TRM6_HUMAN
ID TRM6_HUMAN Reviewed; 497 AA.
AC Q9UJA5; B4DUV6; Q76P92; Q9BQV5; Q9ULR7; Q9Y2Z8;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6;
DE AltName: Full=mRNA methyladenosine-N(1)-methyltransferase non-catalytic subunit TRM6 {ECO:0000303|PubMed:29072297};
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM6;
DE Short=tRNA(m1A58)MTase subunit TRM6;
GN Name=TRMT6; Synonyms=KIAA1153, TRM6; ORFNames=CGI-09;
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 TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLY-299.
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP GLY-299.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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, AND SUBUNIT.
RX PubMed=16043508; DOI=10.1261/rna.5040605;
RA Ozanick S., Krecic A., Andersland J., Anderson J.T.;
RT "The bipartite structure of the tRNA m1A58 methyltransferase from S.
RT cerevisiae is conserved in humans.";
RL RNA 11:1281-1290(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-305, 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 [10]
RP FUNCTION.
RX PubMed=29107537; DOI=10.1016/j.molcel.2017.10.019;
RA Li X., Xiong X., Zhang M., Wang K., Chen Y., Zhou J., Mao Y., Lv J., Yi D.,
RA Chen X.W., Wang C., Qian S.B., Yi C.;
RT "Base-resolution mapping reveals distinct m1A methylome in nuclear- and
RT mitochondrial-encoded transcripts.";
RL Mol. Cell 0:0-0(2017).
RN [11]
RP FUNCTION.
RX PubMed=29072297; DOI=10.1038/nature24456;
RA Safra M., Sas-Chen A., Nir R., Winkler R., Nachshon A., Bar-Yaacov D.,
RA Erlacher M., Rossmanith W., Stern-Ginossar N., Schwartz S.;
RT "The m(1)A landscape on cytosolic and mitochondrial mRNA at single-base
RT resolution.";
RL Nature 551:251-255(2017).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH TRMT61A.
RX PubMed=26470919; DOI=10.1016/j.jmb.2015.10.005;
RA Finer-Moore J., Czudnochowski N., O'Connell J.D. III, Wang A.L.,
RA Stroud R.M.;
RT "Crystal structure of the human tRNA m(1)A58 methyltransferase-tRNA(3)(Lys)
RT complex: refolding of substrate tRNA allows access to the methylation
RT target.";
RL J. Mol. Biol. 427:3862-3876(2015).
CC -!- FUNCTION: Substrate-binding subunit of tRNA (adenine-N(1)-)-
CC methyltransferase, which catalyzes the formation of N(1)-methyladenine
CC at position 58 (m1A58) in initiator methionyl-tRNA (PubMed:16043508).
CC Together with the TRMT61A catalytic subunit, part of a mRNA N(1)-
CC methyltransferase complex that mediates methylation of adenosine
CC residues at the N(1) position of a small subset of mRNAs: N(1)
CC methylation takes place in tRNA T-loop-like structures of mRNAs and is
CC only present at low stoichiometries (PubMed:29107537, PubMed:29072297).
CC {ECO:0000269|PubMed:16043508, ECO:0000269|PubMed:29072297,
CC ECO:0000269|PubMed:29107537}.
CC -!- SUBUNIT: Heterotetramer; composed of two copies of TRMT6 and two copies
CC of TRMT61A. {ECO:0000269|PubMed:26470919, ECO:0000305|PubMed:16043508}.
CC -!- INTERACTION:
CC Q9UJA5; Q92993: KAT5; NbExp=3; IntAct=EBI-934061, EBI-399080;
CC Q9UJA5; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-934061, EBI-11742507;
CC Q9UJA5; P62937-2: PPIA; NbExp=3; IntAct=EBI-934061, EBI-25884072;
CC Q9UJA5; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-934061, EBI-9090795;
CC Q9UJA5; Q96FX7: TRMT61A; NbExp=2; IntAct=EBI-934061, EBI-934042;
CC Q9UJA5; P61981: YWHAG; NbExp=3; IntAct=EBI-934061, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P41814}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UJA5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJA5-2; Sequence=VSP_018025;
CC Name=3;
CC IsoId=Q9UJA5-3; Sequence=VSP_031100, VSP_031101;
CC Name=4;
CC IsoId=Q9UJA5-4; Sequence=VSP_054740;
CC -!- TISSUE SPECIFICITY: Expressed in brain, liver, testis and ovary.
