ZN189_HUMAN
ID ZN189_HUMAN Reviewed; 626 AA.
AC O75820; O75802; Q5T7D7; Q5T7D8; Q5T7D9; Q9UBL4; Q9UPE9; Q9UPF0; Q9UPF1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Zinc finger protein 189;
GN Name=ZNF189;
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] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Bone marrow;
RX PubMed=9653648; DOI=10.1006/geno.1998.5309;
RA Odeberg J., Roesok O., Gudmundsson G., Ahmadian A., Roshani L.,
RA Williams C., Larsson C., Ponten F., Uhlen M., Aasheim H.-C., Lundeberg J.;
RT "Cloning and characterization of ZNF189, a novel human Kruppel-like zinc
RT finger gene localized to chromosome 9q22-q31.";
RL Genomics 50:213-221(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 4).
RX PubMed=10415338; DOI=10.1016/s0378-1119(99)00205-x;
RA Odeberg J., Ahmadian A., Williams C., Uhlen M., Ponten F., Lundeberg J.;
RT "Context-dependent Taq-polymerase-mediated nucleotide alterations, as
RT revealed by direct sequencing of the ZNF189 gene: implications for mutation
RT detection.";
RL Gene 235:103-109(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Thalamus;
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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-88, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-88, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-88, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67; LYS-88; LYS-160; LYS-434 AND
RP LYS-452, AND IDENTIFICATION BY MASS 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: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O75820-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75820-2; Sequence=VSP_006900;
CC Name=3; Synonyms=B2;
CC IsoId=O75820-3; Sequence=VSP_006901;
CC Name=4;
CC IsoId=O75820-4; Sequence=VSP_006899;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U95992; AAC25910.1; -; mRNA.
DR EMBL; U95991; AAC25909.1; -; mRNA.
DR EMBL; U75454; AAC39798.1; -; mRNA.
DR EMBL; AF025770; AAC39799.1; -; mRNA.
DR EMBL; AF025771; AAC39800.1; -; mRNA.
DR EMBL; AF025772; AAD50527.1; -; Genomic_DNA.
DR EMBL; AF025772; AAD50528.1; -; Genomic_DNA.
DR EMBL; AK290163; BAF82852.1; -; mRNA.
DR EMBL; AL353621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW58949.1; -; Genomic_DNA.
DR EMBL; BC092425; AAH92425.1; -; mRNA.
DR EMBL; BC126120; AAI26121.1; -; mRNA.
DR EMBL; BC143876; AAI43877.1; -; mRNA.
DR CCDS; CCDS65096.1; -. [O75820-2]
DR CCDS; CCDS6754.1; -. [O75820-1]
DR CCDS; CCDS6755.1; -. [O75820-4]
DR RefSeq; NP_001265160.1; NM_001278231.1. [O75820-2]
DR RefSeq; NP_001265161.1; NM_001278232.1.
DR RefSeq; NP_001265169.1; NM_001278240.1.
DR RefSeq; NP_003443.2; NM_003452.3. [O75820-1]
DR RefSeq; NP_932094.1; NM_197977.2. [O75820-4]
DR RefSeq; XP_006717343.1; XM_006717280.3. [O75820-4]
DR RefSeq; XP_006717344.1; XM_006717281.3. [O75820-4]
DR RefSeq; XP_011517300.1; XM_011518998.2. [O75820-4]
DR RefSeq; XP_016870610.1; XM_017015121.1. [O75820-4]
DR AlphaFoldDB; O75820; -.
DR SMR; O75820; -.
DR BioGRID; 113528; 46.
DR IntAct; O75820; 22.
DR MINT; O75820; -.
DR STRING; 9606.ENSP00000342019; -.
DR iPTMnet; O75820; -.
DR PhosphoSitePlus; O75820; -.
DR BioMuta; ZNF189; -.
DR EPD; O75820; -.
DR jPOST; O75820; -.
DR MassIVE; O75820; -.
DR MaxQB; O75820; -.
DR PaxDb; O75820; -.
DR PeptideAtlas; O75820; -.
DR PRIDE; O75820; -.
DR ProteomicsDB; 50210; -. [O75820-1]
DR ProteomicsDB; 50211; -. [O75820-2]
DR ProteomicsDB; 50212; -. [O75820-3]
DR ProteomicsDB; 50213; -. [O75820-4]
DR Antibodypedia; 29147; 57 antibodies from 17 providers.
