MYG1_HUMAN
ID MYG1_HUMAN Reviewed; 376 AA.
AC Q9HB07; Q86UA3;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=MYG1 exonuclease {ECO:0000305};
DE EC=3.1.-.- {ECO:0000303|PubMed:31081026};
DE Flags: Precursor;
GN Name=MYG1 {ECO:0000312|HGNC:HGNC:17590}; Synonyms=C12orf10;
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 VARIANT ILE-349.
RA Smicun Y.;
RT "The human homologue of MYG1 the highly conserved gene from autonomously
RT proliferating mouse melanocytes.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH51871.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAH51871.1};
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 [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19014353; DOI=10.1042/bc20080086;
RA Philips M.-A., Vikesaa J., Luuk H., Joenson L., Lillevaeli K.,
RA Rehfeld J.F., Vasar E., Koks S., Nielsen F.C.;
RT "Characterization of MYG1 gene and protein: subcellular distribution and
RT function.";
RL Biol. Cell 101:361-373(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP FUNCTION, MUTAGENESIS OF 106-ASP--HIS-108 AND HIS-344, AND INVOLVEMENT IN
RP VITILIGO.
RX PubMed=31081026; DOI=10.1093/nar/gkz371;
RA Grover R., Burse S.A., Shankrit S., Aggarwal A., Kirty K., Narta K.,
RA Srivastav R., Ray A.K., Malik G., Vats A., Motiani R.K., Thukral L.,
RA Roy S.S., Bhattacharya S., Sharma R., Natarajan K., Mukerji M., Pandey R.,
RA Gokhale R.S., Natarajan V.T.;
RT "Myg1 exonuclease couples the nuclear and mitochondrial translational
RT programs through RNA processing.";
RL Nucleic Acids Res. 47:5852-5866(2019).
RN [10]
RP INVOLVEMENT IN VITILIGO, VARIANT GLN-4, CHARACTERIZATION OF VARIANT GLN-4,
RP AND SUBCELLULAR LOCATION.
RX PubMed=20377893; DOI=10.1186/1471-2350-11-56;
RA Philips M.A., Kingo K., Karelson M., Raetsep R., Aunin E., Reimann E.,
RA Reemann P., Porosaar O., Vikesaa J., Nielsen F.C., Vasar E., Silm H.,
RA Koks S.;
RT "Promoter polymorphism -119C/G in MYG1 (C12orf10) gene is related to
RT vitiligo susceptibility and Arg4Gln affects mitochondrial entrance of
RT Myg1.";
RL BMC Med. Genet. 11:56-56(2010).
RN [11]
RP INVOLVEMENT IN VITILIGO.
RX PubMed=30051642; DOI=10.1111/jdv.15195;
RA Traks T., Keermann M., Karelson M., Raetsep R., Reimann E., Silm H.,
RA Vasar E., Koks S., Kingo K.;
RT "Polymorphisms in melanocortin system and MYG1 genes are associated with
RT vitiligo.";
RL J. Eur. Acad. Dermatol. Venereol. 33:e65-e67(2019).
CC -!- FUNCTION: 3'-5' RNA exonuclease which cleaves in situ on specific
CC transcripts in both nucleus and mitochondrion. Involved in regulating
CC spatially segregated organellar RNA processing, acts as a coordinator
CC of nucleo-mitochondrial crosstalk (PubMed:31081026). In nucleolus,
CC processes pre-ribosomal RNA involved in ribosome assembly and alters
CC cytoplasmic translation. In mitochondrial matrix, processes 3'-termini
CC of the mito-ribosomal and messenger RNAs and controls translation of
CC mitochondrial proteins (Probable). {ECO:0000269|PubMed:31081026,
CC ECO:0000305|PubMed:31081026}.
