ZN217_HUMAN
ID ZN217_HUMAN Reviewed; 1048 AA.
AC O75362; E1P5Y6; Q14DB8;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Zinc finger protein 217;
GN Name=ZNF217; Synonyms=ZABC1;
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].
RX PubMed=9671742; DOI=10.1073/pnas.95.15.8703;
RA Collins C., Rommens J.M., Kowbel D., Godfrey T., Tanner M., Hwang S.-I.,
RA Polikoff D., Nonet G., Cochran J., Myambo K., Jay K.E., Froula J.,
RA Cloutier T., Kuo W.-L., Yaswen P., Dairkee S., Giovanola J.,
RA Hutchinson G.B., Isola J., Kallioniemi O.-P., Palazzolo M., Martin C.,
RA Ericsson C., Pinkel D., Albertson D., Li W.-B., Gray J.W.;
RT "Positional cloning of ZNF217 and NABC1: genes amplified at 20q13.2 and
RT overexpressed in breast carcinoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8703-8708(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 IDENTIFICATION IN THE BHC COMPLEX WITH GSE1; GTF2I; HDAC1; HDAC2; HMG20B;
RP KDM1A; PHF21A; RCOR1; ZMYM2 AND ZMYM3.
RX PubMed=12493763; DOI=10.1074/jbc.m208992200;
RA Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT "A candidate X-linked mental retardation gene is a component of a new
RT family of histone deacetylase-containing complexes.";
RL J. Biol. Chem. 278:7234-7239(2003).
RN [6]
RP FUNCTION.
RX PubMed=16203743; DOI=10.1093/hmg/ddi352;
RA Huang G., Krig S., Kowbel D., Xu H., Hyun B., Volik S., Feuerstein B.,
RA Mills G.B., Stokoe D., Yaswen P., Collins C.;
RT "ZNF217 suppresses cell death associated with chemotherapy and telomere
RT dysfunction.";
RL Hum. Mol. Genet. 14:3219-3225(2005).
RN [7]
RP FUNCTION.
RX PubMed=17259635; DOI=10.1074/jbc.m611752200;
RA Krig S.R., Jin V.X., Bieda M.C., O'Geen H., Yaswen P., Green R.,
RA Farnham P.J.;
RT "Identification of genes directly regulated by the oncogene ZNF217 using
RT chromatin immunoprecipitation (ChIP)-chip assays.";
RL J. Biol. Chem. 282:9703-9712(2007).
RN [8]
RP SUBUNIT, IDENTIFICATION IN A COMPLEX WITH HDAC2; KDM1A AND CTBP1, AND
RP FUNCTION.
RX PubMed=18625718; DOI=10.1128/mcb.00246-08;
RA Thillainadesan G., Isovic M., Loney E., Andrews J., Tini M., Torchia J.;
RT "Genome analysis identifies the p15ink4b tumor suppressor as a direct
RT target of the ZNF217/CoREST complex.";
RL Mol. Cell. Biol. 28:6066-6077(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; THR-322; THR-648 AND
RP SER-662, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-795, AND
RP 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-106; SER-407; SER-593 AND
RP SER-662, AND IDENTIFICATION BY 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-819, 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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 752-760 IN COMPLEX WITH CTBP1,
RP INTERACTION WITH CTBP1 AND CTBP2, AND FUNCTION.
RX PubMed=16940172; DOI=10.1128/mcb.00680-06;
RA Quinlan K.G.R., Nardini M., Verger A., Francescato P., Yaswen P., Corda D.,
RA Bolognesi M., Crossley M.;
RT "Specific recognition of ZNF217 and other zinc finger proteins at a surface
RT groove of C-terminal binding proteins.";
RL Mol. Cell. Biol. 26:8159-8172(2006).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-323.
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: Binds to the promoters of target genes and functions as
CC repressor. Promotes cell proliferation and antagonizes cell death.
CC Promotes phosphorylation of AKT1 at 'Ser-473'.
