MET15_HUMAN
ID MET15_HUMAN Reviewed; 407 AA.
AC A6NJ78; A8MRS5; B7WNU2; Q3MHD3; Q8N601; Q8NBA7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=12S rRNA N4-methylcytidine (m4C) methyltransferase;
DE Short=12S rRNA m4C methyltransferase;
DE EC=2.1.1.- {ECO:0000269|PubMed:31665743, ECO:0000269|PubMed:32371392};
DE AltName: Full=Methyltransferase 5 domain-containing protein 1;
DE AltName: Full=Methyltransferase-like protein 15;
DE Flags: Precursor;
GN Name=METTL15 {ECO:0000303|PubMed:31665743, ECO:0000312|HGNC:HGNC:26606};
GN Synonyms=METT5D1;
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] (ISOFORM 2), AND VARIANT LYS-31.
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=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP LYS-31.
RC TISSUE=Brain, and 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP 119-ASP-ARG-120 AND GLU-298.
RX PubMed=31665743; DOI=10.1093/nar/gkz735;
RA Van Haute L., Hendrick A.G., D'Souza A.R., Powell C.A., Rebelo-Guiomar P.,
RA Harbour M.E., Ding S., Fearnley I.M., Andrews B., Minczuk M.;
RT "METTL15 introduces N4-methylcytidine into human mitochondrial 12S rRNA and
RT is required for mitoribosome biogenesis.";
RL Nucleic Acids Res. 47:10267-10281(2019).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 98-GLY--GLY-101.
RX PubMed=32371392; DOI=10.1074/jbc.ra119.012127;
RA Chen H., Shi Z., Guo J., Chang K.J., Chen Q., Yao C.H., Haigis M.C.,
RA Shi Y.;
RT "The human mitochondrial 12S rRNA m4C methyltransferase METTL15 is required
RT for mitochondrial function.";
RL J. Biol. Chem. 295:8505-8513(2020).
CC -!- FUNCTION: N4-methylcytidine (m4C) methyltransferase responsible for the
CC methylation of position C839 in mitochondrial 12S rRNA
CC (PubMed:31665743, PubMed:32371392). Involved in the stabilization of
CC 12S rRNA folding, therefore facilitating the assembly of the
CC mitochondrial small ribosomal subunits (PubMed:31665743,
CC PubMed:32371392). {ECO:0000269|PubMed:31665743,
CC ECO:0000269|PubMed:32371392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(839) in 12S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(4)-methylcytidine(839) in 12S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:62524, Rhea:RHEA-COMP:16109, Rhea:RHEA-COMP:16110,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74506, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:31665743, ECO:0000269|PubMed:32371392};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62525;
CC Evidence={ECO:0000269|PubMed:31665743, ECO:0000269|PubMed:32371392};
CC -!- INTERACTION:
CC A6NJ78-4; P55212: CASP6; NbExp=3; IntAct=EBI-10174029, EBI-718729;
CC A6NJ78-4; Q96AQ7: CIDEC; NbExp=3; IntAct=EBI-10174029, EBI-14151404;
CC A6NJ78-4; P33240: CSTF2; NbExp=3; IntAct=EBI-10174029, EBI-711360;
CC A6NJ78-4; G5E9A7: DMWD; NbExp=3; IntAct=EBI-10174029, EBI-10976677;
CC A6NJ78-4; P41091: EIF2S3; NbExp=3; IntAct=EBI-10174029, EBI-1054228;
CC A6NJ78-4; Q9NW38: FANCL; NbExp=3; IntAct=EBI-10174029, EBI-2339898;
CC A6NJ78-4; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-10174029, EBI-10226858;
CC A6NJ78-4; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-10174029, EBI-748515;
CC A6NJ78-4; P31273: HOXC8; NbExp=3; IntAct=EBI-10174029, EBI-1752118;
CC A6NJ78-4; P13473-2: LAMP2; NbExp=3; IntAct=EBI-10174029, EBI-21591415;
CC A6NJ78-4; O60336: MAPKBP1; NbExp=3; IntAct=EBI-10174029, EBI-947402;
CC A6NJ78-4; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-10174029, EBI-10699187;
CC A6NJ78-4; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-10174029, EBI-11750983;
CC A6NJ78-4; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-10174029, EBI-724639;
CC A6NJ78-4; O75360: PROP1; NbExp=3; IntAct=EBI-10174029, EBI-9027467;
CC A6NJ78-4; P62826: RAN; NbExp=3; IntAct=EBI-10174029, EBI-286642;
CC A6NJ78-4; P49591: SARS1; NbExp=3; IntAct=EBI-10174029, EBI-1053431;
CC A6NJ78-4; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-10174029, EBI-11959123;
CC A6NJ78-4; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-10174029, EBI-5235340;
CC A6NJ78-4; Q15645: TRIP13; NbExp=6; IntAct=EBI-10174029, EBI-358993;
CC A6NJ78-4; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-10174029, EBI-739895;
CC A6NJ78-4; Q08AM6: VAC14; NbExp=3; IntAct=EBI-10174029, EBI-2107455;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:31665743, ECO:0000269|PubMed:32371392}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A6NJ78-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6NJ78-2; Sequence=VSP_028973, VSP_028974;
CC Name=3;
CC IsoId=A6NJ78-3; Sequence=VSP_028970, VSP_028971;
CC Name=4;
CC IsoId=A6NJ78-4; Sequence=VSP_028972, VSP_028975;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30997.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK091298; BAC03631.1; -; mRNA.
