MET2B_HUMAN
ID MET2B_HUMAN Reviewed; 378 AA.
AC Q6P1Q9; B4DZ68; Q0IJ54; Q3B7J1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=tRNA N(3)-methylcytidine methyltransferase METTL2B {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305|PubMed:28655767};
DE AltName: Full=Methyltransferase-like protein 2B {ECO:0000305};
GN Name=METTL2B {ECO:0000303|PubMed:28655767, ECO:0000312|HGNC:HGNC:18272};
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] (ISOFORMS 1 AND 2), AND VARIANT
RP ILE-266.
RC TISSUE=Retinoblastoma, and Testis;
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2-378 (ISOFORM 1), AND VARIANTS ILE-68 AND ILE-266.
RC TISSUE=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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, AND IDENTIFICATION BY
RP 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, AND IDENTIFICATION BY
RP 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 [8]
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 [9]
RP FUNCTION.
RX PubMed=21518805; DOI=10.1261/rna.2653411;
RA Noma A., Yi S., Katoh T., Takai Y., Suzuki T., Suzuki T.;
RT "Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine
RT at position 32 of tRNAs in Saccharomyces cerevisiae.";
RL RNA 17:1111-1119(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND THR-154, 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 [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28655767; DOI=10.1074/jbc.m117.798298;
RA Xu L., Liu X., Sheng N., Oo K.S., Liang J., Chionh Y.H., Xu J., Ye F.,
RA Gao Y.G., Dedon P.C., Fu X.Y.;
RT "Three distinct 3-methylcytidine (m3C) methyltransferases modify tRNA and
RT mRNA in mice and humans.";
RL J. Biol. Chem. 292:14695-14703(2017).
RN [13]
RP INTERACTION WITH DALRD3.
RX PubMed=32427860; DOI=10.1038/s41467-020-16321-6;
RA Lentini J.M., Alsaif H.S., Faqeih E., Alkuraya F.S., Fu D.;
RT "DALRD3 encodes a protein mutated in epileptic encephalopathy that targets
RT arginine tRNAs for 3-methylcytosine modification.";
RL Nat. Commun. 11:2510-2510(2020).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=34268557; DOI=10.1093/nar/gkab603;
RA Mao X.L., Li Z.H., Huang M.H., Wang J.T., Zhou J.B., Li Q.R., Xu H.,
RA Wang X.J., Zhou X.L.;
RT "Mutually exclusive substrate selection strategy by human m3C RNA
RT transferases METTL2A and METTL6.";
RL Nucleic Acids Res. 49:8309-8323(2021).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates N(3)-methylcytidine modification of residue 32 of the tRNA
CC anticodon loop of tRNA(Thr)(UGU) and tRNA(Arg)(CCU).
CC {ECO:0000269|PubMed:28655767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32) in tRNA(Thr) + S-adenosyl-L-methionine = H(+) +
CC N(3)-methylcytidine(32) in tRNA(Thr) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:50960, Rhea:RHEA-COMP:12850, Rhea:RHEA-COMP:12852,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74894, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000305|PubMed:28655767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50961;
CC Evidence={ECO:0000305|PubMed:28655767};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32) in tRNA(Arg)(CCU) + S-adenosyl-L-methionine =
CC H(+) + N(3)-methylcytidine(32) in tRNA(Arg)(CCU) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60912, Rhea:RHEA-COMP:15710, Rhea:RHEA-
CC COMP:15712, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74894, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000305|PubMed:28655767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60913;
CC Evidence={ECO:0000305|PubMed:28655767};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with DALRD3
CC (PubMed:32427860). {ECO:0000250|UniProtKB:Q96IZ6,
CC ECO:0000269|PubMed:32427860}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:34268557}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P1Q9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1Q9-2; Sequence=VSP_032816;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METL family.
CC {ECO:0000305}.
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DR EMBL; AK002212; BAA92136.1; -; mRNA.
DR EMBL; AK302775; BAG63980.1; -; mRNA.
DR EMBL; AC010655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064929; AAH64929.1; -; mRNA.
DR EMBL; BC107586; AAI07587.1; -; mRNA.
DR EMBL; BC121115; AAI21116.1; -; mRNA.
DR EMBL; BC121116; AAI21117.1; -; mRNA.
DR CCDS; CCDS5803.2; -. [Q6P1Q9-1]
DR RefSeq; NP_060866.2; NM_018396.2. [Q6P1Q9-1]
DR AlphaFoldDB; Q6P1Q9; -.
DR SMR; Q6P1Q9; -.
DR BioGRID; 120910; 16.
DR IntAct; Q6P1Q9; 6.
DR STRING; 9606.ENSP00000262432; -.
DR GlyGen; Q6P1Q9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6P1Q9; -.
DR PhosphoSitePlus; Q6P1Q9; -.
DR BioMuta; METTL2B; -.
DR DMDM; 317373413; -.
DR EPD; Q6P1Q9; -.
