MTEF4_HUMAN
ID MTEF4_HUMAN Reviewed; 381 AA.
AC Q7Z6M4; A8K6K0; Q9P0E0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Transcription termination factor 4, mitochondrial;
DE AltName: Full=Mitochondrial transcription termination factor 4;
DE AltName: Full=mTERF domain-containing protein 2;
DE Contains:
DE RecName: Full=mTERF domain-containing protein 2 processed;
DE Flags: Precursor;
GN Name=MTERF4; Synonyms=MTERFD2; ORFNames=HSPC096;
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].
RC TISSUE=Placenta;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-157.
RC TISSUE=Umbilical cord blood;
RA Zhang Q.-H., Ye M., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L.,
RA Fan H.Y., Mao Y.F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PARTIAL PROTEIN SEQUENCE, TRANSIT PEPTIDE CLEAVAGE SITE, PROCESSING,
RP FUNCTION, RNA-BINDING, INTERACTION WITH NSUN4, AND SUBCELLULAR LOCATION.
RX PubMed=21531335; DOI=10.1016/j.cmet.2011.04.002;
RA Camara Y., Asin-Cayuela J., Park C.B., Metodiev M.D., Shi Y.,
RA Ruzzenente B., Kukat C., Habermann B., Wibom R., Hultenby K., Franz T.,
RA Erdjument-Bromage H., Tempst P., Hallberg B.M., Gustafsson C.M.,
RA Larsson N.G.;
RT "MTERF4 regulates translation by targeting the methyltransferase NSUN4 to
RT the mammalian mitochondrial ribosome.";
RL Cell Metab. 13:527-539(2011).
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 47-381 IN COMPLEX WITH NSUN4,
RP RNA-BINDING, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=22949673; DOI=10.1073/pnas.1210688109;
RA Spahr H., Habermann B., Gustafsson C.M., Larsson N.G., Hallberg B.M.;
RT "Structure of the human MTERF4-NSUN4 protein complex that regulates
RT mitochondrial ribosome biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:15253-15258(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 122-330 IN COMPLEX WITH NSUN4,
RP MTERF REPEATS, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23022348; DOI=10.1016/j.str.2012.08.027;
RA Yakubovskaya E., Guja K.E., Mejia E., Castano S., Hambardjieva E.,
RA Choi W.S., Garcia-Diaz M.;
RT "Structure of the essential MTERF4:NSUN4 protein complex reveals how an
RT MTERF protein collaborates to facilitate rRNA modification.";
RL Structure 20:1940-1947(2012).
CC -!- FUNCTION: Regulator of mitochondrial ribosome biogenesis and
CC translation. Binds to mitochondrial ribosomal RNAs 16S, 12S and 7S and
CC targets NSUN4 RNA methyltransferase to the mitochondrial large
CC ribosomal subunit (39S). {ECO:0000269|PubMed:21531335}.
CC -!- SUBUNIT: Heterodimer with NSUN4; this interaction may be required for
CC NSUN4 recruitment to the mitochondrial large ribosomal subunit.
CC {ECO:0000269|PubMed:22949673, ECO:0000269|PubMed:23022348}.
CC -!- INTERACTION:
CC Q7Z6M4; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-948435, EBI-11524452;
CC Q7Z6M4; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-948435, EBI-7062247;
CC Q7Z6M4; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-948435, EBI-12831978;
CC Q7Z6M4; P50402: EMD; NbExp=3; IntAct=EBI-948435, EBI-489887;
CC Q7Z6M4; Q96CB9-1: NSUN4; NbExp=7; IntAct=EBI-948435, EBI-16012886;
CC Q7Z6M4; Q9UJX0: OSGIN1; NbExp=5; IntAct=EBI-948435, EBI-9057006;
CC Q7Z6M4; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-948435, EBI-1044859;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21531335,
CC ECO:0000269|PubMed:22949673, ECO:0000269|PubMed:23022348}.
CC -!- DOMAIN: The MTERF repeats form a half-donut shaped, right-handed
CC superhelix, where the concave side displays a positively charged path
CC for nucleic acid interaction.
CC -!- PTM: The mature mitochondrial protein exists in 2 forms differing at
CC the level of their N-terminus, one is starting at residue 43 and the
CC other at residue 48. {ECO:0000269|PubMed:21531335}.
