SSU72_HUMAN
ID SSU72_HUMAN Reviewed; 194 AA.
AC Q9NP77; Q9BZS6; Q9H933;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase SSU72;
DE Short=CTD phosphatase SSU72;
DE EC=3.1.3.16;
GN Name=SSU72; ORFNames=HSPC182, PNAS-120;
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], FUNCTION, INTERACTION WITH RB1; GTF2B AND
RP CD226, AND MUTAGENESIS OF CYS-12.
RX PubMed=15659578; DOI=10.1093/nar/gki171;
RA St Pierre B., Liu X., Kha L.C., Zhu X., Ryan O., Jiang Z., Zacksenhaus E.;
RT "Conserved and specific functions of mammalian ssu72.";
RL Nucleic Acids Res. 33:464-477(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Promyelocytic leukemia;
RA Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W.,
RA Yang H., Zhao Z.-L.;
RT "Human acute promyelocytic leukemia cell line NB4's apoptosis related
RT genes.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RA Stanchi F., Lanfranchi G.;
RT "Full-length sequencing of 100 cDNA clones from human adult skeletal
RT muscle.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, Teratocarcinoma, and 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [9]
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 [10]
RP INTERACTION WITH GTF2B.
RX PubMed=29158257; DOI=10.1074/jbc.m117.811521;
RA Bratkowski M., Unarta I.C., Zhu L., Shubbar M., Huang X., Liu X.;
RT "Structural dissection of an interaction between transcription initiation
RT and termination factors implicated in promoter-terminator cross-talk.";
RL J. Biol. Chem. 293:1651-1665(2018).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SYMPK, FUNCTION,
RP CATALYTIC ACTIVITY, AND INTERACTION WITH SYMPK.
RX PubMed=20861839; DOI=10.1038/nature09391;
RA Xiang K., Nagaike T., Xiang S., Kilic T., Beh M.M., Manley J.L., Tong L.;
RT "Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide
RT complex.";
RL Nature 467:729-733(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SYMPK, FUNCTION,
RP CATALYTIC ACTIVITY, AND INTERACTION WITH SYMPK.
RX PubMed=23070812; DOI=10.1101/gad.198853.112;
RA Xiang K., Manley J.L., Tong L.;
RT "An unexpected binding mode for a Pol II CTD peptide phosphorylated at Ser7
RT in the active site of the CTD phosphatase Ssu72.";
RL Genes Dev. 26:2265-2270(2012).
CC -!- FUNCTION: Protein phosphatase that catalyzes the dephosphorylation of
CC the C-terminal domain of RNA polymerase II. Plays a role in RNA
CC processing and termination. Plays a role in pre-mRNA polyadenylation
CC via its interaction with SYMPK. {ECO:0000269|PubMed:15659578,
CC ECO:0000269|PubMed:20861839, ECO:0000269|PubMed:23070812}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:20861839, ECO:0000269|PubMed:23070812};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:20861839, ECO:0000269|PubMed:23070812};
CC -!- SUBUNIT: Interacts with GTF2B (via C-terminus); this interaction is
CC inhibited by SYMPK (PubMed:15659578, PubMed:29158257). Interacts with
CC RB1 (PubMed:15659578). Interacts with CD226 (PubMed:15659578).
CC Interacts with SYMPK (PubMed:20861839, PubMed:23070812).
CC {ECO:0000269|PubMed:15659578, ECO:0000269|PubMed:20861839,
CC ECO:0000269|PubMed:23070812, ECO:0000269|PubMed:29158257}.
CC -!- INTERACTION:
CC Q9NP77; P42858: HTT; NbExp=3; IntAct=EBI-2515416, EBI-466029;
CC Q9NP77; O60216: RAD21; NbExp=9; IntAct=EBI-2515416, EBI-80739;
CC Q9NP77; Q8N3U4: STAG2; NbExp=4; IntAct=EBI-2515416, EBI-1057252;
CC Q9NP77-1; Q92797: SYMPK; NbExp=3; IntAct=EBI-15879531, EBI-1051992;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly in the
CC cytosol.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NP77-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NP77-2; Sequence=VSP_033005;
CC -!- SIMILARITY: Belongs to the SSU72 phosphatase family. {ECO:0000305}.
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DR EMBL; AF161530; AAF29145.1; -; mRNA.
DR EMBL; AF277178; AAK07538.1; -; mRNA.
DR EMBL; AJ276409; CAC81713.1; -; mRNA.
DR EMBL; AK001809; BAA91921.1; -; mRNA.
DR EMBL; AK023110; BAB14410.1; -; mRNA.
DR EMBL; AK291324; BAF84013.1; -; mRNA.
DR EMBL; AL645728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471183; EAW56182.1; -; Genomic_DNA.
DR EMBL; CH471183; EAW56183.1; -; Genomic_DNA.
DR EMBL; BC008070; AAH08070.1; -; mRNA.
DR CCDS; CCDS32.1; -. [Q9NP77-1]
DR RefSeq; NP_054907.1; NM_014188.2. [Q9NP77-1]
DR PDB; 3O2Q; X-ray; 2.40 A; B/E=1-194.
DR PDB; 3O2S; X-ray; 2.50 A; B=1-194.
DR PDB; 4H3H; X-ray; 2.20 A; B/E=1-194.
DR PDB; 4H3K; X-ray; 2.00 A; B/E=1-194.
DR PDBsum; 3O2Q; -.
DR PDBsum; 3O2S; -.
DR PDBsum; 4H3H; -.
DR PDBsum; 4H3K; -.
DR AlphaFoldDB; Q9NP77; -.
DR SMR; Q9NP77; -.
