- SUBUNIT: Homodimer (PubMed:15238518, PubMed:26787882). Interacts with
CC pgl-2 and pgl-3; this association is not required for P-granule
CC localization of either pgl-2 or pgl-3 (PubMed:15238518). Interacts with
CC ife-1 (PubMed:11641215, PubMed:15238518). Interacts with prmt-1; the
CC interaction is direct (PubMed:24140420). Interacts with nmad-1
CC (PubMed:31283754). Interacts with P granule components meg-1, meg-3 and
CC meg-4 (PubMed:25535836). {ECO:0000269|PubMed:11641215,
CC ECO:0000269|PubMed:15238518, ECO:0000269|PubMed:24140420,
CC ECO:0000269|PubMed:25535836, ECO:0000269|PubMed:26787882,
CC ECO:0000269|PubMed:31283754}.
CC -!- INTERACTION:
CC Q9TZQ3; O45551: ife-1; NbExp=2; IntAct=EBI-332200, EBI-330148;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:15238518,
CC ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:21402787,
CC ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:26598553,
CC ECO:0000269|PubMed:27650246, ECO:0000269|PubMed:28806108,
CC ECO:0000269|PubMed:32843637, ECO:0000269|PubMed:9741628}.
CC Note=Localizes to P granules in germline precursor cells
CC (PubMed:9741628, PubMed:19167332, PubMed:24140420, PubMed:27650246,
CC PubMed:28806108). Localizes to P granules in germ cells at all stages
CC of development except in spermatogenesis (PubMed:15238518). Co-
CC localizes with pgl-3 in P-granules, but localization in P-granules is
CC not dependent on an association with pgl-3 (PubMed:15238518,
CC PubMed:21402787). At P-granules in the adult germline, co-localizes
CC with deps-1 in the pachytene region and with prg-1 (PubMed:32843637).
CC {ECO:0000269|PubMed:15238518, ECO:0000269|PubMed:19167332,
CC ECO:0000269|PubMed:21402787, ECO:0000269|PubMed:24140420,
CC ECO:0000269|PubMed:27650246, ECO:0000269|PubMed:32843637,
CC ECO:0000269|PubMed:9741628}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline (PubMed:9741628,
CC PubMed:15238518). Expressed in most somatic cells (PubMed:27650246).
CC {ECO:0000269|PubMed:15238518, ECO:0000269|PubMed:27650246,
CC ECO:0000269|PubMed:9741628}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development from embryos to
CC adults (PubMed:9741628, PubMed:15238518, PubMed:27650246). Not
CC expressed in somatic cells of embryos (PubMed:28806108). First
CC expressed in 1-cell embryos, and expression persists until the 4-cell
CC stage (PubMed:15238518). Expression diminishes in somatic blastomeres,
CC but remains in E and P3 blastomeres at the 8-cell stage, in P3
CC blastomeres at the 15-cell stage, and in P4 blastomeres at the 24-cell
CC stage (PubMed:15238518). Expressed in the primordial germ cells Z2 and
CC Z3 during the two-fold stage of embryogenesis (PubMed:15238518,
CC PubMed:27650246). Levels are low in young larvae but increase at the
CC end of larval development (PubMed:9741628). Expressed in germ
CC blastomeres (PubMed:19377305). {ECO:0000269|PubMed:15238518,
CC ECO:0000269|PubMed:19377305, ECO:0000269|PubMed:27650246,
CC ECO:0000269|PubMed:28806108, ECO:0000269|PubMed:9741628}.
CC -!- DOMAIN: The dimerization domain also acts as a hinge; changes in its
CC structure probably impact oligomerization and RNA-binding.
CC {ECO:0000305|PubMed:26787882}.
CC -!- DOMAIN: The RNA-binding RGG-box is required for the recruitment of some
CC P-granule components such as pos-1 and probably mRNA, but is
CC dispensable for granule formation. {ECO:0000269|PubMed:21402787,
CC ECO:0000305|PubMed:9741628}.
CC -!- PTM: Methylated at arginine residues in the RNA-binding RGG-box by
CC prmt-1. Methylation promotes P-granule degradation by autophagy.
CC {ECO:0000269|PubMed:24140420}.
