ZN33A_HUMAN
ID ZN33A_HUMAN Reviewed; 810 AA.
AC Q06730; A8K9X9; B4E0M8; F6TH33; F8WAJ5; P17013; Q5VZ86;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Zinc finger protein 33A;
DE AltName: Full=Zinc finger and ZAK-associated protein with KRAB domain;
DE Short=ZZaPK;
DE AltName: Full=Zinc finger protein 11A;
DE AltName: Full=Zinc finger protein KOX31;
GN Name=ZNF33A; Synonyms=KIAA0065, KOX31, ZNF11, ZNF11A, ZNF33;
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 INTERACTION WITH MAP3K20.
RX PubMed=12535642; DOI=10.1016/s0006-291x(02)02980-7;
RA Yang J.-J.;
RT "A novel zinc finger protein, ZZaPK, interacts with ZAK and stimulates the
RT ZAK-expressing cells re-entering the cell cycle.";
RL Biochem. Biophys. Res. Commun. 301:71-77(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP GLU-549.
RC TISSUE=Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 139-361 AND 629-810 (ISOFORM
RP 1).
RX PubMed=8464732; DOI=10.1093/nar/21.6.1409;
RA Tunnacliffe A., Liu L., Moore J.K., Leversha M.A., Jackson M.S.,
RA Ferguson-Smith M.A., Thiesen H.-J., Ponder B.A.;
RT "Duplicated KOX zinc finger gene clusters flank the centromere of human
RT chromosome 10: evidence for a pericentric inversion during primate
RT evolution.";
RL Nucleic Acids Res. 21:1409-1417(1993).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-180, 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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-180, 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-180; LYS-237; LYS-312; LYS-456;
RP LYS-676 AND LYS-732, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-72 AND
RP LYS-92 (ISOFORM 2), 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: May be involved in transcriptional regulation.
CC -!- SUBUNIT: Interacts with MAP3K20/ZAK. {ECO:0000269|PubMed:12535642}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q06730-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q06730-2; Sequence=VSP_046420;
CC Name=3;
CC IsoId=Q06730-3; Sequence=VSP_055165;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY184389; AAO24702.1; -; mRNA.
DR EMBL; D31763; BAA06541.1; -; mRNA.
DR EMBL; AK292844; BAF85533.1; -; mRNA.
DR EMBL; AK303445; BAG64490.1; -; mRNA.
DR EMBL; AL161931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL117337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X68686; CAA48645.1; -; Genomic_DNA.
DR EMBL; X68687; CAA48646.1; -; mRNA.
DR EMBL; X68689; CAA48648.1; -; Genomic_DNA.
DR CCDS; CCDS31182.1; -. [Q06730-1]
DR CCDS; CCDS44372.1; -. [Q06730-2]
DR CCDS; CCDS60514.1; -. [Q06730-3]
DR PIR; S33991; S33991.
DR PIR; S33992; S33990.
DR RefSeq; NP_001265099.1; NM_001278170.1. [Q06730-3]
DR RefSeq; NP_001265100.1; NM_001278171.1.
DR RefSeq; NP_001265102.1; NM_001278173.1.
DR RefSeq; NP_001265103.1; NM_001278174.1.
DR RefSeq; NP_001265104.1; NM_001278175.1.
DR RefSeq; NP_001265105.1; NM_001278176.1.
DR RefSeq; NP_001265106.1; NM_001278177.1.
DR RefSeq; NP_001265107.1; NM_001278178.1.
DR RefSeq; NP_001265108.1; NM_001278179.1.
DR RefSeq; NP_008885.1; NM_006954.1. [Q06730-2]
DR RefSeq; NP_008905.1; NM_006974.2. [Q06730-1]
DR RefSeq; XP_011517952.1; XM_011519650.2. [Q06730-2]
DR RefSeq; XP_011517953.1; XM_011519651.2. [Q06730-1]
DR AlphaFoldDB; Q06730; -.
DR SMR; Q06730; -.
DR BioGRID; 113410; 9.
DR IntAct; Q06730; 6.
DR STRING; 9606.ENSP00000304268; -.
DR iPTMnet; Q06730; -.
DR PhosphoSitePlus; Q06730; -.
DR BioMuta; ZNF33A; -.
DR DMDM; 11140929; -.
DR jPOST; Q06730; -.
DR MassIVE; Q06730; -.
DR MaxQB; Q06730; -.
DR PaxDb; Q06730; -.
DR PeptideAtlas; Q06730; -.
DR PRIDE; Q06730; -.
DR ProteomicsDB; 27974; -.
DR ProteomicsDB; 30512; -.
DR ProteomicsDB; 58475; -. [Q06730-1]
DR Antibodypedia; 26733; 88 antibodies from 16 providers.
DR DNASU; 7581; -.
DR Ensembl; ENST00000432900.7; ENSP00000402467.3; ENSG00000189180.16. [Q06730-2]
DR Ensembl; ENST00000458705.6; ENSP00000387713.2; ENSG00000189180.16. [Q06730-1]
DR Ensembl; ENST00000628825.2; ENSP00000485869.1; ENSG00000189180.16. [Q06730-3]
DR GeneID; 7581; -.