DR BioGRID; 118869; 58.
DR CORUM; Q9NP77; -.
DR DIP; DIP-53666N; -.
DR IntAct; Q9NP77; 24.
DR MINT; Q9NP77; -.
DR STRING; 9606.ENSP00000291386; -.
DR BindingDB; Q9NP77; -.
DR ChEMBL; CHEMBL3317331; -.
DR DEPOD; SSU72; -.
DR iPTMnet; Q9NP77; -.
DR PhosphoSitePlus; Q9NP77; -.
DR BioMuta; SSU72; -.
DR DMDM; 74752877; -.
DR EPD; Q9NP77; -.
DR jPOST; Q9NP77; -.
DR MassIVE; Q9NP77; -.
DR MaxQB; Q9NP77; -.
DR PaxDb; Q9NP77; -.
DR PeptideAtlas; Q9NP77; -.
DR PRIDE; Q9NP77; -.
DR ProteomicsDB; 81915; -. [Q9NP77-1]
DR ProteomicsDB; 81916; -. [Q9NP77-2]
DR Antibodypedia; 26440; 130 antibodies from 21 providers.
DR DNASU; 29101; -.
DR Ensembl; ENST00000291386.4; ENSP00000291386.3; ENSG00000160075.12. [Q9NP77-1]
DR Ensembl; ENST00000359060.5; ENSP00000351955.3; ENSG00000160075.12. [Q9NP77-2]
DR GeneID; 29101; -.
DR KEGG; hsa:29101; -.
DR MANE-Select; ENST00000291386.4; ENSP00000291386.3; NM_014188.3; NP_054907.1.
DR UCSC; uc001agd.4; human. [Q9NP77-1]
DR CTD; 29101; -.
DR DisGeNET; 29101; -.
DR GeneCards; SSU72; -.
DR HGNC; HGNC:25016; SSU72.
DR HPA; ENSG00000160075; Low tissue specificity.
DR MIM; 617680; gene.
DR neXtProt; NX_Q9NP77; -.
DR OpenTargets; ENSG00000160075; -.
DR PharmGKB; PA142670866; -.
DR VEuPathDB; HostDB:ENSG00000160075; -.
DR eggNOG; KOG2424; Eukaryota.
DR GeneTree; ENSGT00390000010165; -.
DR HOGENOM; CLU_062463_2_1_1; -.
DR InParanoid; Q9NP77; -.
DR OMA; PNCYEFG; -.
DR OrthoDB; 1304061at2759; -.
DR PhylomeDB; Q9NP77; -.
DR TreeFam; TF300194; -.
DR PathwayCommons; Q9NP77; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q9NP77; -.
DR SIGNOR; Q9NP77; -.
DR BioGRID-ORCS; 29101; 801 hits in 1087 CRISPR screens.
DR ChiTaRS; SSU72; human.
DR EvolutionaryTrace; Q9NP77; -.
DR GenomeRNAi; 29101; -.
DR Pharos; Q9NP77; Tbio.
DR PRO; PR:Q9NP77; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NP77; protein.
DR Bgee; ENSG00000160075; Expressed in parotid gland and 184 other tissues.
DR Genevisible; Q9NP77; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IDA:UniProtKB.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IDA:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IMP:UniProtKB.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR InterPro; IPR006811; RNA_pol_II_suA.
DR PANTHER; PTHR20383; PTHR20383; 1.
DR Pfam; PF04722; Ssu72; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Hydrolase;
KW mRNA processing; Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..194
FT /note="RNA polymerase II subunit A C-terminal domain
FT phosphatase SSU72"
FT /id="PRO_0000330012"
FT COILED 160..186
FT /evidence="ECO:0000255"
FT VAR_SEQ 77..194
FT /note="TQNGILHMLDRNKRIKPRPERFQNCKDLFDLILTCEERVYDQVVEDLNSREQ
FT ETCQPVHVVNVDIQDNHEEATLGAFLICELCQCIQHTEDMENEIDELLQEFEEKSGRTF
FT LHTVCFY -> PSGLPFKNPPCGPPWKVLRVARAQEACHPVQCTHWLLCLCESLVSIPG
FT ARRIVHGLVPVPPMAVGVVRRTDTVWGSP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_033005"
FT MUTAGEN 12
FT /note="C->S: Abolishes phosphatase activity."
FT /evidence="ECO:0000269|PubMed:15659578"
FT CONFLICT 182..183
FT /note="KS -> RV (in Ref. 3; AAK07538)"
FT /evidence="ECO:0000305"
FT STRAND 7..17
FT /evidence="ECO:0007829|PDB:4H3K"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:4H3K"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:4H3K"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:4H3K"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4H3K"
FT HELIX 61..78
FT /evidence="ECO:0007829|PDB:4H3K"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:4H3K"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4H3K"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:4H3K"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:4H3K"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4H3K"
FT HELIX 145..164
FT /evidence="ECO:0007829|PDB:4H3K"
FT HELIX 168..183
FT /evidence="ECO:0007829|PDB:4H3K"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:4H3K"
SQ SEQUENCE 194 AA; 22574 MW; CA3A3157A2388A77 CRC64;
MPSSPLRVAV VCSSNQNRSM EAHNILSKRG FSVRSFGTGT HVKLPGPAPD KPNVYDFKTT
YDQMYNDLLR KDKELYTQNG ILHMLDRNKR IKPRPERFQN CKDLFDLILT CEERVYDQVV
EDLNSREQET CQPVHVVNVD IQDNHEEATL GAFLICELCQ CIQHTEDMEN EIDELLQEFE
EKSGRTFLHT VCFY
