TRM1_HUMAN
ID TRM1_HUMAN Reviewed; 659 AA.
AC Q9NXH9; O76103; Q548Y5; Q8WVA6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase;
DE EC=2.1.1.216;
DE AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase;
DE AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase;
DE AltName: Full=tRNA(m(2,2)G26)dimethyltransferase;
GN Name=TRMT1;
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] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=10982862; DOI=10.1093/nar/28.18.3445;
RA Liu J., Straby K.B.;
RT "The human tRNA(m22G26)dimethyltransferase: functional expression and
RT characterization of a cloned hTRM1 gene.";
RL Nucleic Acids Res. 28:3445-3451(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon mucosa;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Cervix, and Colon;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-646, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625; THR-628 AND THR-646, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 AND SER-625, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [11]
RP INVOLVEMENT IN MRT68.
RX PubMed=21937992; DOI=10.1038/nature10423;
RA Najmabadi H., Hu H., Garshasbi M., Zemojtel T., Abedini S.S., Chen W.,
RA Hosseini M., Behjati F., Haas S., Jamali P., Zecha A., Mohseni M.,
RA Puettmann L., Vahid L.N., Jensen C., Moheb L.A., Bienek M., Larti F.,
RA Mueller I., Weissmann R., Darvish H., Wrogemann K., Hadavi V.,
RA Lipkowitz B., Esmaeeli-Nieh S., Wieczorek D., Kariminejad R.,
RA Firouzabadi S.G., Cohen M., Fattahi Z., Rost I., Mojahedi F., Hertzberg C.,
RA Dehghan A., Rajab A., Banavandi M.J., Hoffer J., Falah M., Musante L.,
RA Kalscheuer V., Ullmann R., Kuss A.W., Tzschach A., Kahrizi K., Ropers H.H.;
RT "Deep sequencing reveals 50 novel genes for recessive cognitive
RT disorders.";
RL Nature 478:57-63(2011).
RN [12]
RP INVOLVEMENT IN MRT68.
RX PubMed=26308914; DOI=10.1371/journal.pone.0129631;
RA Davarniya B., Hu H., Kahrizi K., Musante L., Fattahi Z., Hosseini M.,
RA Maqsoud F., Farajollahi R., Wienker T.F., Ropers H.H., Najmabadi H.;
RT "The role of a novel TRMT1 gene mutation and rare grm1 gene defect in
RT intellectual disability in two azeri families.";
RL PLoS ONE 10:E0129631-E0129631(2015).
RN [13]
RP INVOLVEMENT IN MRT68.
RX PubMed=30289604; DOI=10.1002/ajmg.a.38631;
RA Blaesius K., Abbasi A.A., Tahir T.H., Tietze A., Picker-Minh S., Ali G.,
RA Farooq S., Hu H., Latif Z., Khan M.N., Kaindl A.;
RT "Mutations in the tRNA methyltransferase 1 gene TRMT1 cause congenital
RT microcephaly, isolated inferior vermian hypoplasia and cystic leukomalacia
RT in addition to intellectual disability.";
RL Am. J. Med. Genet. A 176:2517-2521(2018).
CC -!- FUNCTION: Dimethylates a single guanine residue at position 26 of most
CC tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00958};
CC -!- INTERACTION:
CC Q9NXH9; P43364: MAGEA11; NbExp=5; IntAct=EBI-748900, EBI-739552;
CC Q9NXH9; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-748900, EBI-10178634;
CC Q9NXH9; P54274: TERF1; NbExp=2; IntAct=EBI-748900, EBI-710997;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NXH9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NXH9-2; Sequence=VSP_016720;
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 68
CC (MRT68) [MIM:618302]: A form of intellectual disability, a disorder
CC characterized by significantly below average general intellectual
CC functioning associated with impairments in adaptive behavior and
CC manifested during the developmental period.
CC {ECO:0000269|PubMed:21937992, ECO:0000269|PubMed:26308914,
CC ECO:0000269|PubMed:30289604}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000255|PROSITE-ProRule:PRU00958}.
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DR EMBL; AF196479; AAG28495.1; -; mRNA.
DR EMBL; AK000251; BAA91031.1; -; mRNA.
DR EMBL; AC005546; AAC33150.1; -; Genomic_DNA.
DR EMBL; BC002492; AAH02492.1; -; mRNA.
DR EMBL; BC018302; AAH18302.1; -; mRNA.
DR EMBL; BC040126; AAH40126.1; -; mRNA.
DR CCDS; CCDS12293.1; -. [Q9NXH9-1]
DR CCDS; CCDS45997.1; -. [Q9NXH9-2]
DR RefSeq; NP_001129507.1; NM_001136035.2. [Q9NXH9-1]
DR RefSeq; NP_001136026.1; NM_001142554.1. [Q9NXH9-2]
DR RefSeq; NP_060192.1; NM_017722.3. [Q9NXH9-1]
DR RefSeq; XP_016882433.1; XM_017026944.1.
DR RefSeq; XP_016882434.1; XM_017026945.1.
DR AlphaFoldDB; Q9NXH9; -.
DR SMR; Q9NXH9; -.
DR BioGRID; 120760; 95.
DR IntAct; Q9NXH9; 32.
DR MINT; Q9NXH9; -.
DR STRING; 9606.ENSP00000466967; -.
DR GlyGen; Q9NXH9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NXH9; -.
DR PhosphoSitePlus; Q9NXH9; -.
DR BioMuta; TRMT1; -.
