TTF1_HUMAN
ID TTF1_HUMAN Reviewed; 905 AA.
AC Q15361; A1L160; Q4VXF3; Q58EY2; Q6P5T5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Transcription termination factor 1;
DE Short=TTF-1;
DE AltName: Full=RNA polymerase I termination factor;
DE AltName: Full=Transcription termination factor I;
DE Short=TTF-I;
GN Name=TTF1;
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 [MRNA], AND FUNCTION.
RX PubMed=7597036; DOI=10.1073/pnas.92.13.5827;
RA Evers R., Grummt I.;
RT "Molecular evolution of mammalian ribosomal gene terminator sequences and
RT the transcription termination factor TTF-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5827-5831(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-338 AND 457-905, AND VARIANT
RP LYS-35.
RC TISSUE=Uterus;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-403; SER-481 AND
RP SER-487, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-476; SER-481 AND SER-487, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-487 AND SER-872, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-481; SER-487 AND
RP SER-872, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; THR-248; SER-403; SER-487
RP AND SER-872, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487 AND SER-872, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-700, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Multifunctional nucleolar protein that terminates ribosomal
CC gene transcription, mediates replication fork arrest and regulates RNA
CC polymerase I transcription on chromatin. Plays a dual role in rDNA
CC regulation, being involved in both activation and silencing of rDNA
CC transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding
CC activity. {ECO:0000250|UniProtKB:Q62187, ECO:0000269|PubMed:7597036}.
CC -!- SUBUNIT: Oligomer. The oligomeric structure enables to interact
CC simultaneously with two separate DNA fragments. Interacts with
CC BAZ2A/TIP5. Interacts with CAVIN1. Interacts (via the N-terminal region
CC (NRD) and a C-terminal region) with CDKN2A/ARF; the interaction is
CC direct. Interacts (via C-terminal region) with NPM1/B23.
CC {ECO:0000250|UniProtKB:Q62187}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62187}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q62187}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q62187}. Note=May be localized to the nucleolus
CC in an NPM1/B23-dependent manner. May be displaced from the nucleolus
CC into the nucleoplasm in an CDKN2A/ARF-dependent manner. May shuttle
CC back and forth from nucleoplasm to nucleolus.
CC {ECO:0000250|UniProtKB:Q62187}.
CC -!- DOMAIN: The N-terminal region (NRD) inhibits DNA-binding via its
CC interaction with the C-terminal region. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH62692.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI04640.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI27670.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=AAI27671.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=AAI43049.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=AAI43050.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=CAA58807.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA58807.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR EMBL; X83973; CAA58807.1; ALT_SEQ; mRNA.
DR EMBL; AL353701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050734; AAH50734.1; -; mRNA.
DR EMBL; BC062692; AAH62692.1; ALT_SEQ; mRNA.
DR EMBL; BC104639; AAI04640.1; ALT_SEQ; mRNA.
DR EMBL; BC127669; AAI27670.1; ALT_SEQ; mRNA.
DR EMBL; BC127670; AAI27671.1; ALT_SEQ; mRNA.
DR EMBL; BC143048; AAI43049.1; ALT_SEQ; mRNA.
DR EMBL; BC143049; AAI43050.1; ALT_SEQ; mRNA.
DR CCDS; CCDS6948.1; -.
DR PIR; I38182; I38182.
DR RefSeq; NP_001192225.1; NM_001205296.1.
DR RefSeq; NP_031370.2; NM_007344.3.
DR RefSeq; XP_006717336.2; XM_006717273.3.
DR AlphaFoldDB; Q15361; -.
DR BioGRID; 113121; 114.
DR IntAct; Q15361; 26.
DR MINT; Q15361; -.
DR STRING; 9606.ENSP00000333920; -.
DR iPTMnet; Q15361; -.
DR PhosphoSitePlus; Q15361; -.
DR BioMuta; TTF1; -.
DR DMDM; 158518534; -.
DR EPD; Q15361; -.
DR jPOST; Q15361; -.
DR MassIVE; Q15361; -.
DR MaxQB; Q15361; -.
DR PaxDb; Q15361; -.
DR PeptideAtlas; Q15361; -.
DR PRIDE; Q15361; -.
DR ProteomicsDB; 60539; -.
DR Antibodypedia; 45229; 246 antibodies from 32 providers.
DR DNASU; 7270; -.
DR Ensembl; ENST00000334270.3; ENSP00000333920.2; ENSG00000125482.13.
DR GeneID; 7270; -.
DR KEGG; hsa:7270; -.
DR MANE-Select; ENST00000334270.3; ENSP00000333920.2; NM_007344.4; NP_031370.2.
DR UCSC; uc004cbl.5; human.
DR CTD; 7270; -.
DR DisGeNET; 7270; -.
DR GeneCards; TTF1; -.
DR HGNC; HGNC:12397; TTF1.
DR HPA; ENSG00000125482; Low tissue specificity.
DR MIM; 600777; gene.
DR neXtProt; NX_Q15361; -.
DR OpenTargets; ENSG00000125482; -.
DR PharmGKB; PA37062; -.
DR VEuPathDB; HostDB:ENSG00000125482; -.
DR eggNOG; KOG0051; Eukaryota.