CC -!- DISRUPTION PHENOTYPE: Temperature-sensitive and are only fertile at 20
CC degrees Celsius (PubMed:26787882). 25% of progeny arresting as late
CC embryos and 9% as larvae at 26 degrees Celsius (PubMed:15238518).
CC Surviving progeny are sterile at 26 degrees Celsius, most likely due to
CC germline proliferation defects (PubMed:9741628, PubMed:15238518,
CC PubMed:26787882). The temperature-sensitive period extends from mid-
CC larvae to young adults (PubMed:9741628). Germline defects include
CC increased apoptosis in the gonad, fewer germ nuclei, no sperm and no
CC oocytes in the gonad arms (PubMed:15238518, PubMed:26598553). Double
CC knockout with pgl-3 results in 37% of progeny arresting as late embryos
CC and 9% as larvae at 26 degrees Celsius (PubMed:15238518). Double
CC knockout with pgl-3 enhances the temperature-sensitive sterility
CC phenotype and germline defects of the pgl-1 single knockout
CC (PubMed:15238518, PubMed:26598553). The gonads of the double knockout
CC with pgl-3 degenerate as the adults age (PubMed:15238518). Triple
CC knockout with pgl-2 and pgl-3 results in 58% of progeny arresting as
CC late embryos and 5% as larvae at 26 degrees Celsius (PubMed:15238518).
CC Double knockout with him-3 decreases the number of self-cross progeny
CC in the him-3 single mutant (PubMed:15238518). Triple knockout with pgl-
CC 3 and him-3 further reduces the number of self-cross progeny as
CC compared to the pgl-1 and him-3 double mutant and him-3 single mutant
CC (PubMed:15238518). Double knockout with ced-1 results in an increased
CC number of cell corpses in the gonad as compared to the ced-1 single
CC mutant (PubMed:26598553). Conversely, double knockout with ced-1
CC results in reduced somatic cell apoptosis (PubMed:27650246). Triple
CC knockout with ced-1 and hpl-2 partially recovers the reduced somatic
CC cell apoptotic cell defect in the ced-1 and hpl-2 double knockout
CC (PubMed:27650246). Triple knockout with ced-1 and hpl-2 and knockdown
CC with either ced-3 or ced-4 reduces the somatic cell apoptosis defect in
CC the ced-1, hpl-2 and pgl-1 triple knockout (PubMed:27650246). Double
CC RNAi-mediated knockdown with pgl-1 results in a reduced number of pos-
CC 1, mex-1 and glh-1 positive granules in embryos (PubMed:21402787).
CC Quadruple RNAi-mediated knockdown with glh-1, glh-4 and pgl-3 results
CC in offspring that display 27-89% sterility, abnormal oocytes and do not
CC have embryos in the uterus (PubMed:24746798). These sterile offspring
CC still produce sperm (PubMed:24746798). Furthermore, these offspring may
CC have compromised P-granule integrity as there is diffuse cytoplasmic
CC localization of the P-granule component deps-1, which may cause germ
CC cells to initiate somatic reprogramming (PubMed:24746798). RNAi-
CC mediated knockdown in a double ced-1 and hpl-2 mutant background
CC rescues the reduced somatic cell apoptotic cell defect in the ced-1 and
CC hpl-2 double knockout (PubMed:27650246). {ECO:0000269|PubMed:15238518,
CC ECO:0000269|PubMed:21402787, ECO:0000269|PubMed:24746798,
CC ECO:0000269|PubMed:26598553, ECO:0000269|PubMed:26787882,
CC ECO:0000269|PubMed:27650246, ECO:0000269|PubMed:9741628}.
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DR EMBL; AF077868; AAC36100.1; -; mRNA.
DR EMBL; BX284604; CCD62010.1; -; Genomic_DNA.
DR PIR; T43317; T43317.
DR RefSeq; NP_001041065.1; NM_001047600.3.
DR PDB; 5CV1; X-ray; 3.60 A; A=205-447.
DR PDBsum; 5CV1; -.
DR AlphaFoldDB; Q9TZQ3; -.
DR SMR; Q9TZQ3; -.
DR BioGRID; 42581; 14.
DR DIP; DIP-26042N; -.
DR IntAct; Q9TZQ3; 2.