CC {ECO:0000269|PubMed:10574461}.
CC -!- SIMILARITY: Belongs to the TRM6/GCD10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86467.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA86467.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB032979; BAA86467.1; ALT_INIT; mRNA.
DR EMBL; AF132943; AAD27718.1; ALT_FRAME; mRNA.
DR EMBL; AK000613; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK300812; BAG62468.1; -; mRNA.
DR EMBL; AL035461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001262; AAH01262.1; -; mRNA.
DR CCDS; CCDS13093.1; -. [Q9UJA5-1]
DR CCDS; CCDS63225.1; -. [Q9UJA5-4]
DR RefSeq; NP_001268396.1; NM_001281467.1. [Q9UJA5-4]
DR RefSeq; NP_057023.2; NM_015939.4. [Q9UJA5-1]
DR PDB; 5CCB; X-ray; 2.00 A; B=1-497.
DR PDB; 5CCX; X-ray; 2.10 A; B=1-497.
DR PDB; 5CD1; X-ray; 3.60 A; B/E=1-497.
DR PDBsum; 5CCB; -.
DR PDBsum; 5CCX; -.
DR PDBsum; 5CD1; -.
DR AlphaFoldDB; Q9UJA5; -.
DR SMR; Q9UJA5; -.
DR BioGRID; 119634; 78.
DR ComplexPortal; CPX-6269; tRNA (adenine(58)-N(1))-methyltransferase complex.
DR IntAct; Q9UJA5; 28.
DR MINT; Q9UJA5; -.
DR STRING; 9606.ENSP00000203001; -.
DR iPTMnet; Q9UJA5; -.
DR PhosphoSitePlus; Q9UJA5; -.
DR BioMuta; TRMT6; -.
DR DMDM; 74753354; -.
DR EPD; Q9UJA5; -.
DR jPOST; Q9UJA5; -.
DR MassIVE; Q9UJA5; -.
DR MaxQB; Q9UJA5; -.
DR PaxDb; Q9UJA5; -.
DR PeptideAtlas; Q9UJA5; -.
DR PRIDE; Q9UJA5; -.
DR ProteomicsDB; 5222; -.
DR ProteomicsDB; 84613; -. [Q9UJA5-1]
DR ProteomicsDB; 84614; -. [Q9UJA5-2]
DR ProteomicsDB; 84615; -. [Q9UJA5-3]
DR Antibodypedia; 23943; 93 antibodies from 19 providers.
DR DNASU; 51605; -.
DR Ensembl; ENST00000203001.7; ENSP00000203001.2; ENSG00000089195.15. [Q9UJA5-1]
DR Ensembl; ENST00000453074.6; ENSP00000392070.2; ENSG00000089195.15. [Q9UJA5-4]
DR GeneID; 51605; -.
DR KEGG; hsa:51605; -.
DR MANE-Select; ENST00000203001.7; ENSP00000203001.2; NM_015939.5; NP_057023.2.
DR UCSC; uc002wmh.3; human. [Q9UJA5-1]
DR CTD; 51605; -.
DR DisGeNET; 51605; -.
DR GeneCards; TRMT6; -.
DR HGNC; HGNC:20900; TRMT6.
DR HPA; ENSG00000089195; Low tissue specificity.
DR neXtProt; NX_Q9UJA5; -.
DR OpenTargets; ENSG00000089195; -.
DR PharmGKB; PA162407063; -.
DR VEuPathDB; HostDB:ENSG00000089195; -.
DR eggNOG; KOG1416; Eukaryota.
DR GeneTree; ENSGT00390000008327; -.
DR HOGENOM; CLU_010916_0_1_1; -.
DR InParanoid; Q9UJA5; -.
DR OMA; TFHNRTE; -.