CC {ECO:0000269|PubMed:16203743, ECO:0000269|PubMed:16940172,
CC ECO:0000269|PubMed:17259635, ECO:0000269|PubMed:18625718}.
CC -!- SUBUNIT: Component of a histone deacetylase complex that contains
CC HDAC2, KDM1A, CTBP1 and ZNF217. May be a component of a BHC histone
CC deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A,
CC RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC Interacts with CTBP1 and CTBP2. {ECO:0000269|PubMed:12493763,
CC ECO:0000269|PubMed:16940172, ECO:0000269|PubMed:18625718}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ZNF217ID42875ch20q13.html";
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DR EMBL; AF041259; AAC39895.1; -; mRNA.
DR EMBL; AL157838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75580.1; -; Genomic_DNA.
DR EMBL; BC113427; AAI13428.1; -; mRNA.
DR CCDS; CCDS13443.1; -.
DR RefSeq; NP_006517.1; NM_006526.2.
DR RefSeq; XP_016883548.1; XM_017028059.1.
DR PDB; 2HU2; X-ray; 2.85 A; B=752-760.
DR PDB; 3UK3; X-ray; 2.10 A; C/D=469-523.
DR PDB; 4F2J; X-ray; 2.64 A; C=469-523.
DR PDB; 4IS1; X-ray; 2.10 A; C/D=469-523.
DR PDBsum; 2HU2; -.
DR PDBsum; 3UK3; -.
DR PDBsum; 4F2J; -.
DR PDBsum; 4IS1; -.
DR AlphaFoldDB; O75362; -.
DR SMR; O75362; -.
DR BioGRID; 113547; 58.
DR CORUM; O75362; -.
DR IntAct; O75362; 27.
DR MINT; O75362; -.
DR STRING; 9606.ENSP00000360526; -.
DR iPTMnet; O75362; -.
DR PhosphoSitePlus; O75362; -.
DR BioMuta; ZNF217; -.
DR EPD; O75362; -.
DR jPOST; O75362; -.
DR MassIVE; O75362; -.
DR MaxQB; O75362; -.
DR PaxDb; O75362; -.
DR PeptideAtlas; O75362; -.
DR PRIDE; O75362; -.
DR ProteomicsDB; 49925; -.
DR Antibodypedia; 28736; 343 antibodies from 35 providers.
DR DNASU; 7764; -.
DR Ensembl; ENST00000302342.3; ENSP00000304308.3; ENSG00000171940.14.
DR Ensembl; ENST00000371471.7; ENSP00000360526.2; ENSG00000171940.14.
DR GeneID; 7764; -.
DR KEGG; hsa:7764; -.
DR MANE-Select; ENST00000371471.7; ENSP00000360526.2; NM_006526.3; NP_006517.1.
DR UCSC; uc002xwq.5; human.
DR CTD; 7764; -.
DR DisGeNET; 7764; -.
DR GeneCards; ZNF217; -.
DR HGNC; HGNC:13009; ZNF217.
DR HPA; ENSG00000171940; Low tissue specificity.
DR MIM; 602967; gene.
DR neXtProt; NX_O75362; -.
DR OpenTargets; ENSG00000171940; -.
DR PharmGKB; PA37588; -.
DR VEuPathDB; HostDB:ENSG00000171940; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159884; -.
DR HOGENOM; CLU_010747_0_0_1; -.
DR InParanoid; O75362; -.
DR OMA; HKNCRSK; -.
DR PhylomeDB; O75362; -.
DR TreeFam; TF332241; -.
DR PathwayCommons; O75362; -.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; O75362; -.
DR SIGNOR; O75362; -.
DR BioGRID-ORCS; 7764; 267 hits in 1121 CRISPR screens.
DR ChiTaRS; ZNF217; human.
DR EvolutionaryTrace; O75362; -.
DR GeneWiki; ZNF217; -.