DR STRING; 6239.ZK381.4b; -.
DR EPD; Q9TZQ3; -.
DR PaxDb; Q9TZQ3; -.
DR EnsemblMetazoa; ZK381.4a.1; ZK381.4a.1; WBGene00003992.
DR EnsemblMetazoa; ZK381.4a.2; ZK381.4a.2; WBGene00003992.
DR UCSC; ZK381.4a.1; c. elegans.
DR WormBase; ZK381.4a; CE25689; WBGene00003992; pgl-1.
DR eggNOG; ENOG502QVYU; Eukaryota.
DR GeneTree; ENSGT00970000196090; -.
DR HOGENOM; CLU_362575_0_0_1; -.
DR InParanoid; Q9TZQ3; -.
DR PRO; PR:Q9TZQ3; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003992; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; Q9TZQ3; baseline and differential.
DR GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR GO; GO:0032797; C:SMN complex; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:WormBase.
DR GO; GO:0042802; F:identical protein binding; IPI:WormBase.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IPI:WormBase.
DR GO; GO:0046589; F:ribonuclease T1 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; ISS:WormBase.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0007276; P:gamete generation; IMP:WormBase.
DR GO; GO:0042078; P:germ-line stem cell division; IMP:WormBase.
DR GO; GO:0048477; P:oogenesis; IMP:WormBase.
DR GO; GO:0030719; P:P granule organization; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:WormBase.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IBA:GO_Central.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Differentiation; Endonuclease;
KW Hydrolase; Lyase; Methylation; Nuclease; Oogenesis; Reference proteome;
KW Repeat; RNA-binding.
FT CHAIN 1..730
FT /note="Guanyl-specific ribonuclease pgl-1"
FT /id="PRO_0000058357"
FT REGION 205..447
FT /note="Involved in dimerization"
FT /evidence="ECO:0000269|PubMed:26787882"
FT REGION 452..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..730
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000305|PubMed:9741628"
FT REGION 686..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 437
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:26787882"
FT MUTAGEN 301
FT /note="Q->A: Abolished catalytic activity. No effect on
FT dimerization or RNA-binding."
FT /evidence="ECO:0000269|PubMed:26787882"
FT MUTAGEN 401
FT /note="E->Q: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:26787882"
FT MUTAGEN 437
FT /note="H->A: Reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:26787882"
SQ SEQUENCE 730 AA; 78454 MW; 779FFC6180376D7A CRC64;
MEANKREIVD FGGLRSYFFP NLAHYITKND EELFNNTSQA NKLAAFVLGA SKDAPGDEDI
LEMILPNDAN AAVIAAGMDV CLLLGDKFRP KFDAAAEKLS GLGHAHDLVS VIDDDKKLGM
LARKAKLKKT EDAKILQALL KVIAIDDAAE KFVELTELVS QLDLDFDVYV LTKILGLISE
ETSDEVDIIR DNVVNAFDSC KPLLKQLMLD GPKSEPADPF ISLLMDPLEE SVGKVVNHIA
QLFEEASKNE GDESLVLRSQ LGYQLFFLIV RSLADGKREV SKKILSGIPT SVRAEVFPGL
QRSVYKSAVF LGNHIIQVLL GSKKSFEDWD VVGVAKDLES AWKRRAIAEL IKKFQVSILE
QCFDKPVPLI PQSPLNNDAV IDNVNKALQF ALWLTEFYGS ENETEALGEL RFLDSTSKNL
LVDSFKKFVQ GINSKTHVTR IVESLEKCCL SDTPSGRKSN VQPSTSQQQD SAYTKEEMTT
VHNTYSVNTK AQVLNGLSDT NSSGLLVDSK DSLSLQEISC DEVDSSTLLS SSRNIGEGVT
VKAVDPVPEK VNDAQQQQTV NEIEMASDAN QDTSSSASPE VAPSFSTDGW DSPTKSVALP
PGMQQIDEEE TTVADKDSTP QPQARAETAW GSGDATPMPL PAPTNQYKVS GFGEAKVAKG
FGQFAPTSSA YGGGGGRGGY GGGDRGGRGG YGGDRGGRGG YGGGDRGGRG GYGGDRGRGG
YGGRGGRGGF