DR KEGG; hsa:7581; -.
DR MANE-Select; ENST00000432900.7; ENSP00000402467.3; NM_006954.2; NP_008885.1. [Q06730-2]
DR UCSC; uc001izg.4; human. [Q06730-1]
DR CTD; 7581; -.
DR GeneCards; ZNF33A; -.
DR HGNC; HGNC:13096; ZNF33A.
DR HPA; ENSG00000189180; Low tissue specificity.
DR MIM; 194521; gene.
DR neXtProt; NX_Q06730; -.
DR OpenTargets; ENSG00000189180; -.
DR PharmGKB; PA37671; -.
DR VEuPathDB; HostDB:ENSG00000189180; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162173; -.
DR HOGENOM; CLU_002678_0_12_1; -.
DR InParanoid; Q06730; -.
DR OMA; TEGNDCE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q06730; -.
DR TreeFam; TF337898; -.
DR PathwayCommons; Q06730; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q06730; -.
DR BioGRID-ORCS; 7581; 6 hits in 1089 CRISPR screens.
DR ChiTaRS; ZNF33A; human.
DR GeneWiki; ZNF33A; -.
DR GenomeRNAi; 7581; -.
DR Pharos; Q06730; Tbio.
DR PRO; PR:Q06730; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q06730; protein.
DR Bgee; ENSG00000189180; Expressed in cerebellar vermis and 192 other tissues.
DR ExpressionAtlas; Q06730; baseline and differential.
DR Genevisible; Q06730; 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:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
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 GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
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; 15.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16.
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..810
FT /note="Zinc finger protein 33A"
FT /id="PRO_0000047363"
FT DOMAIN 12..83
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 328..350
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 468..490
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 524..546
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 552..574
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 580..602
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 608..630
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 636..658
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 664..686
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 692..714
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 720..742
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 748..770
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 180
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:28112733"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 312
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 456
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 676
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 732
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..3
FT /note="MNK -> MANATRRGSG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055165"
FT VAR_SEQ 83
FT /note="P -> PE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046420"
FT VARIANT 549
FT /note="Q -> E (in dbSNP:rs2505232)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_052749"
FT VARIANT 614
FT /note="G -> R (in dbSNP:rs12256916)"
FT /id="VAR_052750"
FT VARIANT 804
FT /note="D -> H (in dbSNP:rs10508862)"
FT /id="VAR_052751"
FT CONFLICT 129
FT /note="V -> A (in Ref. 3; BAG64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="C -> R (in Ref. 3; BAG64490)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="Q -> H (in Ref. 3; BAF85533)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="E -> K (in Ref. 3; BAF85533)"
FT /evidence="ECO:0000305"
FT CROSSLNK Q06730-2:72
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q06730-2:92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 810 AA; 94384 MW; 96AD969EF541B73E CRC64;
MNKVEQKSQE SVSFKDVTVG FTQEEWQHLD PSQRALYRDV MLENYSNLVS VGYCVHKPEV
IFRLQQGEEP WKQEEEFPSQ SFPVWTADHL KERSQENQSK HLWEVVFINN EMLTKEQGDV
IGIPFNVDVS SFPSRKMFCQ CDSCGMSFNT VSELVISKIN YLGKKSDEFN ACGKLLLNIK
HDETHTQEKN EVLKNRNTLS HHEETLQHEK IQTLEHNFEY SICQETLLEK AVFNTQKREN
AEENNCDYNE FGRTLCDSSS LLFHQISPSR DNHYEFSDCE KFLCVKSTLS KPHGVSMKHY
DCGESGNNFR RKLCLSHLQK GDKGEKHFEC NECGKAFWEK SHLTRHQRVH TGQKPFQCNE
CEKAFWDKSN LTKHQRSHTG EKPFECNECG KAFSHKSALT LHQRTHTGEK PYQCNACGKT
FCQKSDLTKH QRTHTGLKPY ECYECGKSFR VTSHLKVHQR THTGEKPFEC LECGKSFSEK
SNLTQHQRIH IGDKSYECNA CGKTFYHKSL LTRHQIIHTG WKPYECYECG KTFCLKSDLT
VHQRTHTGQK PFACPECGKF FSHKSTLSQH YRTHTGEKPY ECHECGKIFY NKSYLTKHNR
THTGEKPYEC NECGKAFYQK SQLTQHQRIH IGEKPYKCNE CGKAFCHKSA LIVHQRTHTQ
EKPYKCNECG KSFCVKSGLI FHERKHTGEK PYECNECGKF FRHKSSLTVH HRAHTGEKSC
QCNECGKIFY RKSELAQHQR SHTGEKPYEC NTCRKTFSQK SNLIVHQRRH IGENLMNEMD
IRNFQPQVSL HNASEYSHCG ESPDDILNVQ
