ID TRM2B_HUMAN Reviewed; 504 AA. AC Q96GJ1; A6NDG5; A6NEI9; A6NMG6; Q5JPF0; Q5JVY6; Q96HU7; Q96IH9; Q9H9K2; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 178. DE RecName: Full=tRNA (uracil-5-)-methyltransferase homolog B {ECO:0000305}; DE EC=2.1.1.35 {ECO:0000269|PubMed:31948311}; DE AltName: Full=TRM2 homolog B {ECO:0000305}; DE AltName: Full=rRNA (uracil-5-)-methyltransferase TRMT2B {ECO:0000305}; DE EC=2.1.1.- {ECO:0000269|PubMed:31948311}; DE Flags: Precursor; GN Name=TRMT2B {ECO:0000303|PubMed:31948311, GN ECO:0000312|HGNC:HGNC:25748}; GN Synonyms=CXorf34 {ECO:0000312|HGNC:HGNC:25748}; 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 1). RC TISSUE=Teratocarcinoma; 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 MRNA] (ISOFORM 3). RC TISSUE=Lymph node; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, Colon, Lymph, Placenta, and Skin; 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 [6] RP SUBCELLULAR LOCATION (ISOFORM 1). RX PubMed=27184847; DOI=10.1016/j.celrep.2016.04.064; RA Lee S.Y., Kang M.G., Park J.S., Lee G., Ting A.Y., Rhee H.W.; RT "APEX Fingerprinting Reveals the Subcellular Localization of Proteins of RT Interest."; RL Cell Rep. 15:1837-1847(2016). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=31948311; DOI=10.1080/15476286.2020.1712544; RA Powell C.A., Minczuk M.; RT "TRMT2B is responsible for both tRNA and rRNA m5U-methylation in human RT mitochondria."; RL RNA Biol. 17:451-462(2020). RN [8] RP FUNCTION. RX PubMed=34556860; DOI=10.1038/s41589-021-00874-8; RA Dai W., Li A., Yu N.J., Nguyen T., Leach R.W., Wuehr M., Kleiner R.E.; RT "Activity-based RNA-modifying enzyme probing reveals DUS3L-mediated RT dihydrouridylation."; RL Nat. Chem. Biol. 17:1178-1187(2021). CC -!- FUNCTION: Mitochondrial S-adenosyl-L-methionine-dependent CC methyltransferase that catalyzes the formation of 5-methyl-uridine in CC tRNAs and 12S rRNA (PubMed:31948311, PubMed:34556860). Catalyzes the CC methylation of uridine at position 54 (m5U54) in all tRNAs CC (PubMed:31948311). Specifically methylates the uridine in position 429 CC of 12S rRNA (m5U429) (PubMed:31948311). Does not affect RNA stability CC or mitochondrial translation (PubMed:31948311). CC {ECO:0000269|PubMed:31948311, ECO:0000269|PubMed:34556860}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-adenosyl-L-methionine + uridine(54) in tRNA = 5- CC methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:42712, Rhea:RHEA-COMP:10167, Rhea:RHEA-COMP:10193, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.35; CC Evidence={ECO:0000269|PubMed:31948311}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42713; CC Evidence={ECO:0000269|PubMed:31948311}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a uridine in 12S rRNA + S-adenosyl-L-methionine = a 5- CC methyluridine in 12S rRNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:69859, Rhea:RHEA-COMP:17791, Rhea:RHEA-COMP:17792, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; CC Evidence={ECO:0000269|PubMed:31948311}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69860; CC Evidence={ECO:0000269|PubMed:31948311}; CC -!