CC -!- SIMILARITY: Belongs to the mTERF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28919.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK291665; BAF84354.1; -; mRNA.
DR EMBL; AC005237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053533; AAH53533.2; -; mRNA.
DR EMBL; AF161359; AAF28919.1; ALT_INIT; mRNA.
DR CCDS; CCDS2544.1; -.
DR RefSeq; NP_872307.2; NM_182501.3.
DR RefSeq; XP_016858876.1; XM_017003387.1.
DR PDB; 4FP9; X-ray; 2.90 A; B/E/G/H=47-381.
DR PDB; 4FZV; X-ray; 2.00 A; B=122-330.
DR PDB; 7O9K; EM; 3.10 A; A2=1-381.
DR PDB; 7O9M; EM; 2.50 A; A2=1-381.
DR PDB; 7ODR; EM; 2.90 A; y=1-381.
DR PDB; 7ODS; EM; 3.10 A; y=1-381.
DR PDB; 7ODT; EM; 3.10 A; y=1-381.
DR PDB; 7OF0; EM; 2.20 A; G=1-381.
DR PDB; 7OF3; EM; 2.70 A; G=1-381.
DR PDB; 7OF5; EM; 2.90 A; G=1-381.
DR PDB; 7OF7; EM; 2.50 A; G=1-381.
DR PDB; 7OIC; EM; 3.10 A; y=1-381.
DR PDB; 7PD3; EM; 3.40 A; y=1-381.
DR PDBsum; 4FP9; -.
DR PDBsum; 4FZV; -.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7ODR; -.
DR PDBsum; 7ODS; -.
DR PDBsum; 7ODT; -.
DR PDBsum; 7OF0; -.
DR PDBsum; 7OF3; -.
DR PDBsum; 7OF5; -.
DR PDBsum; 7OF7; -.
DR PDBsum; 7OIC; -.
DR PDBsum; 7PD3; -.
DR AlphaFoldDB; Q7Z6M4; -.
DR SMR; Q7Z6M4; -.
DR BioGRID; 126263; 23.
DR DIP; DIP-49918N; -.
DR IntAct; Q7Z6M4; 17.
DR MINT; Q7Z6M4; -.
DR STRING; 9606.ENSP00000480378; -.
DR iPTMnet; Q7Z6M4; -.
DR PhosphoSitePlus; Q7Z6M4; -.
DR BioMuta; MTERF4; -.
DR DMDM; 296439296; -.
DR EPD; Q7Z6M4; -.
DR jPOST; Q7Z6M4; -.
DR MassIVE; Q7Z6M4; -.
DR MaxQB; Q7Z6M4; -.
DR PaxDb; Q7Z6M4; -.
DR PeptideAtlas; Q7Z6M4; -.
DR PRIDE; Q7Z6M4; -.
DR ProteomicsDB; 69450; -.
DR Antibodypedia; 34543; 68 antibodies from 19 providers.
DR Ensembl; ENST00000241527.10; ENSP00000241527.6; ENSG00000122085.17.
DR Ensembl; ENST00000391980.7; ENSP00000375840.2; ENSG00000122085.17.
DR Ensembl; ENST00000614476.4; ENSP00000480378.1; ENSG00000122085.17.
DR GeneID; 130916; -.
DR KEGG; hsa:130916; -.
DR MANE-Select; ENST00000391980.7; ENSP00000375840.2; NM_182501.4; NP_872307.2.
DR UCSC; uc061uks.1; human.
DR CTD; 130916; -.
DR DisGeNET; 130916; -.
DR GeneCards; MTERF4; -.
DR HGNC; HGNC:28785; MTERF4.
DR HPA; ENSG00000122085; Low tissue specificity.
DR MIM; 615393; gene.
DR neXtProt; NX_Q7Z6M4; -.
DR OpenTargets; ENSG00000122085; -.
DR PharmGKB; PA142671310; -.
DR VEuPathDB; HostDB:ENSG00000122085; -.
DR eggNOG; ENOG502RXUW; Eukaryota.
DR GeneTree; ENSGT00460000041648; -.
DR HOGENOM; CLU_069384_1_0_1; -.
DR InParanoid; Q7Z6M4; -.
DR OMA; TNKNVWK; -.
DR OrthoDB; 1431133at2759; -.
DR PhylomeDB; Q7Z6M4; -.
DR TreeFam; TF329452; -.
DR PathwayCommons; Q7Z6M4; -.
