ZFP62_HUMAN
ID ZFP62_HUMAN Reviewed; 900 AA.
AC Q8NB50; B4DIP6; B4E0N3; B5MDX6; B7ZVZ2; B9EIP6; E9PFT8; J3QTA9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger protein 62 homolog;
DE Short=Zfp-62;
GN Name=ZFP62;
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] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 173-900 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE
RP MRNA] OF 1-145 (ISOFORM 3), AND VARIANTS ILE-34 AND LYS-698.
RC TISSUE=Brain, Hippocampus, and Thymus;
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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 186-900 (ISOFORM 1), AND VARIANT
RP LYS-698.
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 MRNA] OF 186-900 (ISOFORM 1), AND VARIANT
RP LYS-698.
RC TISSUE=Lung;
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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-65 AND LYS-82, AND IDENTIFICATION
RP BY MASS 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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-82, 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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-82, 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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-48; LYS-62; LYS-65;
RP LYS-82; LYS-92; LYS-587; LYS-748 AND LYS-882, 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: May play a role in differentiating skeletal muscle.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NB50-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NB50-2; Sequence=VSP_010136;
CC Name=3;
CC IsoId=Q8NB50-3; Sequence=VSP_045257;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI40762.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC03691.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG58558.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical GTG valine codon.; Evidence={ECO:0000305};
CC Sequence=CAI46133.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK091550; BAC03691.1; ALT_INIT; mRNA.
DR EMBL; AK295714; BAG58558.1; ALT_SEQ; mRNA.
DR EMBL; AK303450; BAG64495.1; -; mRNA.
DR EMBL; DA323041; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC022413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL832408; CAI46133.1; ALT_INIT; Transcribed_RNA.
DR EMBL; BC140761; AAI40762.1; ALT_INIT; mRNA.
DR EMBL; BC171780; AAI71780.1; -; mRNA.
DR CCDS; CCDS47357.2; -. [Q8NB50-3]
DR CCDS; CCDS54955.1; -. [Q8NB50-1]
DR RefSeq; NP_001166109.1; NM_001172638.1. [Q8NB50-1]
DR RefSeq; NP_689496.4; NM_152283.4. [Q8NB50-3]
DR RefSeq; XP_016865199.1; XM_017009710.1.
DR RefSeq; XP_016865200.1; XM_017009711.1.
DR RefSeq; XP_016865201.1; XM_017009712.1.
DR RefSeq; XP_016865202.1; XM_017009713.1.
DR RefSeq; XP_016865203.1; XM_017009714.1.
DR RefSeq; XP_016865204.1; XM_017009715.1.
DR RefSeq; XP_016865206.1; XM_017009717.1.
DR AlphaFoldDB; Q8NB50; -.
DR SMR; Q8NB50; -.
DR BioGRID; 569091; 66.
DR IntAct; Q8NB50; 26.
DR STRING; 9606.ENSP00000423820; -.
DR GlyGen; Q8NB50; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NB50; -.
DR PhosphoSitePlus; Q8NB50; -.
DR BioMuta; ZFP62; -.
DR DMDM; 327478553; -.
DR EPD; Q8NB50; -.
DR jPOST; Q8NB50; -.
DR MassIVE; Q8NB50; -.
DR MaxQB; Q8NB50; -.
DR PaxDb; Q8NB50; -.
DR PeptideAtlas; Q8NB50; -.
DR PRIDE; Q8NB50; -.
DR ProteomicsDB; 72735; -. [Q8NB50-1]
DR ProteomicsDB; 72736; -. [Q8NB50-2]
DR Antibodypedia; 53012; 34 antibodies from 10 providers.
DR DNASU; 643836; -.
DR Ensembl; ENST00000502412.2; ENSP00000423820.1; ENSG00000196670.14. [Q8NB50-1]
DR Ensembl; ENST00000512132.5; ENSP00000426193.1; ENSG00000196670.14. [Q8NB50-3]
DR GeneID; 643836; -.
DR KEGG; hsa:643836; -.
DR MANE-Select; ENST00000502412.2; ENSP00000423820.1; NM_001172638.2; NP_001166109.1.
DR UCSC; uc011dhe.3; human. [Q8NB50-1]
DR CTD; 643836; -.
DR GeneCards; ZFP62; -.
DR HGNC; HGNC:23241; ZFP62.
DR HPA; ENSG00000196670; Low tissue specificity.
DR MIM; 610281; gene.
DR neXtProt; NX_Q8NB50; -.