CC -!- INTERACTION:
CC Q9HB07; Q6RW13: AGTRAP; NbExp=4; IntAct=EBI-709754, EBI-741181;
CC Q9HB07; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-709754, EBI-11522760;
CC Q9HB07; P49419-2: ALDH7A1; NbExp=3; IntAct=EBI-709754, EBI-11107920;
CC Q9HB07; Q10567-3: AP1B1; NbExp=3; IntAct=EBI-709754, EBI-11978055;
CC Q9HB07; Q6Q788: APOA5; NbExp=3; IntAct=EBI-709754, EBI-3936819;
CC Q9HB07; Q15041: ARL6IP1; NbExp=6; IntAct=EBI-709754, EBI-714543;
CC Q9HB07; Q8WZ55: BSND; NbExp=3; IntAct=EBI-709754, EBI-7996695;
CC Q9HB07; Q9BSJ5: C17orf80; NbExp=3; IntAct=EBI-709754, EBI-2872520;
CC Q9HB07; O95674: CDS2; NbExp=3; IntAct=EBI-709754, EBI-3913685;
CC Q9HB07; Q96DZ9: CMTM5; NbExp=4; IntAct=EBI-709754, EBI-2548702;
CC Q9HB07; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-709754, EBI-11522780;
CC Q9HB07; Q6PUV4: CPLX2; NbExp=3; IntAct=EBI-709754, EBI-2689453;
CC Q9HB07; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-709754, EBI-10303987;
CC Q9HB07; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-709754, EBI-742054;
CC Q9HB07; Q9BSY9: DESI2; NbExp=3; IntAct=EBI-709754, EBI-12878374;
CC Q9HB07; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-709754, EBI-12831978;
CC Q9HB07; P26641: EEF1G; NbExp=3; IntAct=EBI-709754, EBI-351467;
CC Q9HB07; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-709754, EBI-781551;
CC Q9HB07; Q8IZU0: FAM9B; NbExp=4; IntAct=EBI-709754, EBI-10175124;
CC Q9HB07; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-709754, EBI-372506;
CC Q9HB07; P62993: GRB2; NbExp=3; IntAct=EBI-709754, EBI-401755;
CC Q9HB07; Q86X24: HORMAD1; NbExp=3; IntAct=EBI-709754, EBI-12165207;
CC Q9HB07; Q969L2: MAL2; NbExp=3; IntAct=EBI-709754, EBI-944295;
CC Q9HB07; Q9NR34: MAN1C1; NbExp=3; IntAct=EBI-709754, EBI-7260764;
CC Q9HB07; Q9H1A3: METTL9; NbExp=3; IntAct=EBI-709754, EBI-2804879;
CC Q9HB07; Q9BRX2: PELO; NbExp=3; IntAct=EBI-709754, EBI-1043580;
CC Q9HB07; O60664: PLIN3; NbExp=3; IntAct=EBI-709754, EBI-725795;
CC Q9HB07; Q59EV6: PPGB; NbExp=3; IntAct=EBI-709754, EBI-14210385;
CC Q9HB07; P57052: RBM11; NbExp=3; IntAct=EBI-709754, EBI-741332;
CC Q9HB07; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-709754, EBI-14065960;
CC Q9HB07; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-709754, EBI-17589229;
CC Q9HB07; Q03395: ROM1; NbExp=3; IntAct=EBI-709754, EBI-9395257;
CC Q9HB07; P28702: RXRB; NbExp=3; IntAct=EBI-709754, EBI-748576;
CC Q9HB07; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-709754, EBI-2854842;
CC Q9HB07; Q9BYT1: SLC17A9; NbExp=3; IntAct=EBI-709754, EBI-3940816;
CC Q9HB07; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-709754, EBI-742688;
CC Q9HB07; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-709754, EBI-12187159;
CC Q9HB07; P08247: SYP; NbExp=3; IntAct=EBI-709754, EBI-9071725;
CC Q9HB07; O60830: TIMM17B; NbExp=3; IntAct=EBI-709754, EBI-2372529;
CC Q9HB07; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-709754, EBI-12947623;
CC Q9HB07; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-709754, EBI-12195227;
CC Q9HB07; Q8WW34: TMEM239; NbExp=3; IntAct=EBI-709754, EBI-9675724;
CC Q9HB07; Q9H2S6-2: TNMD; NbExp=3; IntAct=EBI-709754, EBI-12003398;
CC Q9HB07; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-709754, EBI-12040603;
CC Q9HB07; O95070: YIF1A; NbExp=3; IntAct=EBI-709754, EBI-2799703;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:19014353, ECO:0000269|PubMed:20377893}.
CC Mitochondrion matrix {ECO:0000269|PubMed:19014353,
CC ECO:0000269|PubMed:20377893}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9JK81}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC testis. {ECO:0000269|PubMed:19014353}.
CC -!- DISEASE: Note=Several works have found that mRNA expression is elevated
CC in the skin of vitiligo patients. {ECO:0000269|PubMed:20377893,
CC ECO:0000269|PubMed:30051642, ECO:0000269|PubMed:31081026}.
CC -!- SIMILARITY: Belongs to the MYG1 family. {ECO:0000305}.
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DR EMBL; AF289485; AAG17847.1; -; mRNA.
DR EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96688.1; -; Genomic_DNA.
DR EMBL; BC051871; AAH51871.1; -; mRNA.
DR CCDS; CCDS31810.1; -.
DR RefSeq; NP_067653.3; NM_021640.3.