DR GenomeRNAi; 7764; -.
DR Pharos; O75362; Tbio.
DR PRO; PR:O75362; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O75362; protein.
DR Bgee; ENSG00000171940; Expressed in endometrium epithelium and 175 other tissues.
DR ExpressionAtlas; O75362; baseline and differential.
DR Genevisible; O75362; HS.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IDA:NTNU_SB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR IDEAL; IID00188; -.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1048
FT /note="Zinc finger protein 217"
FT /id="PRO_0000047460"
FT ZN_FING 65..88
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 128..150
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 156..178
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 216..238
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 375..397
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 471..493
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 499..521
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 242..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 648
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 819
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 323
FT /note="D -> N (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs767530299)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035572"
FT VARIANT 739
FT /note="V -> I (in dbSNP:rs6063966)"
FT /id="VAR_052795"
FT VARIANT 889
FT /note="D -> G (in dbSNP:rs34323943)"
FT /id="VAR_061939"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:3UK3"
FT HELIX 483..494
FT /evidence="ECO:0007829|PDB:3UK3"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:3UK3"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:3UK3"
FT HELIX 511..521
FT /evidence="ECO:0007829|PDB:3UK3"
SQ SEQUENCE 1048 AA; 115272 MW; 797FC620817D1E1F CRC64;
MQSKVTGNMP TQSLLMYMDG PEVIGSSLGS PMEMEDALSM KGTAVVPFRA TQEKNVIQIE
GYMPLDCMFC SQTFTHSEDL NKHVLMQHRP TLCEPAVLRV EAEYLSPLDK SQVRTEPPKE
KNCKENEFSC EVCGQTFRVA FDVEIHMRTH KDSFTYGCNM CGRRFKEPWF LKNHMRTHNG
KSGARSKLQQ GLESSPATIN EVVQVHAAES ISSPYKICMV CGFLFPNKES LIEHRKVHTK
KTAFGTSSAQ TDSPQGGMPS SREDFLQLFN LRPKSHPETG KKPVRCIPQL DPFTTFQAWQ
LATKGKVAIC QEVKESGQEG STDNDDSSSE KELGETNKGS CAGLSQEKEK CKHSHGEAPS
VDADPKLPSS KEKPTHCSEC GKAFRTYHQL VLHSRVHKKD RRAGAESPTM SVDGRQPGTC
SPDLAAPLDE NGAVDRGEGG SEDGSEDGLP EGIHLDKNDD GGKIKHLTSS RECSYCGKFF
RSNYYLNIHL RTHTGEKPYK CEFCEYAAAQ KTSLRYHLER HHKEKQTDVA AEVKNDGKNQ
DTEDALLTAD SAQTKNLKRF FDGAKDVTGS PPAKQLKEMP SVFQNVLGSA VLSPAHKDTQ
DFHKNAADDS ADKVNKNPTP AYLDLLKKRS AVETQANNLI CRTKADVTPP PDGSTTHNLE
VSPKEKQTET AADCRYRPSV DCHEKPLNLS VGALHNCPAI SLSKSLIPSI TCPFCTFKTF
YPEVLMMHQR LEHKYNPDVH KNCRNKSLLR SRRTGCPPAL LGKDVPPLSS FCKPKPKSAF
PAQSKSLPSA KGKQSPPGPG KAPLTSGIDS STLAPSNLKS HRPQQNVGVQ GAATRQQQSE
MFPKTSVSPA PDKTKRPETK LKPLPVAPSQ PTLGSSNING SIDYPAKNDS PWAPPGRDYF
CNRSASNTAA EFGEPLPKRL KSSVVALDVD QPGANYRRGY DLPKYHMVRG ITSLLPQDCV
YPSQALPPKP RFLSSSEVDS PNVLTVQKPY GGSGPLYTCV PAGSPASSST LEGKRPVSYQ
HLSNSMAQKR NYENFIGNAH YRPNDKKT
