ZN180_HUMAN
ID ZN180_HUMAN Reviewed; 692 AA.
AC Q9UJW8; B2RCN6; B3KV56; K7EQX9; Q58F03; Q9P1U2;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Zinc finger protein 180;
DE AltName: Full=HHZ168;
GN Name=ZNF180;
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 1), AND VARIANTS VAL-41; CYS-89 AND
RP SER-272.
RX PubMed=12743021; DOI=10.1101/gr.963903;
RA Shannon M., Hamilton A.T., Gordon L., Branscomb E., Stubbs L.;
RT "Differential expansion of zinc-finger transcription factor loci in
RT homologous human and mouse gene clusters.";
RL Genome Res. 13:1097-1110(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP VAL-41; CYS-89 AND SER-272 (ISOFORM 3).
RC TISSUE=Amygdala, and Spleen;
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].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-138, 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-138, 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-138; LYS-159; LYS-168; LYS-191;
RP LYS-198; LYS-226; LYS-304; LYS-313 AND LYS-330, 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 be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q9UJW8; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-10322527, EBI-2125614;
CC Q9UJW8; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10322527, EBI-10172290;
CC Q9UJW8; Q9GZM8: NDEL1; NbExp=4; IntAct=EBI-10322527, EBI-928842;
CC Q9UJW8-4; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-12055755, EBI-3866279;
CC Q9UJW8-4; Q96Q77: CIB3; NbExp=3; IntAct=EBI-12055755, EBI-10292696;
CC Q9UJW8-4; G5E9A7: DMWD; NbExp=3; IntAct=EBI-12055755, EBI-10976677;
CC Q9UJW8-4; P28799: GRN; NbExp=3; IntAct=EBI-12055755, EBI-747754;
CC Q9UJW8-4; P28799-2: GRN; NbExp=3; IntAct=EBI-12055755, EBI-25860013;
CC Q9UJW8-4; P42858: HTT; NbExp=9; IntAct=EBI-12055755, EBI-466029;
CC Q9UJW8-4; O60333-2: KIF1B; NbExp=3; IntAct=EBI-12055755, EBI-10975473;
CC Q9UJW8-4; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-12055755, EBI-14069005;
CC Q9UJW8-4; I6L9F6: NEFL; NbExp=3; IntAct=EBI-12055755, EBI-10178578;
CC Q9UJW8-4; P07196: NEFL; NbExp=3; IntAct=EBI-12055755, EBI-475646;
CC Q9UJW8-4; O43933: PEX1; NbExp=3; IntAct=EBI-12055755, EBI-988601;
CC Q9UJW8-4; P60891: PRPS1; NbExp=3; IntAct=EBI-12055755, EBI-749195;
CC Q9UJW8-4; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-12055755, EBI-396669;
CC Q9UJW8-4; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-12055755, EBI-5235340;
CC Q9UJW8-4; O76024: WFS1; NbExp=3; IntAct=EBI-12055755, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UJW8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJW8-2; Sequence=VSP_056706;
CC Name=3;
CC IsoId=Q9UJW8-3; Sequence=VSP_056707;
CC Name=4;
CC IsoId=Q9UJW8-4; Sequence=VSP_056705;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF192913; AAF07950.1; -; mRNA.
DR EMBL; AK122688; BAG53668.1; -; mRNA.
DR EMBL; AK315193; BAG37633.1; -; mRNA.
DR EMBL; AC069278; AAF71790.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57275.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57276.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57279.1; -; Genomic_DNA.
DR EMBL; BC033642; AAH33642.1; -; mRNA.
DR EMBL; BC113015; AAI13016.1; -; mRNA.
DR CCDS; CCDS12639.1; -. [Q9UJW8-1]
DR CCDS; CCDS62707.1; -. [Q9UJW8-2]
DR CCDS; CCDS62708.1; -. [Q9UJW8-3]
DR RefSeq; NP_001265437.2; NM_001278508.2.
DR RefSeq; NP_001265438.2; NM_001278509.2.
DR RefSeq; NP_001275688.2; NM_001288759.2.
DR RefSeq; NP_001275689.1; NM_001288760.2.
DR RefSeq; NP_001275690.1; NM_001288761.2.
DR RefSeq; NP_001275691.1; NM_001288762.2.
DR RefSeq; NP_001278562.1; NM_001291633.1.
DR RefSeq; NP_037388.3; NM_013256.5.
DR AlphaFoldDB; Q9UJW8; -.
DR SMR; Q9UJW8; -.
DR BioGRID; 113521; 7.
DR IntAct; Q9UJW8; 18.
DR STRING; 9606.ENSP00000221327; -.
DR iPTMnet; Q9UJW8; -.
DR PhosphoSitePlus; Q9UJW8; -.
DR BioMuta; ZNF180; -.
DR DMDM; 134044257; -.
DR EPD; Q9UJW8; -.
