ZBTB2_HUMAN
ID ZBTB2_HUMAN Reviewed; 514 AA.
AC Q8N680; A8K7C7; Q5SZ81; Q9P245;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger and BTB domain-containing protein 2;
GN Name=ZBTB2; Synonyms=KIAA1483, ZNF437;
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].
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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=Melanoma;
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 [LARGE SCALE MRNA] OF 87-514.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-505, 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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-505, 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-362 AND LYS-505, AND
RP IDENTIFICATION BY MASS 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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-147; LYS-154; LYS-362; LYS-465;
RP LYS-505 AND LYS-506, 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 -!- INTERACTION:
CC Q8N680; Q9UER7: DAXX; NbExp=3; IntAct=EBI-2515601, EBI-77321;
CC Q8N680; P60520: GABARAPL2; NbExp=3; IntAct=EBI-2515601, EBI-720116;
CC Q8N680; Q9UHH9: IP6K2; NbExp=3; IntAct=EBI-2515601, EBI-747509;
CC Q8N680; Q92993: KAT5; NbExp=3; IntAct=EBI-2515601, EBI-399080;
CC Q8N680; Q969G2: LHX4; NbExp=3; IntAct=EBI-2515601, EBI-2865388;
CC Q8N680; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2515601, EBI-739832;
CC Q8N680; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2515601, EBI-16439278;
CC Q8N680; Q9UL63: MKLN1; NbExp=3; IntAct=EBI-2515601, EBI-1048053;
CC Q8N680; P00540: MOS; NbExp=3; IntAct=EBI-2515601, EBI-1757866;
CC Q8N680; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-2515601, EBI-5453723;
CC Q8N680; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2515601, EBI-79165;
CC Q8N680; Q13526: PIN1; NbExp=3; IntAct=EBI-2515601, EBI-714158;
CC Q8N680; Q8NHQ8-2: RASSF8; NbExp=4; IntAct=EBI-2515601, EBI-10976415;
CC Q8N680; P08047: SP1; NbExp=4; IntAct=EBI-2515601, EBI-298336;
CC Q8N680; P63165: SUMO1; NbExp=3; IntAct=EBI-2515601, EBI-80140;
CC Q8N680; O43463: SUV39H1; NbExp=3; IntAct=EBI-2515601, EBI-349968;
CC Q8N680; Q96A09: TENT5B; NbExp=3; IntAct=EBI-2515601, EBI-752030;
CC Q8N680; Q7Z403: TMC6; NbExp=3; IntAct=EBI-2515601, EBI-9088037;
CC Q8N680; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-2515601, EBI-10180829;
CC Q8N680; Q99592: ZBTB18; NbExp=3; IntAct=EBI-2515601, EBI-3232046;
CC Q8N680; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-2515601, EBI-2515601;
CC Q8N680; P24278: ZBTB25; NbExp=3; IntAct=EBI-2515601, EBI-739899;
CC Q8N680; Q6ZSB9: ZBTB49; NbExp=3; IntAct=EBI-2515601, EBI-2859943;
CC Q8N680; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-2515601, EBI-746595;
CC Q8N680; Q9UID6: ZNF639; NbExp=5; IntAct=EBI-2515601, EBI-947476;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; AK291942; BAF84631.1; -; mRNA.
DR EMBL; AL590413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47751.1; -; Genomic_DNA.
DR EMBL; BC020172; AAH20172.1; -; mRNA.
DR EMBL; AB040916; BAA96007.1; -; mRNA.
DR CCDS; CCDS5231.1; -.
DR RefSeq; NP_065912.1; NM_020861.2.
DR RefSeq; XP_005267133.1; XM_005267076.2.
DR RefSeq; XP_011534306.1; XM_011536004.2.
DR AlphaFoldDB; Q8N680; -.
DR BioGRID; 121667; 457.
DR DIP; DIP-53681N; -.
DR IntAct; Q8N680; 45.
DR MINT; Q8N680; -.
