ANM5_CAEEL
ID ANM5_CAEEL Reviewed; 734 AA.
AC P46580; Q8T8N5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein arginine N-methyltransferase 5 {ECO:0000303|PubMed:19521535};
DE EC=2.1.1.320 {ECO:0000269|PubMed:21531333, ECO:0000269|PubMed:23866019};
GN Name=prmt-5 {ECO:0000312|WormBase:C34E10.5};
GN Synonyms=tag-251 {ECO:0000312|WormBase:C34E10.5};
GN ORFNames=C34E10.5 {ECO:0000312|WormBase:C34E10.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CEP-1 AND CBP-1, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19521535; DOI=10.1371/journal.pgen.1000514;
RA Yang M., Sun J., Sun X., Shen Q., Gao Z., Yang C.;
RT "Caenorhabditis elegans protein arginine methyltransferase PRMT-5
RT negatively regulates DNA damage-induced apoptosis.";
RL PLoS Genet. 5:E1000514-E1000514(2009).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21531333; DOI=10.1016/j.cmet.2011.03.017;
RA Takahashi Y., Daitoku H., Hirota K., Tamiya H., Yokoyama A., Kako K.,
RA Nagashima Y., Nakamura A., Shimada T., Watanabe S., Yamagata K., Yasuda K.,
RA Ishii N., Fukamizu A.;
RT "Asymmetric arginine dimethylation determines life span in C. elegans by
RT regulating forkhead transcription factor DAF-16.";
RL Cell Metab. 13:505-516(2011).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=23866019; DOI=10.1021/bi4005123;
RA Wang M., Xu R.M., Thompson P.R.;
RT "Substrate specificity, processivity, and kinetic mechanism of protein
RT arginine methyltransferase 5.";
RL Biochemistry 52:5430-5440(2013).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28158808; DOI=10.1093/jb/mvw101;
RA Hirota K., Shigekawa C., Araoi S., Sha L., Inagawa T., Kanou A., Kako K.,
RA Daitoku H., Fukamizu A.;
RT "Simultaneous ablation of prmt-1 and prmt-5 abolishes asymmetric and
RT symmetric arginine dimethylations in Caenorhabditis elegans.";
RL J. Biochem. 161:521-527(2017).
RN [6]
RP INTERACTION WITH PID-2; PID-4 AND PID-5.
RX PubMed=33231880; DOI=10.15252/embj.2020105280;
RA Placentino M., de Jesus Domingues A.M., Schreier J., Dietz S., Hellmann S.,
RA de Albuquerque B.F., Butter F., Ketting R.F.;
RT "Intrinsically disordered protein PID-2 modulates Z granules and is
RT required for heritable piRNA-induced silencing in the Caenorhabditis
RT elegans embryo.";
RL EMBO J. 40:e105280-e105280(2021).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVE SITE, SUBUNIT, AND MUTAGENESIS OF PHE-379.
RX PubMed=22143770; DOI=10.1073/pnas.1106946108;
RA Sun L., Wang M., Lv Z., Yang N., Liu Y., Bao S., Gong W., Xu R.M.;
RT "Structural insights into protein arginine symmetric dimethylation by
RT PRMT5.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20538-20543(2011).
CC -!- FUNCTION: Catalyzes the symmetrical dimethylation of arginine residues
CC in targets such as small nuclear ribonucleoproteins, histone H2A/H4 and
CC cbp-1 (PubMed:19521535, PubMed:21531333, PubMed:23866019,
CC PubMed:22143770, PubMed:28158808). Dimethylation occurs in a
CC distributive manner where the protein is released after the addition of
CC the first methyl group prior to rebinding for the addition of the
CC second methyl group (PubMed:23866019). Plays a role in the negative
CC regulation of DNA damage-induced apoptosis (PubMed:19521535). By
CC methylating cbp-1, may prevent apoptosis by repressing the capacity of
CC cbp-1 to enhance cep-1 dependent transcription activation of the
CC programmed cell death activator egl-1 (PubMed:19521535). Plays a role
CC in heat and oxidative stress resistance (PubMed:28158808).
CC {ECO:0000269|PubMed:19521535, ECO:0000269|PubMed:21531333,
CC ECO:0000269|PubMed:22143770, ECO:0000269|PubMed:23866019,
CC ECO:0000269|PubMed:28158808, ECO:0000303|PubMed:19521535}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320;
CC Evidence={ECO:0000269|PubMed:21531333, ECO:0000269|PubMed:23866019};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.5 uM for histone H4 (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:22143770};
CC KM=22 uM for histone H4 (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:23866019};
CC Vmax=1.4 nmol/min/mg enzyme with histone H4 as substrate
CC {ECO:0000269|PubMed:22143770};
CC Temperature dependence:
CC Optimum temperature is about 25 degrees Celsius.