DR EMBL; AC023206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68267.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68266.1; -; Genomic_DNA.
DR EMBL; BC030997; AAH30997.1; ALT_INIT; mRNA.
DR EMBL; BC105287; AAI05288.1; -; mRNA.
DR CCDS; CCDS31450.1; -. [A6NJ78-2]
DR CCDS; CCDS44559.1; -. [A6NJ78-1]
DR CCDS; CCDS73269.1; -. [A6NJ78-4]
DR RefSeq; NP_001107000.1; NM_001113528.1. [A6NJ78-1]
DR RefSeq; NP_001284704.1; NM_001297775.1. [A6NJ78-4]
DR RefSeq; NP_689849.2; NM_152636.2. [A6NJ78-2]
DR RefSeq; XP_016872786.1; XM_017017297.1. [A6NJ78-1]
DR AlphaFoldDB; A6NJ78; -.
DR SMR; A6NJ78; -.
DR BioGRID; 128190; 298.
DR IntAct; A6NJ78; 41.
DR STRING; 9606.ENSP00000384369; -.
DR GlyGen; A6NJ78; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A6NJ78; -.
DR PhosphoSitePlus; A6NJ78; -.
DR BioMuta; METTL15; -.
DR EPD; A6NJ78; -.
DR jPOST; A6NJ78; -.
DR MassIVE; A6NJ78; -.
DR MaxQB; A6NJ78; -.
DR PaxDb; A6NJ78; -.
DR PeptideAtlas; A6NJ78; -.
DR PRIDE; A6NJ78; -.
DR ProteomicsDB; 1313; -. [A6NJ78-1]
DR ProteomicsDB; 1314; -. [A6NJ78-2]
DR ProteomicsDB; 1315; -. [A6NJ78-3]
DR ProteomicsDB; 1316; -. [A6NJ78-4]
DR Antibodypedia; 25483; 44 antibodies from 15 providers.
DR DNASU; 196074; -.
DR Ensembl; ENST00000303459.10; ENSP00000307251.6; ENSG00000169519.21. [A6NJ78-2]
DR Ensembl; ENST00000406787.7; ENSP00000385507.3; ENSG00000169519.21. [A6NJ78-4]
DR Ensembl; ENST00000407364.8; ENSP00000384369.3; ENSG00000169519.21. [A6NJ78-1]
DR Ensembl; ENST00000437814.1; ENSP00000392806.1; ENSG00000169519.21. [A6NJ78-3]
DR GeneID; 196074; -.
DR KEGG; hsa:196074; -.
DR MANE-Select; ENST00000407364.8; ENSP00000384369.3; NM_001113528.2; NP_001107000.1.
DR UCSC; uc001mse.3; human. [A6NJ78-1]
DR CTD; 196074; -.
DR DisGeNET; 196074; -.
DR GeneCards; METTL15; -.
DR HGNC; HGNC:26606; METTL15.
DR HPA; ENSG00000169519; Low tissue specificity.
DR MIM; 618711; gene.
DR neXtProt; NX_A6NJ78; -.
DR OpenTargets; ENSG00000169519; -.
DR PharmGKB; PA142671458; -.
DR VEuPathDB; HostDB:ENSG00000169519; -.
DR eggNOG; KOG2782; Eukaryota.
DR GeneTree; ENSGT00390000014756; -.
DR HOGENOM; CLU_038422_1_0_1; -.
DR InParanoid; A6NJ78; -.
DR OMA; NPAKRTF; -.
