MANF_HUMAN
ID MANF_HUMAN Reviewed; 182 AA.
AC P55145; Q14CX4; Q86U67; Q96IS4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Mesencephalic astrocyte-derived neurotrophic factor;
DE AltName: Full=Arginine-rich protein;
DE AltName: Full=Protein ARMET;
DE Flags: Precursor;
GN Name=MANF; Synonyms=ARMET, ARP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISCUSSION OF A PUTATIVE CANCER VARIANT.
RX PubMed=8649854;
RA Shridhar V., Rivard S., Shridhar R., Mullins C., Bostick L., Sakr W.,
RA Grignon D., Miller O.J., Smith D.I.;
RT "A gene from human chromosomal band 3p21.1 encodes a highly conserved
RT arginine-rich protein and is mutated in renal cell carcinomas.";
RL Oncogene 12:1931-1939(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP PROTEIN SEQUENCE OF 25-39.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP PROTEIN SEQUENCE OF 25-29, FUNCTION, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RX PubMed=12794311; DOI=10.1385/jmn:20:2:173;
RA Petrova P., Raibekas A., Pevsner J., Vigo N., Anafi M., Moore M.K.,
RA Peaire A.E., Shridhar V., Smith D.I., Kelly J., Durocher Y.,
RA Commissiong J.W.;
RT "MANF: a new mesencephalic, astrocyte-derived neurotrophic factor with
RT selectivity for dopaminergic neurons.";
RL J. Mol. Neurosci. 20:173-188(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=18561914; DOI=10.1016/j.yexcr.2008.05.001;
RA Apostolou A., Shen Y., Liang Y., Luo J., Fang S.;
RT "Armet, a UPR-upregulated protein, inhibits cell proliferation and ER
RT stress-induced cell death.";
RL Exp. Cell Res. 314:2454-2467(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION, INTERACTION WITH HSPA5, SUBCELLULAR LOCATION, INDUCTION, AND
RP MUTAGENESIS OF 179-ARG--LYS-182 AND ARG-179.
RX PubMed=22637475; DOI=10.1074/jbc.m112.356345;
RA Glembotski C.C., Thuerauf D.J., Huang C., Vekich J.A., Gottlieb R.A.,
RA Doroudgar S.;
RT "Mesencephalic astrocyte-derived neurotrophic factor protects the heart
RT from ischemic damage and is selectively secreted upon sarco/endoplasmic
RT reticulum calcium depletion.";
RL J. Biol. Chem. 287:25893-25904(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DOMAIN, AND MUTAGENESIS OF
RP LYS-112.
RX PubMed=29497057; DOI=10.1038/s41467-018-03355-0;
RA Bai M., Vozdek R., Hnizda A., Jiang C., Wang B., Kuchar L., Li T.,
RA Zhang Y., Wood C., Feng L., Dang Y., Ma D.K.;
RT "Conserved roles of C. elegans and human MANFs in sulfatide binding and
RT cytoprotection.";
RL Nat. Commun. 9:897-897(2018).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 25-182, DOMAIN, AND DISULFIDE
RP BONDS.
RX PubMed=19258449; DOI=10.1093/protein/gzn080;
RA Parkash V., Lindholm P., Peranen J., Kalkkinen N., Oksanen E., Saarma M.,
RA Leppanen V.-M., Goldman A.;
RT "The structure of the conserved neurotrophic factors MANF and CDNF explains
RT why they are bifunctional.";
RL Protein Eng. Des. Sel. 22:233-241(2009).
RN [15]
RP DISCUSSION OF A PUTATIVE CANCER VARIANT.
RX PubMed=8971156;
RA Shridhar R., Shridhar V., Rivard S., Siegfried J.M., Pietraszkiewicz H.,
RA Ensley J., Pauley R., Grignon D., Sakr W., Miller O.J., Smith D.I.;
RT "Mutations in the arginine-rich protein gene, in lung, breast, and prostate
RT cancers, and in squamous cell carcinoma of the head and neck.";
RL Cancer Res. 56:5576-5578(1996).
RN [16]
RP DISCUSSION OF PUTATIVE CANCER VARIANTS.
RX PubMed=9174057; DOI=10.1038/sj.onc.1201054;
RA Shridhar V., Rivard S., Wang X., Shridhar R., Paisley C., Mullins C.,
RA Beirnat L., Dugan M., Sarkar F., Miller O.J., Vaitkevicius V.K.,
RA Smith D.I.;
RT "Mutations in the arginine-rich protein gene (ARP) in pancreatic cancer.";
RL Oncogene 14:2213-2216(1997).
