ZN668_HUMAN
ID ZN668_HUMAN Reviewed; 619 AA.
AC Q96K58; C9JHH8; F5H7E7; Q59EV1; Q8N669; Q9H8L4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Zinc finger protein 668;
GN Name=ZNF668;
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), AND VARIANT LEU-25.
RC TISSUE=Mammary gland, and 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 MRNA] (ISOFORM 1), AND VARIANT LEU-25.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LEU-25 AND
RP GLU-304.
RC TISSUE=Skin;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND IDENTIFICATION BY
RP 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-59; LYS-65; LYS-80;
RP LYS-154 AND LYS-512, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-66; SER-286; ARG-331 AND GLN-556.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- INTERACTION:
CC Q96K58-2; Q13895: BYSL; NbExp=3; IntAct=EBI-12817597, EBI-358049;
CC Q96K58-2; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-12817597, EBI-1567797;
CC Q96K58-2; P49910: ZNF165; NbExp=3; IntAct=EBI-12817597, EBI-741694;
CC Q96K58-2; P15622-3: ZNF250; NbExp=3; IntAct=EBI-12817597, EBI-10177272;
CC Q96K58-2; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-12817597, EBI-10240849;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96K58-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96K58-2; Sequence=VSP_053786;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14602.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD92947.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK023541; BAB14602.1; ALT_INIT; mRNA.
DR EMBL; AK027398; BAB55084.1; -; mRNA.
DR EMBL; AB209710; BAD92947.2; ALT_INIT; mRNA.
DR EMBL; AC135050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021997; AAH21997.1; -; mRNA.
DR CCDS; CCDS10701.1; -. [Q96K58-1]
DR CCDS; CCDS54003.1; -. [Q96K58-2]
DR RefSeq; NP_001166139.1; NM_001172668.1.
DR RefSeq; NP_001166140.1; NM_001172669.1.
DR RefSeq; NP_001166141.1; NM_001172670.1.
DR RefSeq; NP_078982.3; NM_024706.4.
DR AlphaFoldDB; Q96K58; -.
DR SMR; Q96K58; -.
DR BioGRID; 122868; 255.
DR IntAct; Q96K58; 39.
DR STRING; 9606.ENSP00000442573; -.
DR iPTMnet; Q96K58; -.
DR PhosphoSitePlus; Q96K58; -.
DR BioMuta; ZNF668; -.
DR DMDM; 306526260; -.
DR EPD; Q96K58; -.
DR jPOST; Q96K58; -.
DR MassIVE; Q96K58; -.
DR MaxQB; Q96K58; -.
DR PaxDb; Q96K58; -.
DR PeptideAtlas; Q96K58; -.
DR PRIDE; Q96K58; -.
DR ProteomicsDB; 10221; -.
DR ProteomicsDB; 77043; -. [Q96K58-1]
DR Antibodypedia; 13908; 120 antibodies from 27 providers.
DR DNASU; 79759; -.
DR Ensembl; ENST00000300849.5; ENSP00000300849.4; ENSG00000167394.13.
DR Ensembl; ENST00000394983.6; ENSP00000378434.2; ENSG00000167394.13.
DR Ensembl; ENST00000426488.6; ENSP00000403975.2; ENSG00000167394.13.
DR Ensembl; ENST00000535577.5; ENSP00000441349.1; ENSG00000167394.13.
DR Ensembl; ENST00000538906.5; ENSP00000440149.1; ENSG00000167394.13.
DR Ensembl; ENST00000539836.3; ENSP00000442573.3; ENSG00000167394.13.
DR GeneID; 79759; -.
DR KEGG; hsa:79759; -.
DR UCSC; uc002eao.4; human. [Q96K58-1]
DR CTD; 79759; -.
DR DisGeNET; 79759; -.
DR GeneCards; ZNF668; -.
DR HGNC; HGNC:25821; ZNF668.
DR HPA; ENSG00000167394; Low tissue specificity.
DR neXtProt; NX_Q96K58; -.
DR PharmGKB; PA142670515; -.
DR VEuPathDB; HostDB:ENSG00000167394; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_002678_44_10_1; -.
DR InParanoid; Q96K58; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q96K58; -.
DR TreeFam; TF331849; -.
DR PathwayCommons; Q96K58; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q96K58; -.
DR BioGRID-ORCS; 79759; 15 hits in 1099 CRISPR screens.
DR ChiTaRS; ZNF668; human.
DR GenomeRNAi; 79759; -.
DR Pharos; Q96K58; Tbio.
DR PRO; PR:Q96K58; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96K58; protein.
DR Bgee; ENSG00000167394; Expressed in stromal cell of endometrium and 98 other tissues.
DR ExpressionAtlas; Q96K58; baseline and differential.
DR Genevisible; Q96K58; 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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
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; 13.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..619
FT /note="Zinc finger protein 668"
FT /id="PRO_0000251478"
FT ZN_FING 22..44
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 84..106
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 112..134
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 140..162
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 168..190
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 196..218
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 224..246
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 252..274
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 280..302
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 308..330
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 336..358
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 364..386
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..414
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 516..538
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 544..566
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 572..594
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 34..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 59
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:28112733"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MSEPGMLGRKDVWVPRETPFTKAM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053786"
FT VARIANT 25
FT /note="V -> L (in dbSNP:rs2032917)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_027689"
FT VARIANT 66
FT /note="A -> T (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1429688220)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035595"
FT VARIANT 286
FT /note="G -> S (in a breast cancer sample; somatic mutation;
FT dbSNP:rs553159663)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035596"
FT VARIANT 304
FT /note="G -> E (in dbSNP:rs17851949)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027690"
FT VARIANT 331
FT /note="T -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035597"
FT VARIANT 447
FT /note="A -> V (in dbSNP:rs8046978)"
FT /id="VAR_027691"
FT VARIANT 556
FT /note="R -> Q (in a breast cancer sample; somatic mutation;
FT dbSNP:rs148738674)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035598"
FT CONFLICT 130
FT /note="H -> R (in Ref. 1; BAB14602)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="F -> I (in Ref. 1; BAB55084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 67890 MW; B86A2E15E9E7D7E8 CRC64;
MEVEAAEARS PAPGYKRSGR RYKCVSCTKT FPNAPRAARH AATHGPADCS EEVAEVKPKP
ETEAKAEEAS GEKVSGSAAK PRPYACPLCP KAYKTAPELR SHGRSHTGEK PFPCPECGRR
FMQPVCLRVH LASHAGELPF RCAHCPKAYG ALSKLKIHQR GHTGERPYAC ADCGKSFADP
SVFRKHRRTH AGLRPYSCER CGKAYAELKD LRNHERSHTG ERPFLCSECG KSFSRSSSLT
CHQRIHAAQK PYRCPACGKG FTQLSSYQSH ERTHSGEKPF LCPRCGRMFS DPSSFRRHQR
AHEGVKPYHC EKCGKDFRQP ADLAMHRRVH TGDRPFKCLQ CDKTFVASWD LKRHALVHSG
QRPFRCEECG RAFAERASLT KHSRVHSGER PFHCNACGKS FVVSSSLRKH ERTHRSSEAA
GVPPAQELVV GLALPVGVAG ESSAAPAAGA GLGDPPAGLL GLPPESGGVM ATQWQVVGMT
VEHVECQDAG VREAPGPLEG AGEAGGEEAD EKPPQFVCRE CKETFSTMTL LRRHERSHPE
LRPFPCTQCG KSFSDRAGLR KHSRTHSSVR PYTCPHCPKA FLSASDLRKH ERTHPVPMGT
PTPLEPLVAL LGMPEEGPA