DR DNASU; 7743; -.
DR Ensembl; ENST00000259395.4; ENSP00000259395.4; ENSG00000136870.11. [O75820-4]
DR Ensembl; ENST00000339664.7; ENSP00000342019.2; ENSG00000136870.11. [O75820-1]
DR Ensembl; ENST00000374861.7; ENSP00000363995.3; ENSG00000136870.11. [O75820-2]
DR GeneID; 7743; -.
DR KEGG; hsa:7743; -.
DR MANE-Select; ENST00000339664.7; ENSP00000342019.2; NM_003452.4; NP_003443.2.
DR UCSC; uc004bbg.3; human. [O75820-1]
DR CTD; 7743; -.
DR DisGeNET; 7743; -.
DR GeneCards; ZNF189; -.
DR HGNC; HGNC:12980; ZNF189.
DR HPA; ENSG00000136870; Tissue enhanced (epididymis).
DR MIM; 603132; gene.
DR neXtProt; NX_O75820; -.
DR OpenTargets; ENSG00000136870; -.
DR PharmGKB; PA37561; -.
DR VEuPathDB; HostDB:ENSG00000136870; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161823; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; O75820; -.
DR OMA; CHISLIQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O75820; -.
DR TreeFam; TF336942; -.
DR PathwayCommons; O75820; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; O75820; -.
DR BioGRID-ORCS; 7743; 8 hits in 1103 CRISPR screens.
DR GenomeRNAi; 7743; -.
DR Pharos; O75820; Tdark.
DR PRO; PR:O75820; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O75820; protein.
DR Bgee; ENSG00000136870; Expressed in corpus epididymis and 209 other tissues.
DR ExpressionAtlas; O75820; baseline and differential.
DR Genevisible; O75820; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 15.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..626
FT /note="Zinc finger protein 189"
FT /id="PRO_0000047444"
FT DOMAIN 14..89
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 148..170
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 176..198
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 204..226
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 232..254
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 260..282
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 288..310
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 316..338
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 344..366
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 372..394
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..422
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 456..478
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 484..506
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 512..534
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 540..562
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 568..590
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 599..621
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 67
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 434
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 452
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..95
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9653648"
FT /id="VSP_006901"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9653648"
FT /id="VSP_006899"
FT VAR_SEQ 12..25
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9653648"
FT /id="VSP_006900"
FT VARIANT 221
FT /note="R -> K (in dbSNP:rs10989492)"
FT /id="VAR_025403"
FT CONFLICT 588
FT /note="K -> M (in Ref. 1; AAC25910/AAC25909/AAC39798/
FT AAC39799/AAC39800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 72976 MW; BF6E0F9943F15E4C CRC64;
MASPSPPPES KGLLTFEDVA VFFTQEEWDY LDPAQRSLYK DVMMENYGNL VSLDVLNRDK
DEEPTVKQEI EEIEEEVEPQ GVIVTRIKSE IDQDPMGRET FELVGRLDKQ RGIFLWEIPR
ESLTQEQRMF RENTNIIRKR PNSEEKCHKC EECGKGFVRK AHFIQHQRVH TGEKPFQCNE
CGKSFSRSSF VIEHQRIHTG ERPYECNYCG KTFSVSSTLI RHQRIHTGER PYQCNQCKQS
FSQRRSLVKH QRIHTGEKPH KCSDCGKAFS WKSHLIEHQR THTGEKPYHC TKCKKSFSRN
SLLVEHQRIH TGERPHKCGE CGKAFRLSTY LIQHQKIHTG EKPFLCIECG KSFSRSSFLI
EHQRIHTGER PYQCKECGKS FSQLCNLTRH QRIHTGDKPH KCEECGKAFS RSSGLIQHQR
IHTREKTYPY NETKESFDPN CSLVIQQEVY PKEKSYKCDE CGKTFSVSAH LVQHQRIHTG
EKPYLCTVCG KSFSRSSFLI EHQRIHTGER PYLCRQCGKS FSQLCNLIRH QGVHTGNKPH
KCDECGKAFS RNSGLIQHQR IHTGEKPYKC EKCDKSFSQQ RSLVNHQKIH AEVKTQETHE
CDACGEAFNC RISLIQHQKL HTAWMQ