CC -!- FUNCTION: Selectively promotes the survival of dopaminergic neurons of
CC the ventral mid-brain (PubMed:12794311). Modulates GABAergic
CC transmission to the dopaminergic neurons of the substantia nigra (By
CC similarity). Enhances spontaneous, as well as evoked, GABAergic
CC inhibitory postsynaptic currents in dopaminergic neurons (By
CC similarity). Inhibits cell proliferation and endoplasmic reticulum (ER)
CC stress-induced cell death (PubMed:18561914, PubMed:22637475,
CC PubMed:29497057). Retained in the ER/sarcoplasmic reticulum (SR)
CC through association with the endoplasmic reticulum chaperone protein
CC HSPA5 under normal conditions (PubMed:22637475). Up-regulated and
CC secreted by the ER/SR in response to ER stress and hypoxia
CC (PubMed:22637475). Following secretion by the ER/SR, directly binds to
CC 3-O-sulfogalactosylceramide, a lipid sulfatide in the outer cell
CC membrane of target cells (PubMed:29497057). Sulfatide binding promotes
CC its cellular uptake by endocytosis, and is required for its role in
CC alleviating ER stress and cell toxicity under hypoxic and ER stress
CC conditions (PubMed:29497057). {ECO:0000250|UniProtKB:P0C5H9,
CC ECO:0000269|PubMed:12794311, ECO:0000269|PubMed:18561914,
CC ECO:0000269|PubMed:22637475, ECO:0000269|PubMed:29497057}.
CC -!- SUBUNIT: Interacts with HSPA5; the interaction is direct
CC (PubMed:22637475). Component of a complex containing at least CRELD2,
CC MANF, MATN3 and PDIA4 (By similarity). {ECO:0000250|UniProtKB:Q9CXI5,
CC ECO:0000269|PubMed:22637475}.
CC -!- INTERACTION:
CC P55145; Q16799-3: RTN1; NbExp=4; IntAct=EBI-1044104, EBI-10180131;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12794311,
CC ECO:0000269|PubMed:18561914, ECO:0000269|PubMed:22637475,
CC ECO:0000269|PubMed:29497057}. Endoplasmic reticulum lumen
CC {ECO:0000305|PubMed:29497057}. Sarcoplasmic reticulum lumen
CC {ECO:0000269|PubMed:22637475}. Note=Retained in the endoplasmic
CC reticulum (ER), and sarcoplasmic reticulum (SR) under normal conditions
CC (PubMed:22637475). Up-regulated and secreted by the ER/SR in response
CC to ER stress and hypoxia (PubMed:22637475, PubMed:29497057).
CC {ECO:0000269|PubMed:22637475, ECO:0000269|PubMed:29497057}.
CC -!- INDUCTION: By endoplasmic reticulum stress (PubMed:18561914,
CC PubMed:22637475, PubMed:29497057). By hypoxia (PubMed:29497057).
CC {ECO:0000269|PubMed:18561914, ECO:0000269|PubMed:22637475,
CC ECO:0000269|PubMed:29497057}.
CC -!- DOMAIN: The N-terminal region may be responsible for neurotrophic
CC activity while the C-terminal region may play a role in the ER stress
CC response. {ECO:0000269|PubMed:19258449}.
CC -!- DOMAIN: The N-terminal region may be required for lipid sulfatide
CC binding. {ECO:0000269|PubMed:29497057}.
CC -!- PTM: May contain sialic acid residues.
CC -!- SIMILARITY: Belongs to the ARMET family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:8649854, PubMed:8971156 and
CC PubMed:9174057) thought to be much longer and included an arginine-rich
CC region thought to be the target of cancer-causing mutations. All these
CC mutations are in what is now thought to be the 5'-UTR of the mRNA.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB08753.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI13589.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI13591.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M83751; AAB08753.1; ALT_INIT; mRNA.
DR EMBL; BT007110; AAP35774.1; -; mRNA.
DR EMBL; AC092037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007282; AAH07282.1; -; mRNA.
DR EMBL; BC113588; AAI13589.1; ALT_INIT; mRNA.
DR EMBL; BC113590; AAI13591.1; ALT_INIT; mRNA.
DR CCDS; CCDS46836.3; -.
DR RefSeq; NP_006001.4; NM_006010.5.
DR PDB; 2KVD; NMR; -; A=25-182.
DR PDB; 2KVE; NMR; -; A=120-182.
DR PDB; 2W51; X-ray; 2.80 A; A=25-182.
DR PDBsum; 2KVD; -.
DR PDBsum; 2KVE; -.
DR PDBsum; 2W51; -.
DR AlphaFoldDB; P55145; -.
DR SMR; P55145; -.
DR BioGRID; 113621; 98.
DR IntAct; P55145; 26.
DR MINT; P55145; -.
DR STRING; 9606.ENSP00000432799; -.
DR iPTMnet; P55145; -.
DR MetOSite; P55145; -.
DR PhosphoSitePlus; P55145; -.
DR SwissPalm; P55145; -.
DR BioMuta; MANF; -.
DR DMDM; 332278201; -.
DR OGP; P55145; -.
DR CPTAC; CPTAC-403; -.
DR CPTAC; CPTAC-404; -.
DR EPD; P55145; -.
DR jPOST; P55145; -.
DR MassIVE; P55145; -.
DR MaxQB; P55145; -.
DR PaxDb; P55145; -.
