CMTR2_HUMAN
ID CMTR2_HUMAN Reviewed; 770 AA.
AC Q8IYT2; B2RCD5; D3DWS1; Q8NE77; Q8NFR5; Q9H8Z4; Q9NUS3; Q9NXF5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2;
DE EC=2.1.1.296 {ECO:0000269|PubMed:21310715};
DE AltName: Full=Cap methyltransferase 2;
DE AltName: Full=Cap2 2'O-ribose methyltransferase 2;
DE Short=HMTr2;
DE Short=MTr2;
DE AltName: Full=FtsJ methyltransferase domain-containing protein 1;
DE AltName: Full=Protein adrift homolog;
GN Name=CMTR2; Synonyms=AFT, FTSJD1;
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 [LARGE SCALE MRNA], AND VARIANTS PHE-60 AND SER-416.
RC TISSUE=Placenta, and Trachea;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-60.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-163.
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-343.
RC TISSUE=Testis;
RA Zan Q., Guo J.H., Yu L.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-117; ASP-235 AND LYS-275.
RX PubMed=21310715; DOI=10.1093/nar/gkr038;
RA Werner M., Purta E., Kaminska K.H., Cymerman I.A., Campbell D.A.,
RA Mittra B., Zamudio J.R., Sturm N.R., Jaworski J., Bujnicki J.M.;
RT "2'-O-ribose methylation of cap2 in human: function and evolution in a
RT horizontally mobile family.";
RL Nucleic Acids Res. 39:4756-4768(2011).
RN [7]
RP MUTAGENESIS OF LYS-74; LEU-77; SER-78; TRP-85; HIS-86; THR-89; GLN-113;
RP HIS-142; GLU-145 AND LYS-307.
RX PubMed=24402442; DOI=10.1038/ncomms4004;
RA Smietanski M., Werner M., Purta E., Kaminska K.H., Stepinski J.,
RA Darzynkiewicz E., Nowotny M., Bujnicki J.M.;
RT "Structural analysis of human 2'-O-ribose methyltransferases involved in
RT mRNA cap structure formation.";
RL Nat. Commun. 5:3004-3004(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of
CC mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG-
CC capped mRNA and small nuclear RNA (snRNA) (cap0) to produce
CC m(7)GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently
CC of its N(7) methylation status. Display cap2 methylation on both cap0
CC and cap1. Displays a preference for cap1 RNAs.
CC {ECO:0000269|PubMed:21310715}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC ribonucleoside)-(ribonucleotide) in mRNA + S-adenosyl-L-methionine =
CC a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC ribonucleoside)-(2'-O-methyl-ribonucleotide) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67024, Rhea:RHEA-COMP:17169,
CC Rhea:RHEA-COMP:17170, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:167612, ChEBI:CHEBI:167614;
CC EC=2.1.1.296; Evidence={ECO:0000269|PubMed:21310715};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21310715}. Cytoplasm
CC {ECO:0000269|PubMed:21310715}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM49718.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91058.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB14452.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK000289; BAA91058.1; ALT_FRAME; mRNA.
DR EMBL; AK002033; BAA92047.1; -; mRNA.
DR EMBL; AK023183; BAB14452.1; ALT_INIT; mRNA.
DR EMBL; AK315056; BAG37532.1; -; mRNA.
DR EMBL; AC106736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471166; EAW59246.1; -; Genomic_DNA.
DR EMBL; CH471166; EAW59247.1; -; Genomic_DNA.
DR EMBL; BC034468; AAH34468.1; -; mRNA.
DR EMBL; BC035005; AAH35005.1; -; mRNA.
DR EMBL; AF458590; AAM49718.1; ALT_FRAME; mRNA.
DR CCDS; CCDS10898.1; -.
DR RefSeq; NP_001093112.1; NM_001099642.1.
DR RefSeq; NP_001311303.1; NM_001324374.1.
DR RefSeq; NP_001311306.1; NM_001324377.1.
DR RefSeq; NP_001311307.1; NM_001324378.1.
DR RefSeq; NP_001311308.1; NM_001324379.1.
DR RefSeq; NP_060818.4; NM_018348.5.
DR RefSeq; XP_011521530.1; XM_011523228.1.
DR RefSeq; XP_011521531.1; XM_011523229.1.
DR RefSeq; XP_016878933.1; XM_017023444.1.
DR AlphaFoldDB; Q8IYT2; -.
DR SMR; Q8IYT2; -.
DR BioGRID; 120897; 25.
