ID ZBTB4_HUMAN Reviewed; 1013 AA.
AC Q9P1Z0; B3KVL6; Q7Z697; Q86XJ4; Q8N4V8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 3.
DT 10-MAY-2017, entry version 141.
DE RecName: Full=Zinc finger and BTB domain-containing protein 4;
DE AltName: Full=KAISO-like zinc finger protein 1;
DE Short=KAISO-L1;
GN Name=ZBTB4; Synonyms=KIAA1538;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RA Weber A., Klinkhammer B., Glaum A., Bergmann E., Berwanger B.,
RA Eilers M., Christiansen H.;
RT "Identification of a novel zinc-finger-protein encoding gene on
RT 17p13.1.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP ZBTB38.
RX PubMed=16354688; DOI=10.1128/MCB.26.1.169-181.2006;
RA Filion G.J., Zhenilo S., Salozhin S., Yamada D., Prokhortchouk E.,
RA Defossez P.A.;
RT "A family of human zinc finger proteins that bind methylated DNA and
RT repress transcription.";
RL Mol. Cell. Biol. 26:169-181(2006).
RN [8]
RP PHOSPHORYLATION AT THR-795; THR-797 AND THR-983 BY HIPK2, MUTAGENESIS
RP OF THR-795; THR-797 AND THR-983, AND INTERACTION WITH HIPK2.
RX PubMed=19448668; DOI=10.1038/onc.2009.109;
RA Yamada D., Perez-Torrado R., Filion G., Caly M., Jammart B.,
RA Devignot V., Sasai N., Ravassard P., Mallet J., Sastre-Garau X.,
RA Schmitz M.L., Defossez P.A.;
RT "The human protein kinase HIPK2 phosphorylates and downregulates the
RT methyl-binding transcription factor ZBTB4.";
RL Oncogene 28:2535-2544(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP INTERACTION WITH CBFA2T3.
RX PubMed=23251453; DOI=10.1371/journal.pone.0051205;
RA Barrett C.W., Smith J.J., Lu L.C., Markham N., Stengel K.R.,
RA Short S.P., Zhang B., Hunt A.A., Fingleton B.M., Carnahan R.H.,
RA Engel M.E., Chen X., Beauchamp R.D., Wilson K.T., Hiebert S.W.,
RA Reynolds A.B., Williams C.S.;
RT "Kaiso directs the transcriptional corepressor MTG16 to the Kaiso
RT binding site in target promoters.";
RL PLoS ONE 7:E51205-E51205(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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-615, AND IDENTIFICATION BY
RP MASS 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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND IDENTIFICATION BY
RP 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
RT replication stress reveals novel small ubiquitin-like modified target
RT proteins and acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
CC -!- FUNCTION: Transcriptional repressor with bimodal DNA-binding
CC specificity. Represses transcription in a methyl-CpG-dependent
CC manner. Binds with a higher affinity to methylated CpG
CC dinucleotides in the consensus sequence 5'-CGCG-3' but can also
CC bind to the non-methylated consensus sequence 5'-CTGCNA-3' also
CC known as the consensus kaiso binding site (KBS). Can also bind
CC specifically to a single methyl-CpG pair and can bind
CC hemimethylated DNA but with a lower affinity compared to
CC methylated DNA (PubMed:16354688). {ECO:0000269|PubMed:16354688}.
CC -!- SUBUNIT: Interacts with HIPK2. Interacts with CBFA2T3. Interacts
CC with ZBTB38. {ECO:0000269|PubMed:16354688,
CC ECO:0000269|PubMed:19448668, ECO:0000269|PubMed:23251453}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16354688}.
CC Chromosome {ECO:0000269|PubMed:16354688}. Note=Localizes to
CC chromocenters. {ECO:0000269|PubMed:16354688}.
CC -!- PTM: Phosphorylated by HIPK2. This phosphorylation reduces
CC stability and triggers ZBTB4 protein degradation in response to
CC DNA damage. {ECO:0000269|PubMed:19448668}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96062.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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DR EMBL; AY302699; AAP59447.1; -; mRNA.
DR EMBL; AB040971; BAA96062.2; ALT_INIT; mRNA.
DR EMBL; AK122971; BAG53828.1; -; mRNA.
DR EMBL; CH471108; EAW90185.1; -; Genomic_DNA.
DR EMBL; BC033259; AAH33259.1; -; mRNA.
DR EMBL; BC043352; AAH43352.1; -; mRNA.
DR CCDS; CCDS11107.1; -.
DR RefSeq; NP_001122305.1; NM_001128833.1.