CC {ECO:0000269|PubMed:23866019};
CC -!- SUBUNIT: Homodimer (PubMed:22143770). Interacts with cep-1 (via C-
CC terminus domain); does not methylate cep-1 (PubMed:19521535). Interacts
CC with cbp-1 (via N-terminus domain and HAT domain); the interaction
CC results in methylation of cbp-1 (PubMed:19521535). Component of a
CC complex that contains cep-1 and cbp-1 (PubMed:19521535). May interact
CC with pid-2, pid-4 and pid-5 (PubMed:33231880).
CC {ECO:0000269|PubMed:19521535, ECO:0000269|PubMed:22143770,
CC ECO:0000269|PubMed:33231880}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19521535}.
CC -!- DISRUPTION PHENOTYPE: Defective arginine methyltransferase activity
CC with reduced symmetric dimethylation of targets (PubMed:28158808).
CC Increased sensitivity to heat and oxidative stress (PubMed:28158808).
CC Increased germ cell apoptosis following treatment with ionizing
CC radiation (IR) or ethylnitrosourea and significantly enhanced IR-
CC induced egl-1 levels (PubMed:19521535). Double knockout with prmt-1
CC results in prolonged larval development, shorter body size, reduced
CC brood size, decreased egg-laying and 30% of eggs fail to hatch
CC (PubMed:28158808). Double knockout also results in reduced asymmetric
CC and symmetric arginine dimethylation of proteins (PubMed:28158808).
CC {ECO:0000269|PubMed:19521535, ECO:0000269|PubMed:28158808}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR EMBL; BX284603; CCD66649.1; -; Genomic_DNA.
DR PIR; T15762; T15762.
DR RefSeq; NP_498112.1; NM_065711.6.
DR PDB; 3UA3; X-ray; 3.00 A; A/B=1-734.
DR PDB; 3UA4; X-ray; 3.00 A; A/B=1-734.
DR PDBsum; 3UA3; -.
DR PDBsum; 3UA4; -.
DR AlphaFoldDB; P46580; -.
DR SMR; P46580; -.
DR BioGRID; 40948; 19.
DR ComplexPortal; CPX-1131; Prmt-5-cep-1-cbp-1 complex.
DR DIP; DIP-25435N; -.
DR IntAct; P46580; 2.
DR STRING; 6239.C34E10.5.3; -.
DR iPTMnet; P46580; -.
DR EPD; P46580; -.
DR PaxDb; P46580; -.
DR PeptideAtlas; P46580; -.
DR EnsemblMetazoa; C34E10.5.1; C34E10.5.1; WBGene00016408.
DR EnsemblMetazoa; C34E10.5.2; C34E10.5.2; WBGene00016408.
DR EnsemblMetazoa; C34E10.5.3; C34E10.5.3; WBGene00016408.
DR GeneID; 175717; -.
DR KEGG; cel:CELE_C34E10.5; -.
DR UCSC; C34E10.5.3; c. elegans.
DR CTD; 175717; -.
DR WormBase; C34E10.5; CE29033; WBGene00016408; prmt-5.
DR eggNOG; KOG0822; Eukaryota.
DR GeneTree; ENSGT00390000001141; -.
DR HOGENOM; CLU_010247_3_0_1; -.
DR InParanoid; P46580; -.
DR OMA; IKYAWYE; -.
DR OrthoDB; 475852at2759; -.
DR PhylomeDB; P46580; -.
DR BRENDA; 2.1.1.320; 1045.
DR SignaLink; P46580; -.
DR PRO; PR:P46580; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00016408; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0017053; C:transcription repressor complex; IPI:ComplexPortal.
DR GO; GO:0016277; F:[myelin basic protein]-arginine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); IDA:WormBase.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:WormBase.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:WormBase.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:UniProtKB.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034969; P:histone arginine methylation; IDA:WormBase.
DR GO; GO:0043985; P:histone H4-R3 methylation; IDA:WormBase.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:WormBase.
DR GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IGI:WormBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:WormBase.
DR GO; GO:0019918; P:peptidyl-arginine methylation, to symmetrical-dimethyl arginine; IDA:UniProtKB.