DR OpenTargets; ENSG00000196670; -.
DR PharmGKB; PA134969387; -.
DR VEuPathDB; HostDB:ENSG00000196670; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162750; -.
DR HOGENOM; CLU_002678_17_3_1; -.
DR InParanoid; Q8NB50; -.
DR OMA; GNTESKW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8NB50; -.
DR TreeFam; TF343410; -.
DR PathwayCommons; Q8NB50; -.
DR SignaLink; Q8NB50; -.
DR BioGRID-ORCS; 643836; 7 hits in 1103 CRISPR screens.
DR ChiTaRS; ZFP62; human.
DR GenomeRNAi; 643836; -.
DR Pharos; Q8NB50; Tdark.
DR PRO; PR:Q8NB50; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8NB50; protein.
DR Bgee; ENSG00000196670; Expressed in ganglionic eminence and 186 other tissues.
DR ExpressionAtlas; Q8NB50; baseline and differential.
DR Genevisible; Q8NB50; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator 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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 22.
DR SMART; SM00355; ZnF_C2H2; 26.
DR SUPFAM; SSF57667; SSF57667; 16.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 25.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 26.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..900
FT /note="Zinc finger protein 62 homolog"
FT /id="PRO_0000047305"
FT ZN_FING 225..247
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 253..275
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 281..303
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 309..331
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 337..359
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 365..387
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 393..415
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 421..443
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 449..471
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 477..499
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 505..527
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 533..555
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 561..583
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 589..611
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 617..639
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 645..667
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 673..695
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 701..723
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 729..751
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 757..779
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 785..807
FT /note="C2H2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 813..834
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 840..862
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 62
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 82
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 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 587
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 748
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 882
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045257"
FT VAR_SEQ 339..534
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010136"
FT VARIANT 34
FT /note="M -> I (in dbSNP:rs705441)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_064881"
FT VARIANT 698
FT /note="R -> K (in dbSNP:rs168726)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_064882"
FT CONFLICT 321
FT /note="C -> R (in Ref. 1; BAC03691)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="N -> I (in Ref. 1; BAG64495)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="L -> F (in Ref. 1; BAG58558)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 900 AA; 102511 MW; 0C1D915D03FBBE67 CRC64;
MSHLKTSTED EEPTEEYENV GNAASKWPKV EDPMPESKVG DTCVWDSKVE NQQKKPVENR
MKEDKSSIRE AISKAKSTAN IKTEQEGEAS EKSLHLSPQH ITHQTMPIGQ RGSEQGKRVE
NINGTSYPSL QQKTNAVKKL HKCDECGKSF KYNSRLVQHK IMHTGEKRYE CDDCGGTFRS
SSSLRVHKRI HTGEKPYKCE ECGKAYMSYS SLINHKSTHS GEKNCKCDEC GKSFNYSSVL
DQHKRIHTGE KPYECGECGK AFRNSSGLRV HKRIHTGEKP YECDICGKTF SNSSGLRVHK
RIHTGEKPYE CDECGKAFIT CRTLLNHKSI HFGDKPYKCD ECEKSFNYSS LLIQHKVIHT
GEKPYECDEC GKAFRNSSGL IVHKRIHTGE KPYKCDVCGK AFSYSSGLAV HKSIHPGKKA
HECKECGKSF SYNSLLLQHR TIHTGERPYV CDVCGKTFRN NAGLKVHRRL HTGEKPYKCD
VCGKAYISRS SLKNHKGIHL GEKPYKCSYC EKSFNYSSAL EQHKRIHTRE KPFGCDECGK
AFRNNSGLKV HKRIHTGERP YKCEECGKAY ISLSSLINHK SVHPGEKPFK CDECEKAFIT
YRTLTNHKKV HLGEKPYKCD VCEKSFNYTS LLSQHRRVHT REKPYECDRC EKVFRNNSSL
KVHKRIHTGE RPYECDVCGK AYISHSSLIN HKSTHPGRTP HTCDECGKAF FSSRTLISHK
RVHLGEKPFK CVECGKSFSY SSLLSQHKRI HTGEKPYVCD RCGKAFRNSS GLTVHKRIHT
GEKPYECDEC GKAYISHSSL INHKSVHQGK QPYNCECGKS FNYRSVLDQH KRIHTGKKPY
RCNECGKAFN IRSNLTKHKR THTGEESLNV IYVGSYSGTS QKRTYEGGNA LDGGRMRMPL