- INTERACTION: CC Q96GJ1; P07992: ERCC1; NbExp=3; IntAct=EBI-10195625, EBI-750962; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:31948311}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion matrix CC {ECO:0000269|PubMed:27184847}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96GJ1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96GJ1-2; Sequence=VSP_029644; CC Name=3; CC IsoId=Q96GJ1-3; Sequence=VSP_029643; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE- CC ProRule:PRU01024}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK022749; BAB14223.1; -; mRNA. DR EMBL; AL832849; CAI46112.1; -; mRNA. DR EMBL; AL109952; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133275; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z97985; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471115; EAX02831.1; -; Genomic_DNA. DR EMBL; CH471115; EAX02837.1; -; Genomic_DNA. DR EMBL; BC007526; AAH07526.1; -; mRNA. DR EMBL; BC008067; AAH08067.2; -; mRNA. DR EMBL; BC009437; AAH09437.1; -; mRNA. DR EMBL; BC020116; AAH20116.1; -; mRNA. DR EMBL; BC034272; AAH34272.1; -; mRNA. DR CCDS; CCDS14477.1; -. [Q96GJ1-1] DR CCDS; CCDS55464.1; -. [Q96GJ1-3] DR RefSeq; NP_001161442.1; NM_001167970.1. [Q96GJ1-1] DR RefSeq; NP_001161443.1; NM_001167971.1. [Q96GJ1-3] DR RefSeq; NP_001161444.1; NM_001167972.1. [Q96GJ1-1] DR RefSeq; NP_079193.2; NM_024917.5. [Q96GJ1-1] DR RefSeq; XP_005262252.1; XM_005262195.2. DR RefSeq; XP_005262253.1; XM_005262196.2. [Q96GJ1-1] DR RefSeq; XP_006724768.1; XM_006724705.2. DR RefSeq; XP_016885351.1; XM_017029862.1. DR AlphaFoldDB; Q96GJ1; -. DR SMR; Q96GJ1; -. DR BioGRID; 123044; 28. DR IntAct; Q96GJ1; 12. DR STRING; 9606.ENSP00000362027; -. DR iPTMnet; Q96GJ1; -. DR PhosphoSitePlus; Q96GJ1; -. DR BioMuta; TRMT2B; -. DR DMDM; 74762656; -. DR EPD; Q96GJ1; -. DR jPOST; Q96GJ1; -. DR MassIVE; Q96GJ1; -. DR MaxQB; Q96GJ1; -. DR PaxDb; 9606-ENSP00000362027; -. DR PeptideAtlas; Q96GJ1; -. DR ProteomicsDB; 76637; -. [Q96GJ1-1] DR ProteomicsDB; 76638; -. [Q96GJ1-2] DR ProteomicsDB; 76639; -. [Q96GJ1-3] DR Pumba; Q96GJ1; -. DR Antibodypedia; 28575; 190 antibodies from 24 providers. DR DNASU; 79979; -. DR Ensembl; ENST00000372935.5; ENSP00000362026.1; ENSG00000188917.15. [Q96GJ1-1] DR Ensembl; ENST00000372936.4; ENSP00000362027.3; ENSG00000188917.15. [Q96GJ1-1] DR Ensembl; ENST00000372939.5; ENSP00000362030.1; ENSG00000188917.15. [Q96GJ1-3] DR Ensembl; ENST00000545398.5; ENSP00000438134.1; ENSG00000188917.15. [Q96GJ1-1] DR GeneID; 79979; -. DR KEGG; hsa:79979; -. DR MANE-Select; ENST00000372936.4; ENSP00000362027.3; NM_024917.6; NP_079193.2. DR UCSC; uc004egq.4; human. [Q96GJ1-1] DR AGR; HGNC:25748; -. DR CTD; 79979; -. DR GeneCards; TRMT2B; -. DR HGNC; HGNC:25748; TRMT2B. DR HPA; ENSG00000188917; Low tissue specificity. DR neXtProt; NX_Q96GJ1; -. DR OpenTargets; ENSG00000188917; -. DR PharmGKB; PA164726782; -. DR VEuPathDB; HostDB:ENSG00000188917; -. DR eggNOG; KOG2187; Eukaryota. DR GeneTree; ENSGT00530000063723; -. DR