DR PeptideAtlas; P55145; -.
DR PRIDE; P55145; -.
DR ProteomicsDB; 56793; -.
DR Antibodypedia; 2505; 339 antibodies from 35 providers.
DR DNASU; 7873; -.
DR Ensembl; ENST00000528157.7; ENSP00000432799.3; ENSG00000145050.19.
DR GeneID; 7873; -.
DR KEGG; hsa:7873; -.
DR MANE-Select; ENST00000528157.7; ENSP00000432799.3; NM_006010.6; NP_006001.5.
DR UCSC; uc003dbc.4; human.
DR CTD; 7873; -.
DR DisGeNET; 7873; -.
DR GeneCards; MANF; -.
DR HGNC; HGNC:15461; MANF.
DR HPA; ENSG00000145050; Low tissue specificity.
DR MIM; 601916; gene.
DR neXtProt; NX_P55145; -.
DR OpenTargets; ENSG00000145050; -.
DR PharmGKB; PA24993; -.
DR VEuPathDB; HostDB:ENSG00000145050; -.
DR eggNOG; KOG4154; Eukaryota.
DR GeneTree; ENSGT00390000007160; -.
DR HOGENOM; CLU_099080_1_0_1; -.
DR InParanoid; P55145; -.
DR OMA; ECEVCVS; -.
DR OrthoDB; 1427430at2759; -.
DR PhylomeDB; P55145; -.
DR TreeFam; TF314252; -.
DR PathwayCommons; P55145; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; P55145; -.
DR BioGRID-ORCS; 7873; 202 hits in 1077 CRISPR screens.
DR ChiTaRS; MANF; human.
DR EvolutionaryTrace; P55145; -.
DR GeneWiki; ARMET; -.
DR GenomeRNAi; 7873; -.
DR Pharos; P55145; Tbio.
DR PRO; PR:P55145; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P55145; protein.
DR Bgee; ENSG00000145050; Expressed in islet of Langerhans and 197 other tissues.
DR ExpressionAtlas; P55145; baseline and differential.
DR Genevisible; P55145; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0120146; F:sulfatide binding; IPI:UniProtKB.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:1905897; P:regulation of response to endoplasmic reticulum stress; IMP:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR Gene3D; 1.10.720.30; -; 1.
DR InterPro; IPR045333; ARMET-like.
DR InterPro; IPR019345; ARMET_C.
DR InterPro; IPR045332; ARMET_N.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR12990; PTHR12990; 1.
DR Pfam; PF10208; ARMET_C; 1.
DR Pfam; PF20145; ARMET_N; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Growth factor; Lipid-binding;
KW Phosphoprotein; Reference proteome; Sarcoplasmic reticulum; Secreted;
KW Sialic acid; Signal; Stress response; Unfolded protein response.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:12794311"
FT CHAIN 25..182
FT /note="Mesencephalic astrocyte-derived neurotrophic factor"
FT /id="PRO_0000002305"
FT MOD_RES 76
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CXI5"
FT DISULFID 30..117
FT /evidence="ECO:0000269|PubMed:19258449"
FT DISULFID 33..106
FT /evidence="ECO:0000269|PubMed:19258449"
FT DISULFID 64..75
FT /evidence="ECO:0000269|PubMed:19258449"
FT DISULFID 151..154
FT /evidence="ECO:0000269|PubMed:19258449"
FT MUTAGEN 112
FT /note="K->L: Reduced sulfatide binding and uptake by target
FT cells. Reduces cytoprotective effect of the wild-type
FT protein. Attenuates stress granule formation in response to
FT endoplasmic reticulum stress."
FT /evidence="ECO:0000269|PubMed:29497057"
FT MUTAGEN 179..182
FT /note="Missing: Two-fold increase in secretion."
FT /evidence="ECO:0000269|PubMed:22637475"
FT MUTAGEN 179
FT /note="R->K: 14-fold decrease in secretion."
FT /evidence="ECO:0000269|PubMed:22637475"
FT CONFLICT 13..14
FT /note="AL -> RV (in Ref. 1; AAB08753)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="R -> P (in Ref. 1; AAB08753)"
FT /evidence="ECO:0000305"
FT HELIX 31..46
FT /evidence="ECO:0007829|PDB:2W51"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:2W51"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:2W51"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2W51"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2W51"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:2W51"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:2W51"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:2W51"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2KVD"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2KVD"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:2W51"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:2W51"
FT TURN 166..173
FT /evidence="ECO:0007829|PDB:2KVD"
SQ SEQUENCE 182 AA; 20700 MW; EE25A5D1A58D1AD7 CRC64;
MRRMWATQGL AVALALSVLP GSRALRPGDC EVCISYLGRF YQDLKDRDVT FSPATIENEL
IKFCREARGK ENRLCYYIGA TDDAATKIIN EVSKPLAHHI PVEKICEKLK KKDSQICELK
YDKQIDLSTV DLKKLRVKEL KKILDDWGET CKGCAEKSDY IRKINELMPK YAPKAASART
DL