DR Reactome; R-HSA-6793080; rRNA modification in the mitochondrion.
DR SignaLink; Q7Z6M4; -.
DR BioGRID-ORCS; 130916; 170 hits in 1079 CRISPR screens.
DR ChiTaRS; MTERF4; human.
DR GenomeRNAi; 130916; -.
DR Pharos; Q7Z6M4; Tbio.
DR PRO; PR:Q7Z6M4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q7Z6M4; protein.
DR Bgee; ENSG00000122085; Expressed in sural nerve and 181 other tissues.
DR ExpressionAtlas; Q7Z6M4; baseline and differential.
DR Genevisible; Q7Z6M4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IDA:MGI.
DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0006390; P:mitochondrial transcription; IEA:Ensembl.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0042255; P:ribosome assembly; IEA:Ensembl.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.25.70.10; -; 1.
DR InterPro; IPR003690; MTERF.
DR InterPro; IPR038538; MTERF_sf.
DR PANTHER; PTHR13068; PTHR13068; 1.
DR Pfam; PF02536; mTERF; 1.
DR SMART; SM00733; Mterf; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Mitochondrion; Reference proteome;
KW Repeat; RNA-binding; rRNA processing; Transit peptide.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:21531335"
FT CHAIN 43..381
FT /note="Transcription termination factor 4, mitochondrial"
FT /id="PRO_0000255461"
FT CHAIN 48..381
FT /note="mTERF domain-containing protein 2 processed"
FT /id="PRO_0000424341"
FT REPEAT 142..172
FT /note="MTERF 1"
FT /evidence="ECO:0000269|PubMed:23022348"
FT REPEAT 177..204
FT /note="MTERF 2"
FT /evidence="ECO:0000269|PubMed:23022348"
FT REPEAT 209..239
FT /note="MTERF 3"
FT /evidence="ECO:0000269|PubMed:23022348"
FT REPEAT 245..270
FT /note="MTERF 4"
FT /evidence="ECO:0000269|PubMed:23022348"
FT REPEAT 290..318
FT /note="MTERF 5"
FT /evidence="ECO:0000269|PubMed:23022348"
FT REGION 310..327
FT /note="Dimerization with NSUN4"
FT REGION 322..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..381
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 45
FT /note="T -> A (in dbSNP:rs3796093)"
FT /id="VAR_028865"
FT VARIANT 189
FT /note="M -> T (in dbSNP:rs2286323)"
FT /id="VAR_028866"
FT VARIANT 339
FT /note="L -> V (in dbSNP:rs2240539)"
FT /id="VAR_028867"
FT VARIANT 347
FT /note="D -> E (in dbSNP:rs10203977)"
FT /id="VAR_028868"
FT VARIANT 378
FT /note="D -> E (in dbSNP:rs10167328)"
FT /id="VAR_028869"
FT CONFLICT 27
FT /note="P -> R (in Ref. 4; AAF28919)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="S -> G (in Ref. 1; BAF84354)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="C -> R (in Ref. 3; AAH53533)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="E -> G (in Ref. 1; BAF84354)"
FT /evidence="ECO:0000305"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:4FZV"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:4FP9"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 258..270
FT /evidence="ECO:0007829|PDB:4FZV"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:4FZV"
FT HELIX 310..327
FT /evidence="ECO:0007829|PDB:4FZV"
SQ SEQUENCE 381 AA; 43958 MW; 45592F93558EE190 CRC64;
MAAFGRQVLD WHRLIPLTWA CMARQTPHLG EQRRTTASLL RKLTTASNGG VIEELSCVRS
NNYVQEPECR RNLVQCLLEK QGTPVVQGSL ELERVMSSLL DMGFSNAHIN ELLSVRRGAS
LQQLLDIISE FILLGLNPEP VCVVLKKSPQ LLKLPIMQMR KRSSYLQKLG LGEGKLKRVL
YCCPEIFTMR QQDINDTVRL LKEKCLFTVQ QVTKILHSCP SVLREDLGQL EYKFQYAYFR
MGIKHPDIVK SEYLQYSLTK IKQRHIYLER LGRYQTPDKK GQTQIPNPLL KDILRVSEAE
FLARTACTSV EEFQVFKKLL AREEEESESS TSDDKRASLD EDEDDDDEED NDEDDNDEDD
DDEDDDEAED NDEDEDDDEE E
