ZNF3_HUMAN
ID ZNF3_HUMAN Reviewed; 446 AA.
AC P17036; D6W5U0; P13683; Q9HBR4; Q9NNX8; Q9NXJ1; Q9UC15; Q9UC16;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Zinc finger protein 3;
DE AltName: Full=Zinc finger protein HF.12;
DE AltName: Full=Zinc finger protein HZF3.1;
DE AltName: Full=Zinc finger protein KOX25;
GN Name=ZNF3; Synonyms=KOX25;
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] (ISOFORM 2).
RA Gu J.R., Wan D.F., Zhao X.T., Zhou X.M., Jiang H.Q., Zhang P.P., Qin W.X.,
RA Huang Y., Qiu X.K., Qian L.F., He L.P., Li H.N., Yu Y., Yu J., Han L.H.;
RT "Novel Human cDNA clones with function of inhibiting cancer cell growth.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-387 (ISOFORM 1).
RC TISSUE=Colon mucosa;
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 [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] (ISOFORM 1).
RC TISSUE=Ovary, and 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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-250 (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RX PubMed=1945843; DOI=10.1093/nar/19.20.5661;
RA Rosati M., Marino M., Franze A., Tramontano A., Grimaldi G.;
RT "Members of the zinc finger protein gene family sharing a conserved N-
RT terminal module.";
RL Nucleic Acids Res. 19:5661-5667(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 340-395.
RC TISSUE=Lymphoid tissue;
RX PubMed=2288909;
RA Thiesen H.-J.;
RT "Multiple genes encoding zinc finger domains are expressed in human T
RT cells.";
RL New Biol. 2:363-374(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 252-446.
RC TISSUE=Placenta;
RX PubMed=3380682; DOI=10.1093/nar/16.10.4227;
RA Pannuti A., Lanfrancone L., Pascucci A., Pelicci P.-G., la Mantia G.,
RA Lania L.;
RT "Isolation of cDNAs encoding finger proteins and measurement of the
RT corresponding mRNA levels during myeloid terminal differentiation.";
RL Nucleic Acids Res. 16:4227-4237(1988).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-419, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-151, 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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-125; LYS-151; LYS-163; LYS-173;
RP LYS-422 AND LYS-431, 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).
CC -!- FUNCTION: Involved in cell differentiation and/or proliferation.
CC -!- INTERACTION:
CC P17036; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1640965, EBI-618309;
CC P17036; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-1640965, EBI-3044087;
CC P17036; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-1640965, EBI-1216080;
CC P17036; P23508: MCC; NbExp=3; IntAct=EBI-1640965, EBI-307531;
CC P17036; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-1640965, EBI-742948;
CC P17036; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-1640965, EBI-928842;
CC P17036; Q15427: SF3B4; NbExp=3; IntAct=EBI-1640965, EBI-348469;
CC P17036; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-1640965, EBI-2212028;
CC P17036; Q9BUZ4: TRAF4; NbExp=8; IntAct=EBI-1640965, EBI-3650647;
CC P17036; P13994: YJU2B; NbExp=5; IntAct=EBI-1640965, EBI-716093;
CC P17036; Q9UDV6: ZNF212; NbExp=4; IntAct=EBI-1640965, EBI-1640204;
CC P17036; P17036: ZNF3; NbExp=2; IntAct=EBI-1640965, EBI-1640965;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P17036-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P17036-2; Sequence=VSP_041156;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF217988; AAG17231.1; -; mRNA.
DR EMBL; AF193057; AAG22485.1; -; mRNA.
DR EMBL; AK000223; BAA91019.1; -; mRNA.
DR EMBL; AK297625; BAH12633.1; -; mRNA.
DR EMBL; CH471091; EAW76605.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76606.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76608.1; -; Genomic_DNA.
DR EMBL; BC011887; AAH11887.2; -; mRNA.
DR EMBL; BC013603; AAH13603.2; -; mRNA.
DR EMBL; X60153; CAB94195.1; -; mRNA.
DR EMBL; X52356; CAA36582.1; -; mRNA.
DR EMBL; X07290; CAA30269.1; -; mRNA.
DR CCDS; CCDS43618.1; -. [P17036-2]
DR CCDS; CCDS43619.1; -. [P17036-1]
DR PIR; S00754; S00754.
DR RefSeq; NP_001265213.1; NM_001278284.1. [P17036-1]
DR RefSeq; NP_001265216.1; NM_001278287.1. [P17036-1]
DR RefSeq; NP_001265219.1; NM_001278290.1. [P17036-1]
DR RefSeq; NP_001305064.1; NM_001318135.1. [P17036-1]
DR RefSeq; NP_001305065.1; NM_001318136.1.
DR RefSeq; NP_001305066.1; NM_001318137.1.
DR RefSeq; NP_060185.2; NM_017715.3. [P17036-2]
DR RefSeq; NP_116313.3; NM_032924.4. [P17036-1]
DR AlphaFoldDB; P17036; -.
DR SMR; P17036; -.
DR BioGRID; 113383; 29.
DR IntAct; P17036; 22.
DR STRING; 9606.ENSP00000306372; -.
DR iPTMnet; P17036; -.
DR PhosphoSitePlus; P17036; -.
DR BioMuta; ZNF3; -.
DR DMDM; 46577682; -.
DR EPD; P17036; -.
DR jPOST; P17036; -.
DR MassIVE; P17036; -.
DR MaxQB; P17036; -.
DR PaxDb; P17036; -.
DR PeptideAtlas; P17036; -.