DR jPOST; Q6P1Q9; -.
DR MassIVE; Q6P1Q9; -.
DR MaxQB; Q6P1Q9; -.
DR PaxDb; Q6P1Q9; -.
DR PeptideAtlas; Q6P1Q9; -.
DR PRIDE; Q6P1Q9; -.
DR ProteomicsDB; 66867; -. [Q6P1Q9-1]
DR ProteomicsDB; 66868; -. [Q6P1Q9-2]
DR Antibodypedia; 31876; 136 antibodies from 22 providers.
DR DNASU; 55798; -.
DR Ensembl; ENST00000262432.13; ENSP00000262432.9; ENSG00000165055.16. [Q6P1Q9-1]
DR Ensembl; ENST00000480046.5; ENSP00000418402.1; ENSG00000165055.16. [Q6P1Q9-2]
DR GeneID; 55798; -.
DR KEGG; hsa:55798; -.
DR MANE-Select; ENST00000262432.13; ENSP00000262432.9; NM_018396.3; NP_060866.2.
DR UCSC; uc003vnf.3; human. [Q6P1Q9-1]
DR CTD; 55798; -.
DR DisGeNET; 55798; -.
DR GeneCards; METTL2B; -.
DR HGNC; HGNC:18272; METTL2B.
DR HPA; ENSG00000165055; Low tissue specificity.
DR MIM; 607846; gene.
DR neXtProt; NX_Q6P1Q9; -.
DR PharmGKB; PA134924546; -.
DR VEuPathDB; HostDB:ENSG00000165055; -.
DR eggNOG; KOG2361; Eukaryota.
DR GeneTree; ENSGT00940000156059; -.
DR HOGENOM; CLU_029724_0_1_1; -.
DR InParanoid; Q6P1Q9; -.
DR OMA; LPPHYKG; -.
DR OrthoDB; 987359at2759; -.
DR PhylomeDB; Q6P1Q9; -.
DR TreeFam; TF323232; -.
DR BRENDA; 2.1.1.268; 2681.
DR BRENDA; 2.1.1.B109; 2681.
DR PathwayCommons; Q6P1Q9; -.
DR SignaLink; Q6P1Q9; -.
DR BioGRID-ORCS; 55798; 37 hits in 649 CRISPR screens.
DR ChiTaRS; METTL2B; human.
DR GeneWiki; METTL2B; -.
DR GenomeRNAi; 55798; -.
DR Pharos; Q6P1Q9; Tbio.
DR PRO; PR:Q6P1Q9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q6P1Q9; protein.
DR Bgee; ENSG00000165055; Expressed in colonic epithelium and 107 other tissues.
DR ExpressionAtlas; Q6P1Q9; baseline and differential.
DR Genevisible; Q6P1Q9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016427; F:tRNA (cytosine) methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0052735; F:tRNA (cytosine-3-)-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026113; MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22809; PTHR22809; 1.
DR PIRSF; PIRSF037755; Mettl2_prd; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Methyltransferase;
KW Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..378
FT /note="tRNA N(3)-methylcytidine methyltransferase METTL2B"
FT /id="PRO_0000328847"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 154
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..67
FT /note="MAGSYPEGAPAILADKRQQFGSRFLSDPARVFHHNAWDNVEWSEEQAAAAER
FT KVQENSIQRVCQEKQ -> MP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032816"
FT VARIANT 68
FT /note="V -> I (in dbSNP:rs2288557)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_059465"
FT VARIANT 124
FT /note="C -> R (in dbSNP:rs2896399)"
FT /id="VAR_042547"
FT VARIANT 129
FT /note="N -> H (in dbSNP:rs2023329)"
FT /id="VAR_042548"
FT VARIANT 169
FT /note="E -> K (in dbSNP:rs1065267)"
FT /id="VAR_042549"
FT VARIANT 266
FT /note="V -> I (in dbSNP:rs2562741)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_042550"
SQ SEQUENCE 378 AA; 43426 MW; A9719EF1074BA011 CRC64;
MAGSYPEGAP AILADKRQQF GSRFLSDPAR VFHHNAWDNV EWSEEQAAAA ERKVQENSIQ
RVCQEKQVDY EINAHKYWND FYKIHENGFF KDRHWLFTEF PELAPSQNQN HLKDWFLENK
SEVCECRNNE DGPGLIMEEQ HKCSSKSLEH KTQTPPVEEN VTQKISDLEI CADEFPGSSA
TYRILEVGCG VGNTVFPILQ TNNDPGLFVY CCDFSSTAIE LVQTNSEYDP SRCFAFVHDL
CDEEKSYPVP KGSLDIIILI FVLSAVVPDK MQKAINRLSR LLKPGGMVLL RDYGRYDMAQ
LRFKKGQCLS GNFYVRGDGT RVYFFTQEEL DTLFTTAGLE KVQNLVDRRL QVNRGKQLTM
YRVWIQCKYC KPLLSSTS