DR OrthoDB; 809593at2759; -.
DR PhylomeDB; A6NJ78; -.
DR TreeFam; TF106425; -.
DR PathwayCommons; A6NJ78; -.
DR SignaLink; A6NJ78; -.
DR BioGRID-ORCS; 196074; 78 hits in 1043 CRISPR screens.
DR ChiTaRS; METTL15; human.
DR GenomeRNAi; 196074; -.
DR Pharos; A6NJ78; Tdark.
DR PRO; PR:A6NJ78; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; A6NJ78; protein.
DR Bgee; ENSG00000169519; Expressed in adrenal tissue and 175 other tissues.
DR ExpressionAtlas; A6NJ78; baseline and differential.
DR Genevisible; A6NJ78; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0070475; P:rRNA base methylation; IDA:UniProtKB.
DR Gene3D; 1.10.150.170; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01007; 16SrRNA_methyltr_H; 1.
DR InterPro; IPR002903; RsmH.
DR InterPro; IPR023397; SAM-dep_MeTrfase_MraW_recog.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11265; PTHR11265; 1.
DR Pfam; PF01795; Methyltransf_5; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF81799; SSF81799; 1.
DR TIGRFAMs; TIGR00006; TIGR00006; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Mitochondrion; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..407
FT /note="12S rRNA N4-methylcytidine (m4C) methyltransferase"
FT /id="PRO_0000308332"
FT BINDING 100..102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT BINDING 146
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT BINDING 169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 91..99
FT /note="IFLDMTFGS -> SLGVRSVGI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028970"
FT VAR_SEQ 100..407
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028971"
FT VAR_SEQ 201..320
FT /note="YPDMPTAADVVNALDQQALASILRTYGEEKHAKKIASAIVQARSIYPITRTQ
FT QLASIVAGAFPPSAIYTRKDLLQRSTHIATKTFQALRIFVNNELNELYTGLKTAQKFLR
FT PGGRLVALS -> STGTCIYPKNIRGGEACQENRFSNCSGTQHLPHHQNPAACQHRCRS
FT ISSLCYLYTERLTTAIYPYCHQDFPGSSHICEQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028972"
FT VAR_SEQ 260..273
FT /note="GAFPPSAIYTRKDL -> EYSETYFPVAQTLY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028973"
FT VAR_SEQ 274..407
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028974"
FT VAR_SEQ 321..407
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028975"
FT VARIANT 31
FT /note="N -> K (in dbSNP:rs2883478)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_036801"
FT VARIANT 149
FT /note="A -> T (in dbSNP:rs11823114)"
FT /id="VAR_036802"
FT VARIANT 267
FT /note="I -> F (in dbSNP:rs11030280)"
FT /id="VAR_059446"
FT MUTAGEN 98..101
FT /note="GSGG->ASAA: Abolished methylation of 12S rRNA
FT position C839."
FT /evidence="ECO:0000269|PubMed:32371392"
FT MUTAGEN 119..120
FT /note="DR->AA: Absence of methylation of 12S rRNA position
FT C839 and decreased methylation at position C841."
FT /evidence="ECO:0000269|PubMed:31665743"
FT MUTAGEN 298
FT /note="E->A: Decreased methylation of 12S rRNA positions
FT C839 and C841."
FT /evidence="ECO:0000269|PubMed:31665743"
FT CONFLICT 191
FT /note="P -> S (in Ref. 4; AAH30997)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="M -> V (in Ref. 1; BAC03631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 46121 MW; 1DA02B5842483080 CRC64;
MLRYPYFCRM YKECLSCWLE SGIPNLGVWP NRIHTTAEKY REYEAREQTD QTQAQELHRS
QDRDFETMAK LHIPVMVDEV VHCLSPQKGQ IFLDMTFGSG GHTKAILQKE SDIVLYALDR
DPTAYALAEH LSELYPKQIR AMLGQFSQAE ALLMKAGVQP GTFDGVLMDL GCSSMQLDTP
ERGFSLRKDG PLDMRMDGGR YPDMPTAADV VNALDQQALA SILRTYGEEK HAKKIASAIV
QARSIYPITR TQQLASIVAG AFPPSAIYTR KDLLQRSTHI ATKTFQALRI FVNNELNELY
TGLKTAQKFL RPGGRLVALS FHSLEDRIVK RFLLGISMTE RFNLSVRQQV MKTSQLGSDH
ENTEEVSMRR APLMWELIHK KVLSPQDQDV QDNPRGRSAK LRAAIKL