DR PRIDE; P17036; -.
DR ProteomicsDB; 53438; -. [P17036-1]
DR ProteomicsDB; 53439; -. [P17036-2]
DR Antibodypedia; 832; 123 antibodies from 22 providers.
DR DNASU; 7551; -.
DR Ensembl; ENST00000299667.9; ENSP00000299667.4; ENSG00000166526.18. [P17036-1]
DR Ensembl; ENST00000303915.10; ENSP00000306372.6; ENSG00000166526.18. [P17036-1]
DR Ensembl; ENST00000413658.6; ENSP00000399951.2; ENSG00000166526.18. [P17036-2]
DR Ensembl; ENST00000424697.5; ENSP00000415358.1; ENSG00000166526.18. [P17036-1]
DR GeneID; 7551; -.
DR KEGG; hsa:7551; -.
DR MANE-Select; ENST00000299667.9; ENSP00000299667.4; NM_032924.5; NP_116313.3.
DR UCSC; uc003usp.5; human. [P17036-1]
DR CTD; 7551; -.
DR DisGeNET; 7551; -.
DR GeneCards; ZNF3; -.
DR HGNC; HGNC:13089; ZNF3.
DR HPA; ENSG00000166526; Low tissue specificity.
DR MIM; 194510; gene.
DR MIM; 601261; gene.
DR neXtProt; NX_P17036; -.
DR OpenTargets; ENSG00000166526; -.
DR PharmGKB; PA37664; -.
DR VEuPathDB; HostDB:ENSG00000166526; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000153104; -.
DR HOGENOM; CLU_1980905_0_0_1; -.
DR InParanoid; P17036; -.
DR OMA; MGDRPHK; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P17036; -.
DR TreeFam; TF337732; -.
DR PathwayCommons; P17036; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; P17036; -.
DR BioGRID-ORCS; 7551; 10 hits in 1102 CRISPR screens.
DR ChiTaRS; ZNF3; human.
DR GeneWiki; ZNF3; -.
DR GenomeRNAi; 7551; -.
DR Pharos; P17036; Tbio.
DR PRO; PR:P17036; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P17036; protein.
DR Bgee; ENSG00000166526; Expressed in right uterine tube and 170 other tissues.
DR ExpressionAtlas; P17036; baseline and differential.
DR Genevisible; P17036; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045321; P:leukocyte activation; NAS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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; 8.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Developmental protein; Differentiation;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..446
FT /note="Zinc finger protein 3"
FT /id="PRO_0000047368"
FT DOMAIN 51..123
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 200..222
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 228..250
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 256..278
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 284..306
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 312..334
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 340..362
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 368..390
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 396..418
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 431
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 92..446
FT /note="RETRTENDQEISEDTRSHGVLLGRFQKDISQGLKFKEAYEREVSLKRPLGNS
FT PGERLNRKMPDFGQVTVEEKLTPRGERSEKYNDFGNSFTVNSNLISHQRLPVGDRPHKC
FT DECSKSFNRTSDLIQHQRIHTGEKPYECNECGKAFSQSSHLIQHQRIHTGEKPYECSDC
FT GKTFSCSSALILHRRIHTGEKPYECNECGKTFSWSSTLTHHQRIHTGEKPYACNECGKA
FT FSRSSTLIHHQRIHTGEKPYECNECGKAFSQSSHLYQHQRIHTGEKPYECMECGGKFTY
FT SSGLIQHQRIHTGENPYECSECGKAFRYSSALVRHQRIHTGEKPLNGIGMSKSSLRVTT
FT ELNIREST -> WIHVCLTTQKVMLAWLTGTLSVAKGLCSSELASVEPPDTF (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_041156"
FT VARIANT 102
FT /note="I -> T (in dbSNP:rs11550034)"
FT /id="VAR_052743"
FT CONFLICT 21
FT /note="P -> L (in Ref. 2; BAA91019)"
FT /evidence="ECO:0000305"
FT CONFLICT 252..256
FT /note="GEKPY -> IRDSG (in Ref. 7; CAA30269)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..387
FT /note="GEKPYECNECGKAFSQSSHLYQHQRIHTGEKPYECMECGGKFTYSSGLIQHQ
FT -> EALPTFVTLIRLLPSVDPIVTNEAAFPAESLATIFALIWRLFCVHSLMFKKV (in
FT Ref. 2; BAA91019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 50916 MW; EEF50906695779A6 CRC64;
METQADLVSQ EPQALLDSAL PSKVPAFSDK DSLGDEMLAA ALLKAKSQEL VTFEDVAVYF
IRKEWKRLEP AQRDLYRDVM LENYGNVFSL DRETRTENDQ EISEDTRSHG VLLGRFQKDI
SQGLKFKEAY EREVSLKRPL GNSPGERLNR KMPDFGQVTV EEKLTPRGER SEKYNDFGNS
FTVNSNLISH QRLPVGDRPH KCDECSKSFN RTSDLIQHQR IHTGEKPYEC NECGKAFSQS
SHLIQHQRIH TGEKPYECSD CGKTFSCSSA LILHRRIHTG EKPYECNECG KTFSWSSTLT
HHQRIHTGEK PYACNECGKA FSRSSTLIHH QRIHTGEKPY ECNECGKAFS QSSHLYQHQR
IHTGEKPYEC MECGGKFTYS SGLIQHQRIH TGENPYECSE CGKAFRYSSA LVRHQRIHTG
EKPLNGIGMS KSSLRVTTEL NIREST