DR GO; GO:0035246; P:peptidyl-arginine N-methylation; IDA:WormBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:1990834; P:response to odorant; IMP:WormBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR007857; Arg_MeTrfase_PRMT5.
DR InterPro; IPR035075; PRMT5.
DR InterPro; IPR035248; PRMT5_C.
DR InterPro; IPR035247; PRMT5_TIM.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10738; PTHR10738; 1.
DR Pfam; PF05185; PRMT5; 1.
DR Pfam; PF17286; PRMT5_C; 1.
DR Pfam; PF17285; PRMT5_TIM; 1.
DR PIRSF; PIRSF015894; Skb1_MeTrfase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Chromatin regulator; DNA damage;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..734
FT /note="Protein arginine N-methyltransferase 5"
FT /id="PRO_0000212348"
FT DOMAIN 360..706
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..329
FT /note="TIM barrel"
FT /evidence="ECO:0000269|PubMed:22143770"
FT REGION 529..734
FT /note="Beta barrel"
FT /evidence="ECO:0000269|PubMed:22143770"
FT REGION 541..589
FT /note="Dimerization"
FT /evidence="ECO:0000269|PubMed:22143770"
FT ACT_SITE 499
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:22143770"
FT ACT_SITE 508
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:22143770"
FT BINDING 376
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 379
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_note="substrate"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 385..386
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 450
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 477..478
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 499
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_note="substrate"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 508
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_note="substrate"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT SITE 379
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000269|PubMed:22143770"
FT MUTAGEN 379
FT /note="F->M: Significantly elevates methylase activity, and
FT converts PRMT5 to an enzyme catalyzing both symmetric and
FT asymmetric arginine dimethylation."
FT /evidence="ECO:0000269|PubMed:22143770"
FT MUTAGEN 379
FT /note="F->Y: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:22143770"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3UA4"
FT TURN 61..66
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3UA4"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3UA4"
FT HELIX 138..157
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3UA3"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:3UA3"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:3UA3"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 285..293
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:3UA3"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:3UA3"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:3UA3"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 373..381
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 383..401
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 406..414
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 419..435
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 453..465
FT /evidence="ECO:0007829|PDB:3UA3"
FT TURN 466..469
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 481..487
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 494..498
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 510..515
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 516..520
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 531..540
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 542..549
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 584..589
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 601..606
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 608..616
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 625..632
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 635..651
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 654..657
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:3UA4"
FT STRAND 673..683
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 688..698
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 701..711
FT /evidence="ECO:0007829|PDB:3UA3"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:3UA3"
FT HELIX 725..727
FT /evidence="ECO:0007829|PDB:3UA3"
SQ SEQUENCE 734 AA; 83292 MW; 415AAC571206DB2C CRC64;
MSNRTYADNL FPQQVAEQHE EQMSSGSSPK SNSPSRSISS VEAANSRIHI GWMATTLDVA
ENLDRHVATF CTRLGEFKYN FVVYPIGGVV RAFWTPNGSA ENHPPVIDLP DVQLRNDLWE
SYVVGKISPW IDCDSSDPAF ASLSEEHLLK ELSYICYLGL QTMAIELTRI SSPRTAAILK
KWIWTRNSRF TVWVQLPSAI EKCKDYDAFT IEHVDLWTIW ADFRKNCGNF SGVYFQVALT
ISSELPDELT ELKLVDRWKA EPLAAFVIES GLFISGRNGE ASIPSAHINL LKHLWTTDAL
RIVLRATTDT FKYNTSIKSE YSQALRHAVR NVNYRSRPDV GEGSNDSTHY LNVIEYKDVL
QAPLQPLSEN LDSGVYNTFE QDQIKYDVYG EAVVGALKDL GADGRKTVVI YLLGGGRGPI
GTKILKSERE YNNTFRQGQE SLKVKLYIVE KNPNAIVTLK YMNVRTWKRR VTIIESDMRS
LPGIAKDRGF EQPDIIVSEL LGSFGDNELS PECLDGVTGF LKPTTISIPQ KYTSYVKPIM
STHIHQTIKA QSIPYLSRAI PSHGRGEPEL DEDEMWIQKY PQGHVRNNMD QIYVVYLSKY
IPLAETTKPV FTFEHPNFMN SSNERSDSIE FVMDRNADLM GFAGYFDLQL YKTVMLSIEP
STHTPGMVSW FPAVIPLRDQ LRVGEGDRIS LKIDRKVDNT GVWYEWHVEK KKTNGESVST
PIQNPNGESY YMRM