DR IntAct; Q8IYT2; 9.
DR STRING; 9606.ENSP00000337512; -.
DR iPTMnet; Q8IYT2; -.
DR PhosphoSitePlus; Q8IYT2; -.
DR BioMuta; CMTR2; -.
DR DMDM; 269849596; -.
DR EPD; Q8IYT2; -.
DR jPOST; Q8IYT2; -.
DR MassIVE; Q8IYT2; -.
DR MaxQB; Q8IYT2; -.
DR PaxDb; Q8IYT2; -.
DR PeptideAtlas; Q8IYT2; -.
DR PRIDE; Q8IYT2; -.
DR ProteomicsDB; 71233; -.
DR Antibodypedia; 44554; 81 antibodies from 18 providers.
DR DNASU; 55783; -.
DR Ensembl; ENST00000338099.9; ENSP00000337512.5; ENSG00000180917.18.
DR Ensembl; ENST00000434935.7; ENSP00000411148.2; ENSG00000180917.18.
DR GeneID; 55783; -.
DR KEGG; hsa:55783; -.
DR MANE-Select; ENST00000434935.7; ENSP00000411148.2; NM_018348.6; NP_060818.4.
DR UCSC; uc002ezy.5; human.
DR CTD; 55783; -.
DR DisGeNET; 55783; -.
DR GeneCards; CMTR2; -.
DR HGNC; HGNC:25635; CMTR2.
DR HPA; ENSG00000180917; Low tissue specificity.
DR MIM; 616190; gene.
DR neXtProt; NX_Q8IYT2; -.
DR OpenTargets; ENSG00000180917; -.
DR PharmGKB; PA162389041; -.
DR VEuPathDB; HostDB:ENSG00000180917; -.
DR eggNOG; KOG3674; Eukaryota.
DR GeneTree; ENSGT00940000161773; -.
DR HOGENOM; CLU_019427_0_0_1; -.
DR InParanoid; Q8IYT2; -.
DR OMA; VSPLHYC; -.
DR OrthoDB; 1327262at2759; -.
DR PhylomeDB; Q8IYT2; -.
DR TreeFam; TF314897; -.
DR BioCyc; MetaCyc:ENSG00000180917-MON; -.
DR BRENDA; 2.1.1.296; 2681.
DR PathwayCommons; Q8IYT2; -.
DR SignaLink; Q8IYT2; -.
DR BioGRID-ORCS; 55783; 70 hits in 1066 CRISPR screens.
DR ChiTaRS; CMTR2; human.
DR GenomeRNAi; 55783; -.
DR Pharos; Q8IYT2; Tbio.
DR PRO; PR:Q8IYT2; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8IYT2; protein.
DR Bgee; ENSG00000180917; Expressed in germinal epithelium of ovary and 187 other tissues.
DR ExpressionAtlas; Q8IYT2; baseline and differential.
DR Genevisible; Q8IYT2; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
DR GO; GO:0097309; P:cap1 mRNA methylation; IBA:GO_Central.
DR GO; GO:0097310; P:cap2 mRNA methylation; IDA:UniProtKB.
DR InterPro; IPR025807; Adrift-typ_MeTrfase.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01728; FtsJ; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51614; SAM_MT_ADRIFT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..770
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 2"
FT /id="PRO_0000326180"
FT DOMAIN 109..322
FT /note="Adrift-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT ACT_SITE 117
FT /evidence="ECO:0000305|PubMed:21310715"
FT ACT_SITE 235
FT /evidence="ECO:0000305|PubMed:21310715"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946,
FT ECO:0000305|PubMed:21310715"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT BINDING 167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT BINDING 235
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00946"
FT VARIANT 60
FT /note="L -> F (in dbSNP:rs3096380)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3"
FT /id="VAR_039998"
FT VARIANT 163
FT /note="F -> Y (in dbSNP:rs17853360)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039999"
FT VARIANT 416
FT /note="N -> S (in dbSNP:rs3803704)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_040000"
FT VARIANT 608
FT /note="T -> K (in dbSNP:rs3096381)"
FT /id="VAR_040001"
FT VARIANT 753
FT /note="F -> L (in dbSNP:rs16970857)"
FT /id="VAR_040002"
FT MUTAGEN 74
FT /note="K->A: Strongly reduces mRNA cap binding and
FT catalytic activity of the enzyme."
FT /evidence="ECO:0000269|PubMed:24402442"
FT MUTAGEN 77
FT /note="L->A: Strongly reduces mRNA cap binding and
FT catalytic activity of the enzyme."