DR OrthoDB; 543764at2759; -.
DR PhylomeDB; Q9UJA5; -.
DR TreeFam; TF314835; -.
DR BRENDA; 2.1.1.220; 2681.
DR PathwayCommons; Q9UJA5; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q9UJA5; -.
DR BioGRID-ORCS; 51605; 298 hits in 1055 CRISPR screens.
DR ChiTaRS; TRMT6; human.
DR GenomeRNAi; 51605; -.
DR Pharos; Q9UJA5; Tbio.
DR PRO; PR:Q9UJA5; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9UJA5; protein.
DR Bgee; ENSG00000089195; Expressed in secondary oocyte and 187 other tissues.
DR Genevisible; Q9UJA5; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IDA:ComplexPortal.
DR InterPro; IPR017423; TRM6.
DR PANTHER; PTHR12945; PTHR12945; 1.
DR Pfam; PF04189; Gcd10p; 1.
DR PIRSF; PIRSF038170; tRNA_m1A_mtfrase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; tRNA processing.
FT CHAIN 1..497
FT /note="tRNA (adenine(58)-N(1))-methyltransferase non-
FT catalytic subunit TRM6"
FT /id="PRO_0000233098"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94..104
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 145..154
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 175..182
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 415..423
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 434..441
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..170
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054740"
FT VAR_SEQ 344..365
FT /note="QEKQRRQEEQRKRHLEAAALLS -> SGKNRGRQGRSSGKDFWGCRFA (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10810093"
FT /id="VSP_031100"
FT VAR_SEQ 366..497
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10810093"
FT /id="VSP_031101"
FT VAR_SEQ 372..497
FT /note="LIVASRFHPTPLLLSLLDFVAPSRPFVVYCQYKEPLLECYTKLRERGGVINL
FT RLSETWLRNYQVLPDRSHPKLLMSGGGGYLLSGFTVAMDNLKADTSLKSNASTLESHET
FT EEPAAKKRKCPESDS -> CVDGRRQETPQCMWALLQTDWHSLSPCL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10574461"
FT /id="VSP_018025"
FT VARIANT 293
FT /note="E -> K (in dbSNP:rs6139876)"
FT /id="VAR_053789"
FT VARIANT 299
FT /note="E -> G (in dbSNP:rs451571)"
FT /evidence="ECO:0000269|PubMed:10810093,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_053790"
FT VARIANT 333
FT /note="P -> L (in dbSNP:rs35203742)"
FT /id="VAR_053791"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 64..74
FT /evidence="ECO:0007829|PDB:5CCX"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 140..154
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 212..221
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 342..365
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 380..387
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 396..404
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 405..417
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 420..434
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 452..458
FT /evidence="ECO:0007829|PDB:5CCB"
SQ SEQUENCE 497 AA; 55799 MW; 920800D0722A6CBB CRC64;
MEGSGEQPGP QPQHPGDHRI RDGDFVVLKR EDVFKAVQVQ RRKKVTFEKQ WFYLDNVIGH
SYGTAFEVTS GGSLQPKKKR EEPTAETKEA GTDNRNIVDD GKSQKLTQDD IKALKDKGIK
GEEIVQQLIE NSTTFRDKTE FAQDKYIKKK KKKYEAIITV VKPSTRILSI MYYAREPGKI
NHMRYDTLAQ MLTLGNIRAG NKMIVMETCA GLVLGAMMER MGGFGSIIQL YPGGGPVRAA
TACFGFPKSF LSGLYEFPLN KVDSLLHGTF SAKMLSSEPK DSALVEESNG TLEEKQASEQ
ENEDSMAEAP ESNHPEDQET METISQDPEH KGPKERGSKK DYIQEKQRRQ EEQRKRHLEA
AALLSERNAD GLIVASRFHP TPLLLSLLDF VAPSRPFVVY CQYKEPLLEC YTKLRERGGV
INLRLSETWL RNYQVLPDRS HPKLLMSGGG GYLLSGFTVA MDNLKADTSL KSNASTLESH
ETEEPAAKKR KCPESDS
