TRM2B_HUMAN
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 03-AUG-2022, entry version 169.
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, 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 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 [7]
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 -!- 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}.
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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. [Q96GJ1-1]
DR RefSeq; XP_005262253.1; XM_005262196.2. [Q96GJ1-1]
DR RefSeq; XP_006724768.1; XM_006724705.2. [Q96GJ1-1]
DR RefSeq; XP_016885351.1; XM_017029862.1. [Q96GJ1-3]
DR AlphaFoldDB; Q96GJ1; -.
DR SMR; Q96GJ1; -.
DR BioGRID; 123044; 27.
DR IntAct; Q96GJ1; 11.
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; Q96GJ1; -.
DR PeptideAtlas; Q96GJ1; -.
DR PRIDE; Q96GJ1; -.
DR ProteomicsDB; 76637; -. [Q96GJ1-1]
DR ProteomicsDB; 76638; -. [Q96GJ1-2]
DR ProteomicsDB; 76639; -. [Q96GJ1-3]
DR Antibodypedia; 28575; 163 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 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; VLNCEFI; -.
DR PhylomeDB; Q96GJ1; -.
DR TreeFam; TF352239; -.
DR PathwayCommons; Q96GJ1; -.
DR SignaLink; Q96GJ1; -.
DR BioGRID-ORCS; 79979; 13 hits in 701 CRISPR screens.
DR ChiTaRS; TRMT2B; human.
DR GenomeRNAi; 79979; -.
DR Pharos; Q96GJ1; Tbio.
DR PRO; PR:Q96GJ1; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q96GJ1; protein.
DR Bgee; ENSG00000188917; Expressed in granulocyte and 142 other tissues.
DR ExpressionAtlas; Q96GJ1; baseline and differential.
DR Genevisible; Q96GJ1; HS.
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:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR045850; TRM2_euk.
DR InterPro; IPR025823; tRNA_(uracil-5-)_MeTrfase_met.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR45904; PTHR45904; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
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