FT /evidence="ECO:0000269|PubMed:24402442"
FT MUTAGEN 78
FT /note="S->A: Only mildly affects mRNA cap binding and
FT catalytic activity of the enzyme."
FT /evidence="ECO:0000269|PubMed:24402442"
FT MUTAGEN 85
FT /note="W->A: Strongly reduces mRNA cap binding and
FT catalytic activity of the enzyme."
FT /evidence="ECO:0000269|PubMed:24402442"
FT MUTAGEN 86
FT /note="H->A: Only mildly affects mRNA cap binding and
FT catalytic activity of the enzyme."
FT /evidence="ECO:0000269|PubMed:24402442"
FT MUTAGEN 89
FT /note="T->A: Strongly reduces mRNA cap binding and
FT catalytic activity of the enzyme."
FT /evidence="ECO:0000269|PubMed:24402442"
FT MUTAGEN 113
FT /note="Q->A: Only mildly affects mRNA cap binding and
FT catalytic activity of the enzyme."
FT /evidence="ECO:0000269|PubMed:24402442"
FT MUTAGEN 117
FT /note="K->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21310715"
FT MUTAGEN 142
FT /note="H->A: Strongly reduces mRNA cap binding and
FT catalytic activity of the enzyme."
FT /evidence="ECO:0000269|PubMed:24402442"
FT MUTAGEN 145
FT /note="E->A: Strongly reduces mRNA cap binding and
FT catalytic activity of the enzyme."
FT /evidence="ECO:0000269|PubMed:24402442"
FT MUTAGEN 235
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21310715"
FT MUTAGEN 275
FT /note="K->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21310715"
FT MUTAGEN 307
FT /note="K->A: Strongly reduces mRNA cap binding and
FT catalytic activity of the enzyme."
FT /evidence="ECO:0000269|PubMed:24402442"
FT CONFLICT 27
FT /note="F -> L (in Ref. 5; AAM49718)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="F -> Y (in Ref. 5; AAM49718)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="D -> E (in Ref. 5; AAM49718)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="N -> K (in Ref. 5; AAM49718)"
FT /evidence="ECO:0000305"
FT CONFLICT 85..86
FT /note="WH -> LD (in Ref. 5; AAM49718)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..202
FT /note="YF -> HL (in Ref. 5; AAM49718)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="F -> I (in Ref. 5; AAM49718)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="C -> S (in Ref. 5; AAM49718)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="C -> S (in Ref. 1; BAA92047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 770 AA; 88120 MW; E5BE4A2B31AE3580 CRC64;
MSKCRKTPVQ QLASPASFSP DILADIFELF AKNFSYGKPL NNEWQLPDPS EIFTCDHTEL
NAFLDLKNSL NEVKNLLSDK KLDEWHEHTA FTNKAGKIIS HVRKSVNAEL CTQAWCKFHE
ILCSFPLIPQ EAFQNGKLNS LHLCEAPGAF IASLNHYLKS HRFPCHWSWV ANTLNPYHEA
NDDLMMIMDD RLIANTLHWW YFGPDNTGDI MTLKFLTGLQ NFISSMATVH LVTADGSFDC
QGNPGEQEAL VSSLHYCEVV TALTTLGNGG SFVLKMFTMF EHCSINLMYL LNCCFDQVHV
FKPATSKAGN SEVYVVCLHY KGREAIHPLL SKMTLNFGTE MKRKALFPHH VIPDSFLKRH
EECCVFFHKY QLETISENIR LFECMGKAEQ EKLNNLRDCA IQYFMQKFQL KHLSRNNWLV
KKSSIGCSTN TKWFGQRNKY FKTYNERKML EALSWKDKVA KGYFNSWAEE HGVYHPGQSS
ILEGTASNLE CHLWHILEGK KLPKVKCSPF CNGEILKTLN EAIEKSLGGA FNLDSKFRPK
QQYSCSCHVF SEELIFSELC SLTECLQDEQ VVVPSNQIKC LLVGFSTLRN IKMHIPLEVR
LLESAELTTF SCSLLHDGDP TYQRLFLDCL LHSLRELHTG DVMILPVLSC FTRFMAGLIF
VLHSCFRFIT FVCPTSSDPL RTCAVLLCVG YQDLPNPVFR YLQSVNELLS TLLNSDSPQQ
VLQFVPMEVL LKGALLDFLW DLNAAIAKRH LHFIIQRERE EIINSLQLQN