DR MassIVE; Q9UJW8; -.
DR MaxQB; Q9UJW8; -.
DR PaxDb; Q9UJW8; -.
DR PeptideAtlas; Q9UJW8; -.
DR PRIDE; Q9UJW8; -.
DR ProteomicsDB; 84675; -. [Q9UJW8-1]
DR Antibodypedia; 31184; 91 antibodies from 20 providers.
DR DNASU; 7733; -.
DR Ensembl; ENST00000221327.8; ENSP00000221327.3; ENSG00000167384.11.
DR GeneID; 7733; -.
DR KEGG; hsa:7733; -.
DR UCSC; uc002ozf.6; human. [Q9UJW8-1]
DR CTD; 7733; -.
DR GeneCards; ZNF180; -.
DR HGNC; HGNC:12970; ZNF180.
DR HPA; ENSG00000167384; Low tissue specificity.
DR MIM; 606740; gene.
DR neXtProt; NX_Q9UJW8; -.
DR PharmGKB; PA37552; -.
DR VEuPathDB; HostDB:ENSG00000167384; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_002678_35_3_1; -.
DR InParanoid; Q9UJW8; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9UJW8; -.
DR TreeFam; TF350793; -.
DR PathwayCommons; Q9UJW8; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9UJW8; -.
DR BioGRID-ORCS; 7733; 6 hits in 1097 CRISPR screens.
DR ChiTaRS; ZNF180; human.
DR GenomeRNAi; 7733; -.
DR Pharos; Q9UJW8; Tdark.
DR PRO; PR:Q9UJW8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UJW8; protein.
DR Bgee; ENSG00000167384; Expressed in endothelial cell and 133 other tissues.
DR ExpressionAtlas; Q9UJW8; baseline and differential.
DR Genevisible; Q9UJW8; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
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; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
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..692
FT /note="Zinc finger protein 180"
FT /id="PRO_0000047442"
FT DOMAIN 72..145
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 353..375
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 381..403
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 409..431
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 437..459
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 465..487
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 493..515
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 521..543
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 549..571
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 577..599
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 605..627
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 633..655
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 661..683
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056706"
FT VAR_SEQ 1..14
FT /note="MRACAGSTREAGSG -> MRRVYAGSWKRCA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056705"
FT VAR_SEQ 41..69
FT /note="ACAQDSFLPQEIIIKVEGEDTGSLTIPSQ -> ACAQ (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056707"
FT VARIANT 41
FT /note="A -> V (in dbSNP:rs2571108)"
FT /evidence="ECO:0000269|PubMed:12743021"
FT /id="VAR_030864"
FT VARIANT 89
FT /note="W -> C (in dbSNP:rs2253563)"
FT /evidence="ECO:0000269|PubMed:12743021"
FT /id="VAR_030865"
FT VARIANT 272
FT /note="C -> S (in dbSNP:rs1897820)"
FT /evidence="ECO:0000269|PubMed:12743021"
FT /id="VAR_030866"
FT CONFLICT 558
FT /note="F -> L (in Ref. 2; BAG53668)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 79111 MW; 689812AB1E277525 CRC64;
MRACAGSTRE AGSGAQDLST LLCLEESMEE QDEKPPEPPK ACAQDSFLPQ EIIIKVEGED
TGSLTIPSQE GVNFKIVTVD FTREEQGTWN PAQRTLDRDV ILENHRDLVS WDLATAVGKK
DSTSKQRIFD EEPANGVKIE RFTRDDPWLS SCEEVDDCKD QLEKQQEKQE ILLQEVAFTQ
RKAVIHERVC KSDETGEKSG LNSSLFSSPV IPIRNHFHKH VSHAKKWHLN AAVNSHQKIN
ENETLYENNE CGKPPQSIHL IQFTRTQTKD KCYGFSDRIQ SFCHGTPLHI HEKIHGGGKT
FDFKECGQVL NPKISHNEQQ RIPFEESQYK CSETSHSSSL TQNMRNNSEE KPFECNQCGK
SFSWSSHLVA HQRTHTGEKP YECSECGKSF SRSSHLVSHQ RTHTGEKPYR CNQCGKSFSQ
SYVLVVHQRT HTGEKPYECN QCGKSFRQSY KLIAHQRTHT GEKPYECNQC GKSFIQSYKL
IAHQRIHTGE KPYECNQCGK SFSQSYKLVA HQRTHTGEKP FECNQCGKSF SWSSQLVAHQ
RTHTGEKPYE CSECGKSFNR SSHLVMHQRI HTGEKPYECN QCGKSFSQSY VLVVHQRTHT
GEKPYECSQC GKSFRQSSCL TQHQRTHTGE KPFECNQCGK TFSLSARLIV HQRTHTGEKP
FTCIQCGKAF INSYKLIRHQ ATHTEEKLYE CN