HOGENOM; CLU_014689_4_0_1; -. DR InParanoid; Q96GJ1; -. DR OMA; LHYRVIR; -. DR OrthoDB; 120922at2759; -. DR PhylomeDB; Q96GJ1; -. DR TreeFam; TF352239; -. DR PathwayCommons; Q96GJ1; -. DR SignaLink; Q96GJ1; -. DR BioGRID-ORCS; 79979; 13 hits in 774 CRISPR screens. DR ChiTaRS; TRMT2B; human. DR GenomeRNAi; 79979; -. DR Pharos; Q96GJ1; Tdark. DR PRO; PR:Q96GJ1; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q96GJ1; Protein. DR Bgee; ENSG00000188917; Expressed in granulocyte and 143 other cell types or tissues. DR ExpressionAtlas; Q96GJ1; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IDA:UniProtKB. DR GO; GO:0030697; F:tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent; IDA:UniProtKB. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 2.40.50.1070; -; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR045850; TRM2_met. DR InterPro; IPR025823; TRM2B_chor. DR InterPro; IPR010280; U5_MeTrfase_fam. DR PANTHER; PTHR45904; TRNA (URACIL-5-)-METHYLTRANSFERASE; 1. DR PANTHER; PTHR45904:SF1; TRNA (URACIL-5-)-METHYLTRANSFERASE HOMOLOG B; 1. DR Pfam; PF05958; tRNA_U5-meth_tr; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1. DR PROSITE; PS51621; SAM_MT_RNA_M5U_1; 1. DR Genevisible; Q96GJ1; HS. PE 1: Evidence at protein level; KW Alternative splicing; Methyltransferase; Mitochondrion; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase; Transit peptide; KW tRNA processing. FT TRANSIT 1..16 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 17..504 FT /note="tRNA (uracil-5-)-methyltransferase homolog B" FT /id="PRO_0000311932" FT ACT_SITE 451 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024" FT ACT_SITE 497 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P23003" FT BINDING 323 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024" FT BINDING 373 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024" FT BINDING 423 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024" FT VAR_SEQ 102..146 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_029643" FT VAR_SEQ 464..504 FT /note="LCCPPDPAKKLLGEPFVLQQAVPVDLFPHTPHCELVLLFTR -> RSLILLE FT CSGMVSAHCSLHLPGSSDSPASAS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_029644" FT VARIANT 12 FT /note="S -> R (in dbSNP:rs7064613)" FT /id="VAR_037355" FT CONFLICT 238 FT /note="H -> R (in Ref. 1; BAB14223)" FT /evidence="ECO:0000305" FT CONFLICT 451 FT /note="C -> R (in Ref. 2; CAI46112)" FT /evidence="ECO:0000305" SQ SEQUENCE 504 AA; 56476 MW; D7A28E168AC9C366 CRC64; MAGLKRRVPL HSLRYFISMV GLFSKPGLLP WYARNPPGWS QLFLGTVCKG DFTRVIATKC QKGQKSQKKP SHLGPLDGSW QERLADVVTP LWRLSYEEQL KVKFAAQKKI LQRLESYIQM LNGVSVTTAV PKSERLSCLL HPIIPSPVIN GYRNKSTFSV NRGPDGNPKT VGFYLGTWRD GNVVCVQSNH LKNIPEKHSQ VAQYYEVFLR QSPLEPCLVF HEGGYWRELT VRTNSQGHTM AIITFHPQKL SQEELHVQKE IVKEFFIRGP GAACGLTSLY FQESTMTRCS HQQSPYQLLF GEPYIFEELL SLKIRISPDA FFQINTAGAE MLYRTVGELT GVNSDTILLD ICCGTGVIGL SLAQHTSRVL GIELLEQAVE DARWTAAFNG ITNSEFHTGQ AEKILPGLLK SKEDGQSIVA VVNPARAGLH YKVIQAIRNF RAIHTLVFVS CKLHGESTRN VIELCCPPDP AKKLLGEPFV LQQAVPVDLF PHTPHCELVL LFTR //