DR STRING; 9606.ENSP00000323183; -.
DR iPTMnet; Q8N680; -.
DR PhosphoSitePlus; Q8N680; -.
DR SwissPalm; Q8N680; -.
DR BioMuta; ZBTB2; -.
DR DMDM; 30316315; -.
DR EPD; Q8N680; -.
DR jPOST; Q8N680; -.
DR MassIVE; Q8N680; -.
DR MaxQB; Q8N680; -.
DR PaxDb; Q8N680; -.
DR PeptideAtlas; Q8N680; -.
DR PRIDE; Q8N680; -.
DR ProteomicsDB; 72136; -.
DR Antibodypedia; 19926; 162 antibodies from 29 providers.
DR DNASU; 57621; -.
DR Ensembl; ENST00000325144.5; ENSP00000323183.4; ENSG00000181472.5.
DR GeneID; 57621; -.
DR KEGG; hsa:57621; -.
DR MANE-Select; ENST00000325144.5; ENSP00000323183.4; NM_020861.3; NP_065912.1.
DR UCSC; uc003qoh.4; human.
DR CTD; 57621; -.
DR DisGeNET; 57621; -.
DR GeneCards; ZBTB2; -.
DR HGNC; HGNC:20868; ZBTB2.
DR HPA; ENSG00000181472; Low tissue specificity.
DR MIM; 616595; gene.
DR neXtProt; NX_Q8N680; -.
DR OpenTargets; ENSG00000181472; -.
DR PharmGKB; PA134949885; -.
DR VEuPathDB; HostDB:ENSG00000181472; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158401; -.
DR HOGENOM; CLU_025271_1_0_1; -.
DR InParanoid; Q8N680; -.
DR OMA; WGVGGLN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8N680; -.
DR TreeFam; TF332229; -.
DR PathwayCommons; Q8N680; -.
DR SignaLink; Q8N680; -.
DR BioGRID-ORCS; 57621; 56 hits in 1139 CRISPR screens.
DR ChiTaRS; ZBTB2; human.
DR GenomeRNAi; 57621; -.
DR Pharos; Q8N680; Tbio.
DR PRO; PR:Q8N680; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8N680; protein.
DR Bgee; ENSG00000181472; Expressed in secondary oocyte and 162 other tissues.
DR Genevisible; Q8N680; HS.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
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..514
FT /note="Zinc finger and BTB domain-containing protein 2"
FT /id="PRO_0000047709"
FT DOMAIN 24..89
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 254..276
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 363..385
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 390..410
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 448..468
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 149..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 147
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 362
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 505
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:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 506
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 466
FT /note="H -> L (in Ref. 5; BAA96007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 57337 MW; 2087A104CCA3DD85 CRC64;
MDLANHGLIL LQQLNAQREF GFLCDCTVAI GDVYFKAHKS VLASFSNYFK MLFVHQTSEC
VRLKPTDIQP DIFSYLLHLM YTGKMAPQLI DPVRLEQGIK FLHAYPLIQE ASLASQGAFS
HPDQVFPLAS SLYGIQIADH QLRQATKIAS APEKLGRDPR PQTSRISQEQ VPEASQLSQL
TSNLAQVNRT NMTPSDPLQT SLSPELVSTP VPPPPPGEET NLEASSSDEQ PASLTIAHVK
PSIMKRNGSF PKYYACHLCG RRFTLRSSLR EHLQIHTGVP FTSSQQGESR VPLTLCSNAA
DLGKDAMEVP EAGMISDSEL QHISDSPIID GQQQSETPPP SDIADIDNLE QADQEREVKR
RKYECTICGR KFIQKSHWRE HMYIHTGKPF KCSTCDKSFC RANQAARHVC LNQSIDTYTM
VDKQTLELCT FEEGSQMDNM LVQTNKPYKC NLCDKTFSTP NEVVKHSCQN QNSDVFALDE
GRSILLGSGD SEVTEPDHPV LASIKKEQET VLLD