DR AlphaFoldDB; Q9HB07; -.
DR IntAct; Q9HB07; 50.
DR MINT; Q9HB07; -.
DR STRING; 9606.ENSP00000267103; -.
DR iPTMnet; Q9HB07; -.
DR MetOSite; Q9HB07; -.
DR PhosphoSitePlus; Q9HB07; -.
DR SwissPalm; Q9HB07; -.
DR BioMuta; C12orf10; -.
DR DMDM; 296439232; -.
DR REPRODUCTION-2DPAGE; IPI00029444; -.
DR EPD; Q9HB07; -.
DR jPOST; Q9HB07; -.
DR MassIVE; Q9HB07; -.
DR MaxQB; Q9HB07; -.
DR PaxDb; Q9HB07; -.
DR PeptideAtlas; Q9HB07; -.
DR PRIDE; Q9HB07; -.
DR ProteomicsDB; 81466; -.
DR Antibodypedia; 48361; 35 antibodies from 12 providers.
DR DNASU; 60314; -.
DR Ensembl; ENST00000267103.10; ENSP00000267103.5; ENSG00000139637.14.
DR GeneID; 60314; -.
DR KEGG; hsa:60314; -.
DR UCSC; uc001scp.5; human.
DR CTD; 60314; -.
DR GeneCards; MYG1; -.
DR HGNC; HGNC:17590; MYG1.
DR HPA; ENSG00000139637; Low tissue specificity.
DR MIM; 611366; gene.
DR neXtProt; NX_Q9HB07; -.
DR VEuPathDB; HostDB:ENSG00000139637; -.
DR eggNOG; KOG2948; Eukaryota.
DR InParanoid; Q9HB07; -.
DR OrthoDB; 1174497at2759; -.
DR PhylomeDB; Q9HB07; -.
DR TreeFam; TF313313; -.
DR PathwayCommons; Q9HB07; -.
DR SignaLink; Q9HB07; -.
DR BioGRID-ORCS; 60314; 34 hits in 1073 CRISPR screens.
DR ChiTaRS; C12orf10; human.
DR GenomeRNAi; 60314; -.
DR Pharos; Q9HB07; Tbio.
DR PRO; PR:Q9HB07; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9HB07; protein.
DR Bgee; ENSG00000139637; Expressed in primary visual cortex and 98 other tissues.
DR ExpressionAtlas; Q9HB07; baseline and differential.
DR Genevisible; Q9HB07; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR InterPro; IPR003226; Met-dep_prot_hydro.
DR PANTHER; PTHR11215; PTHR11215; 1.
DR Pfam; PF03690; UPF0160; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Mitochondrion; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 48..376
FT /note="MYG1 exonuclease"
FT /id="PRO_0000213483"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 273
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK81"
FT VARIANT 4
FT /note="R -> Q (loss of mitochondrial location)"
FT /evidence="ECO:0000269|PubMed:20377893"
FT /id="VAR_083553"
FT VARIANT 349
FT /note="T -> I (in dbSNP:rs1534282)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_059854"
FT MUTAGEN 106..108
FT /note="DHH->AAL: Catalytically inactive."
FT /evidence="ECO:0000269|PubMed:31081026"
FT MUTAGEN 344
FT /note="H->Q: Loss of RNase activity and gained single
FT stranded DNase activity."
FT /evidence="ECO:0000269|PubMed:31081026"
FT CONFLICT 150
FT /note="T -> P (in Ref. 1; AAG17847)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..353
FT /note="TGGHH -> IGGHR (in Ref. 4; AAH51871)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="H -> P (in Ref. 1; AAG17847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 42477 MW; 9CCB511AFF6A0C16 CRC64;
MGHRFLRGLL TLLLPPPPLY TRHRMLGPES VPPPKRSRSK LMAPPRIGTH NGTFHCDEAL
ACALLRLLPE YRDAEIVRTR DPEKLASCDI VVDVGGEYDP RRHRYDHHQR SFTETMSSLS
PGKPWQTKLS SAGLIYLHFG HKLLAQLLGT SEEDSMVGTL YDKMYENFVE EVDAVDNGIS
QWAEGEPRYA LTTTLSARVA RLNPTWNHPD QDTEAGFKRA MDLVQEEFLQ RLDFYQHSWL
PARALVEEAL AQRFQVDPSG EIVELAKGAC PWKEHLYHLE SGLSPPVAIF FVIYTDQAGQ
WRIQCVPKEP HSFQSRLPLP EPWRGLRDEA LDQVSGIPGC IFVHASGFTG GHHTREGALS
MARATLAQRS YLPQIS