DR GeneTree; ENSGT00940000159729; -.
DR HOGENOM; CLU_016962_1_0_1; -.
DR InParanoid; Q15361; -.
DR OMA; MQESRPA; -.
DR OrthoDB; 1474117at2759; -.
DR PhylomeDB; Q15361; -.
DR TreeFam; TF333537; -.
DR PathwayCommons; Q15361; -.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5683826; Surfactant metabolism.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR SignaLink; Q15361; -.
DR SIGNOR; Q15361; -.
DR BioGRID-ORCS; 7270; 275 hits in 1101 CRISPR screens.
DR ChiTaRS; TTF1; human.
DR GeneWiki; Transcription_termination_factor,_RNA_polymerase_I; -.
DR GenomeRNAi; 7270; -.
DR Pharos; Q15361; Tbio.
DR PRO; PR:Q15361; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q15361; protein.
DR Bgee; ENSG00000125482; Expressed in buccal mucosa cell and 210 other tissues.
DR ExpressionAtlas; Q15361; baseline and differential.
DR Genevisible; Q15361; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006353; P:DNA-templated transcription, termination; NAS:UniProtKB.
DR GO; GO:0008156; P:negative regulation of DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IBA:GO_Central.
DR InterPro; IPR001005; SANT/Myb.
DR SMART; SM00717; SANT; 2.
DR PROSITE; PS50090; MYB_LIKE; 2.
PE 1: Evidence at protein level;
KW DNA replication inhibitor; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transcription termination; Ubl conjugation.
FT CHAIN 1..905
FT /note="Transcription termination factor 1"
FT /id="PRO_0000250472"
FT DOMAIN 612..661
FT /note="Myb-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DOMAIN 661..745
FT /note="Myb-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..223
FT /note="N-terminal region (NRD)"
FT /evidence="ECO:0000250"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..886
FT /note="May be involved in interaction with ARF"
FT /evidence="ECO:0000250|UniProtKB:Q62187"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 476
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 700
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 35
FT /note="E -> K (in dbSNP:rs11550314)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027563"
FT VARIANT 290
FT /note="A -> S (in dbSNP:rs8999)"
FT /id="VAR_027564"
FT VARIANT 303
FT /note="V -> A (in dbSNP:rs3739914)"
FT /id="VAR_027565"
FT VARIANT 360
FT /note="G -> V (in dbSNP:rs3739915)"
FT /id="VAR_027566"
FT VARIANT 401
FT /note="R -> Q (in dbSNP:rs3739916)"
FT /id="VAR_027567"
FT VARIANT 473
FT /note="E -> K (in dbSNP:rs12336746)"
FT /id="VAR_050201"
FT VARIANT 885
FT /note="A -> V (in dbSNP:rs1752676)"
FT /id="VAR_061363"
FT CONFLICT 281
FT /note="K -> T (in Ref. 3; AAH50734)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="S -> R (in Ref. 1; CAA58807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 905 AA; 103051 MW; 12F829CEFDDF96E8 CRC64;
MEGESSRFEI HTPVSDKKKK KCSIHKERPQ KHSHEIFRDS SLVNEQSQIT RRKKRKKDFQ
HLISSPLKKS RICDETANAT STLKKRKKRR YSALEVDEEA GVTVVLVDKE NINNTPKHFR
KDVDVVCVDM SIEQKLPRKP KTDKFQVLAK SHAHKSEALH SKVREKKNKK HQRKAASWES
QRARDTLPQS ESHQEESWLS VGPGGEITEL PASAHKNKSK KKKKKSSNRE YETLAMPEGS
QAGREAGTDM QESQPTVGLD DETPQLLGPT HKKKSKKKKK KKSNHQEFEA LAMPEGSQVG
SEVGADMQES RPAVGLHGET AGIPAPAYKN KSKKKKKKSN HQEFEAVAMP ESLESAYPEG
SQVGSEVGTV EGSTALKGFK ESNSTKKKSK KRKLTSVKRA RVSGDDFSVP SKNSESTLFD
SVEGDGAMME EGVKSRPRQK KTQACLASKH VQEAPRLEPA NEEHNVETAE DSEIRYLSAD
SGDADDSDAD LGSAVKQLQE FIPNIKDRAT STIKRMYRDD LERFKEFKAQ GVAIKFGKFS
VKENKQLEKN VEDFLALTGI ESADKLLYTD RYPEEKSVIT NLKRRYSFRL HIGRNIARPW
KLIYYRAKKM FDVNNYKGRY SEGDTEKLKM YHSLLGNDWK TIGEMVARSS LSVALKFSQI
SSQRNRGAWS KSETRKLIKA VEEVILKKMS PQELKEVDSK LQENPESCLS IVREKLYKGI
SWVEVEAKVQ TRNWMQCKSK WTEILTKRMT NGRRIYYGMN ALRAKVSLIE RLYEINVEDT
NEIDWEDLAS AIGDVPPSYV QTKFSRLKAV YVPFWQKKTF PEIIDYLYET TLPLLKEKLE
KMMEKKGTKI QTPAAPKQVF PFRDIFYYED DSEGEDIEKE SEGQAPCMAH ACNSSTLGGQ
GRWII
