QTRT2_HUMAN
ID QTRT2_HUMAN Reviewed; 415 AA.
AC Q9H974; A6NGE9; B7Z472; B7Z5R2; J3KR78; Q6IA59;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Queuine tRNA-ribosyltransferase accessory subunit 2 {ECO:0000255|HAMAP-Rule:MF_03043};
DE AltName: Full=Queuine tRNA-ribosyltransferase domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03043};
GN Name=QTRT2 {ECO:0000255|HAMAP-Rule:MF_03043}; Synonyms=QTRTD1;
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; 2 AND 3).
RC TISSUE=Tongue;
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 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph, 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 [7]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20354154; DOI=10.1261/rna.1997610;
RA Chen Y.C., Kelly V.P., Stachura S.V., Garcia G.A.;
RT "Characterization of the human tRNA-guanine transglycosylase: confirmation
RT of the heterodimeric subunit structure.";
RL RNA 16:958-968(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 SUBUNIT.
RX PubMed=30149595; DOI=10.3390/biom8030081;
RA Johannsson S., Neumann P., Ficner R.;
RT "Crystal Structure of the Human tRNA Guanine Transglycosylase Catalytic
RT Subunit QTRT1.";
RL Biomolecules 8:0-0(2018).
CC -!- FUNCTION: Non-catalytic subunit of the queuine tRNA-ribosyltransferase
CC (TGT) that catalyzes the base-exchange of a guanine (G) residue with
CC queuine (Q) at position 34 (anticodon wobble position) in tRNAs with
CC GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the
CC hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
CC cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). {ECO:0000255|HAMAP-
CC Rule:MF_03043}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03043};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03043};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit QTRT1 and an accessory
CC subunit QTRT2. {ECO:0000255|HAMAP-Rule:MF_03043,
CC ECO:0000269|PubMed:20354154, ECO:0000269|PubMed:30149595}.
CC -!- INTERACTION:
CC Q9H974; Q9BXR0: QTRT1; NbExp=2; IntAct=EBI-1221028, EBI-716832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03043}.
CC Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03043};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03043};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03043}. Note=May associate
CC with the mitochondrion outer membrane. {ECO:0000255|HAMAP-
CC Rule:MF_03043}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H974-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H974-2; Sequence=VSP_045140;
CC Name=3;
CC IsoId=Q9H974-3; Sequence=VSP_045141;
CC Name=4;
CC IsoId=Q9H974-4; Sequence=VSP_046859;
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC QTRT2 subfamily. {ECO:0000255|HAMAP-Rule:MF_03043}.
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DR EMBL; AK023022; BAB14361.1; -; mRNA.
DR EMBL; AK296938; BAH12458.1; -; mRNA.
DR EMBL; AK299313; BAH12998.1; -; mRNA.
DR EMBL; CR457296; CAG33577.1; -; mRNA.
DR EMBL; AL833709; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC092896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC128687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79613.1; -; Genomic_DNA.
DR EMBL; BC034559; AAH34559.1; -; mRNA.
DR EMBL; BC039265; AAH39265.1; -; mRNA.
DR CCDS; CCDS33828.1; -. [Q9H974-1]
DR CCDS; CCDS58844.1; -. [Q9H974-4]
DR CCDS; CCDS58845.1; -. [Q9H974-3]
DR CCDS; CCDS58846.1; -. [Q9H974-2]
DR RefSeq; NP_001243764.1; NM_001256835.1. [Q9H974-4]
DR RefSeq; NP_001243765.1; NM_001256836.1. [Q9H974-3]
DR RefSeq; NP_001243766.1; NM_001256837.1. [Q9H974-2]
DR RefSeq; NP_078914.1; NM_024638.3. [Q9H974-1]
DR RefSeq; XP_005247827.1; XM_005247770.3. [Q9H974-2]
DR RefSeq; XP_016862671.1; XM_017007182.1. [Q9H974-2]
DR RefSeq; XP_016862672.1; XM_017007183.1. [Q9H974-2]
DR PDB; 7NQ4; X-ray; 2.88 A; B=1-415.
DR PDBsum; 7NQ4; -.
DR AlphaFoldDB; Q9H974; -.
DR SMR; Q9H974; -.
DR BioGRID; 122812; 47.
DR ComplexPortal; CPX-6662; tRNA-guanine transglycosylase complex.
DR IntAct; Q9H974; 9.
DR STRING; 9606.ENSP00000420682; -.
DR GlyGen; Q9H974; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H974; -.
DR PhosphoSitePlus; Q9H974; -.
DR BioMuta; QTRT2; -.
DR DMDM; 74752736; -.
DR EPD; Q9H974; -.
DR jPOST; Q9H974; -.
DR MassIVE; Q9H974; -.
DR MaxQB; Q9H974; -.
DR PaxDb; Q9H974; -.