DR DMDM; 12643821; -.
DR EPD; Q9NXH9; -.
DR jPOST; Q9NXH9; -.
DR MassIVE; Q9NXH9; -.
DR MaxQB; Q9NXH9; -.
DR PaxDb; Q9NXH9; -.
DR PeptideAtlas; Q9NXH9; -.
DR PRIDE; Q9NXH9; -.
DR ProteomicsDB; 83100; -. [Q9NXH9-1]
DR ProteomicsDB; 83101; -. [Q9NXH9-2]
DR Antibodypedia; 13510; 162 antibodies from 26 providers.
DR DNASU; 55621; -.
DR Ensembl; ENST00000221504.12; ENSP00000221504.7; ENSG00000104907.13. [Q9NXH9-2]
DR Ensembl; ENST00000357720.9; ENSP00000350352.4; ENSG00000104907.13. [Q9NXH9-1]
DR Ensembl; ENST00000437766.5; ENSP00000416149.1; ENSG00000104907.13. [Q9NXH9-1]
DR Ensembl; ENST00000592062.5; ENSP00000466967.1; ENSG00000104907.13. [Q9NXH9-1]
DR GeneID; 55621; -.
DR KEGG; hsa:55621; -.
DR MANE-Select; ENST00000357720.9; ENSP00000350352.4; NM_001136035.4; NP_001129507.1.
DR UCSC; uc002mwj.3; human. [Q9NXH9-1]
DR CTD; 55621; -.
DR DisGeNET; 55621; -.
DR GeneCards; TRMT1; -.
DR HGNC; HGNC:25980; TRMT1.
DR HPA; ENSG00000104907; Low tissue specificity.
DR MalaCards; TRMT1; -.
DR MIM; 611669; gene.
DR MIM; 618302; phenotype.
DR neXtProt; NX_Q9NXH9; -.
DR OpenTargets; ENSG00000104907; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA134867808; -.
DR VEuPathDB; HostDB:ENSG00000104907; -.
DR eggNOG; KOG1253; Eukaryota.
DR GeneTree; ENSGT00530000063646; -.
DR HOGENOM; CLU_010862_4_1_1; -.
DR InParanoid; Q9NXH9; -.
DR OMA; YRVSYSH; -.
DR PhylomeDB; Q9NXH9; -.
DR TreeFam; TF300851; -.
DR PathwayCommons; Q9NXH9; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q9NXH9; -.
DR BioGRID-ORCS; 55621; 31 hits in 1084 CRISPR screens.
DR ChiTaRS; TRMT1; human.
DR GenomeRNAi; 55621; -.
DR Pharos; Q9NXH9; Tbio.
DR PRO; PR:Q9NXH9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NXH9; protein.
DR Bgee; ENSG00000104907; Expressed in lower esophagus mucosa and 148 other tissues.
DR ExpressionAtlas; Q9NXH9; baseline and differential.
DR Genevisible; Q9NXH9; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; EXP:Reactome.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; TAS:Reactome.
DR GO; GO:0002940; P:tRNA N2-guanine methylation; IBA:GO_Central.
DR Gene3D; 3.30.56.70; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002905; Trm1.
DR InterPro; IPR042296; tRNA_met_Trm1_C.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR10631; PTHR10631; 1.
DR Pfam; PF02005; TRM; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR TIGRFAMs; TIGR00308; TRM1; 1.
DR PROSITE; PS51626; SAM_MT_TRM1; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Intellectual disability; Metal-binding;
KW Methyltransferase; Phosphoprotein; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..659
FT /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT /id="PRO_0000147671"
FT DOMAIN 55..499
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00958"
FT ZN_FING 600..627
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 537..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TX08"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 628
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 646
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT VAR_SEQ 340..368
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016720"
FT CONFLICT 500..503
FT /note="RCWE -> Q (in Ref. 3; AAC33150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 659 AA; 72234 MW; E4F0F2B740B44387 CRC64;
MQGSSLWLSL TFRSARVLSR ARFFEWQSPG LPNTAAMENG TGPYGEERPR EVQETTVTEG
AAKIAFPSAN EVFYNPVQEF NRDLTCAVIT EFARIQLGAK GIQIKVPGEK DTQKVVVDLS
EQEEEKVELK ESENLASGDQ PRTAAVGEIC EEGLHVLEGL AASGLRSIRF ALEVPGLRSV
VANDASTRAV DLIRRNVQLN DVAHLVQPSQ ADARMLMYQH QRVSERFDVI DLDPYGSPAT
FLDAAVQAVS EGGLLCVTCT DMAVLAGNSG ETCYSKYGAM ALKSRACHEM ALRIVLHSLD
LRANCYQRFV VPLLSISADF YVRVFVRVFT GQAKVKASAS KQALVFQCVG CGAFHLQRLG
KASGVPSGRA KFSAACGPPV TPECEHCGQR HQLGGPMWAE PIHDLDFVGR VLEAVSANPG
RFHTSERIRG VLSVITEELP DVPLYYTLDQ LSSTIHCNTP SLLQLRSALL HADFRVSLSH
ACKNAVKTDA PASALWDIMR CWEKECPVKR ERLSETSPAF RILSVEPRLQ ANFTIREDAN
PSSRQRGLKR FQANPEANWG PRPRARPGGK AADEAMEERR RLLQNKRKEP PEDVAQRAAR
LKTFPCKRFK EGTCQRGDQC CYSHSPPTPR VSADAAPDCP ETSNQTPPGP GAAAGPGID