DR PeptideAtlas; Q9H974; -.
DR PRIDE; Q9H974; -.
DR ProteomicsDB; 6576; -.
DR ProteomicsDB; 6713; -.
DR ProteomicsDB; 81289; -. [Q9H974-1]
DR Antibodypedia; 32626; 120 antibodies from 20 providers.
DR DNASU; 79691; -.
DR Ensembl; ENST00000281273.8; ENSP00000281273.4; ENSG00000151576.10. [Q9H974-1]
DR Ensembl; ENST00000479882.5; ENSP00000418056.1; ENSG00000151576.10. [Q9H974-2]
DR Ensembl; ENST00000485050.5; ENSP00000420682.1; ENSG00000151576.10. [Q9H974-4]
DR Ensembl; ENST00000493014.1; ENSP00000419169.1; ENSG00000151576.10. [Q9H974-3]
DR GeneID; 79691; -.
DR KEGG; hsa:79691; -.
DR MANE-Select; ENST00000281273.8; ENSP00000281273.4; NM_024638.4; NP_078914.1.
DR UCSC; uc003eay.5; human. [Q9H974-1]
DR CTD; 79691; -.
DR GeneCards; QTRT2; -.
DR HGNC; HGNC:25771; QTRT2.
DR HPA; ENSG00000151576; Low tissue specificity.
DR neXtProt; NX_Q9H974; -.
DR OpenTargets; ENSG00000151576; -.
DR PharmGKB; PA134925851; -.
DR VEuPathDB; HostDB:ENSG00000151576; -.
DR eggNOG; KOG3909; Eukaryota.
DR GeneTree; ENSGT00530000063679; -.
DR HOGENOM; CLU_037350_0_0_1; -.
DR InParanoid; Q9H974; -.
DR OrthoDB; 883398at2759; -.
DR PhylomeDB; Q9H974; -.
DR TreeFam; TF317105; -.
DR BioCyc; MetaCyc:HS07747-MON; -.
DR BRENDA; 2.4.2.64; 2681.
DR PathwayCommons; Q9H974; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q9H974; -.
DR BioGRID-ORCS; 79691; 5 hits in 1065 CRISPR screens.
DR ChiTaRS; QTRT2; human.
DR GenomeRNAi; 79691; -.
DR Pharos; Q9H974; Tbio.
DR PRO; PR:Q9H974; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9H974; protein.
DR Bgee; ENSG00000151576; Expressed in adrenal tissue and 166 other tissues.
DR ExpressionAtlas; Q9H974; baseline and differential.
DR Genevisible; Q9H974; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:1990234; C:transferase complex; IPI:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IDA:UniProtKB.
DR Gene3D; 3.20.20.105; -; 1.
DR HAMAP; MF_03043; QTRT2; 1.
DR InterPro; IPR028592; QTRTD1.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; SSF51713; 1.
DR TIGRFAMs; TIGR00449; tgt_general; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..415
FT /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT /id="PRO_0000295633"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT VAR_SEQ 1..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045140"
FT VAR_SEQ 1..111
FT /note="MKLSLTKVVNGCRLGKIKNLGKTGDHTMDIPGCLLYTKTGSAPHLTHHTLHN
FT IHGVPAMAQLTLSSLAEHHEVLTEYKEGVGKFIGMPESLLYCSLHDPVSPCPAGYVTNK
FT -> MVCWQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045141"
FT VAR_SEQ 1
FT /note="M -> MVCWQDLEESLRM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_046859"
FT CONFLICT 246
FT /note="D -> G (in Ref. 2; CAG33577)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 157..180
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:7NQ4"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 361..369
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 373..399
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 403..410
FT /evidence="ECO:0007829|PDB:7NQ4"
SQ SEQUENCE 415 AA; 46713 MW; C9447FD900DD667B CRC64;
MKLSLTKVVN GCRLGKIKNL GKTGDHTMDI PGCLLYTKTG SAPHLTHHTL HNIHGVPAMA
QLTLSSLAEH HEVLTEYKEG VGKFIGMPES LLYCSLHDPV SPCPAGYVTN KSVSVWSVAG
RVEMTVSKFM AIQKALQPDW FQCLSDGEVS CKEATSIKRV RKSVDRSLLF LDNCLRLQEE
SEVLQKSVII GVIEGGDVME ERLRSARETA KRPVGGFLLD GFQGNPTTLE ARLRLLSSVT
AELPEDKPRL ISGVSRPDEV LECIERGVDL FESFFPYQVT ERGCALTFSF DYQPNPEETL
LQQNGTQEEI KCMDQIKKIE TTGCNQEITS FEINLKEKKY QEDFNPLVRG CSCYCCKNHT
RAYIHHLLVT NELLAGVLLM MHNFEHYFGF FHYIREALKS DKLAQLKELI HRQAS