DR RefSeq; NP_065950.2; NM_020899.3.
DR RefSeq; XP_006721626.1; XM_006721563.3.
DR RefSeq; XP_006721627.1; XM_006721564.2.
DR RefSeq; XP_011522274.1; XM_011523972.2.
DR UniGene; Hs.35096; -.
DR ProteinModelPortal; Q9P1Z0; -.
DR SMR; Q9P1Z0; -.
DR BioGrid; 121693; 7.
DR IntAct; Q9P1Z0; 15.
DR STRING; 9606.ENSP00000307858; -.
DR iPTMnet; Q9P1Z0; -.
DR PhosphoSitePlus; Q9P1Z0; -.
DR BioMuta; ZBTB4; -.
DR DMDM; 46577564; -.
DR EPD; Q9P1Z0; -.
DR MaxQB; Q9P1Z0; -.
DR PaxDb; Q9P1Z0; -.
DR PeptideAtlas; Q9P1Z0; -.
DR PRIDE; Q9P1Z0; -.
DR Ensembl; ENST00000311403; ENSP00000307858; ENSG00000174282.
DR Ensembl; ENST00000380599; ENSP00000369973; ENSG00000174282.
DR GeneID; 57659; -.
DR KEGG; hsa:57659; -.
DR UCSC; uc002ghc.5; human.
DR CTD; 57659; -.
DR DisGeNET; 57659; -.
DR GeneCards; ZBTB4; -.
DR HGNC; HGNC:23847; ZBTB4.
DR HPA; CAB008980; -.
DR HPA; HPA064763; -.
DR MIM; 612308; gene.
DR neXtProt; NX_Q9P1Z0; -.
DR OpenTargets; ENSG00000174282; -.
DR PharmGKB; PA134959224; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; COG5048; LUCA.
DR GeneTree; ENSGT00810000125416; -.
DR HOGENOM; HOG000065759; -.
DR HOVERGEN; HBG055508; -.
DR InParanoid; Q9P1Z0; -.
DR KO; K10491; -.
DR OMA; NMVLPDE; -.
DR OrthoDB; EOG091G01R6; -.
DR PhylomeDB; Q9P1Z0; -.
DR TreeFam; TF333100; -.
DR ChiTaRS; ZBTB4; human.
DR GenomeRNAi; 57659; -.
DR PRO; PR:Q9P1Z0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR Bgee; ENSG00000174282; -.
DR CleanEx; HS_ZBTB4; -.
DR Genevisible; Q9P1Z0; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0010428; F:methyl-CpNpG binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:NTNU_SB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF54695; SSF54695; 2.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Complete proteome; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1 1013 Zinc finger and BTB domain-containing
FT protein 4.
FT /FTId=PRO_0000047712.
FT DOMAIN 30 152 BTB. {ECO:0000255|PROSITE-
FT ProRule:PRU00037}.
FT ZN_FING 234 256 C2H2-type 1; atypical.
FT {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT ZN_FING 309 331 C2H2-type 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 337 359 C2H2-type 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 365 388 C2H2-type 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 726 748 C2H2-type 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 765 787 C2H2-type 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT REGION 186 348 Interaction with CBFA2T3.
FT {ECO:0000269|PubMed:23251453}.
FT COILED 627 663 {ECO:0000255}.
FT COMPBIAS 435 536 Pro-rich.
FT COMPBIAS 610 654 Glu-rich.
FT MOD_RES 391 391 Phosphoserine.
FT {ECO:0000244|PubMed:20068231,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 795 795 Phosphothreonine; by HIPK2.
FT {ECO:0000269|PubMed:19448668}.
FT MOD_RES 797 797 Phosphothreonine; by HIPK2.
FT {ECO:0000269|PubMed:19448668}.
FT MOD_RES 983 983 Phosphothreonine; by HIPK2.
FT {ECO:0000269|PubMed:19448668}.
FT CROSSLNK 40 40 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO2).
FT {ECO:0000244|PubMed:25755297}.
FT CROSSLNK 615 615 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO2).
FT {ECO:0000244|PubMed:25218447}.
FT VARIANT 539 539 A -> V (in dbSNP:rs35231078).
FT /FTId=VAR_052913.
FT VARIANT 550 550 M -> I (in dbSNP:rs871990).
FT /FTId=VAR_018383.
FT VARIANT 561 561 N -> S (in dbSNP:rs34914463).
FT /FTId=VAR_052914.
FT MUTAGEN 795 795 T->A: Impaired HIPK2-mediated
FT phosphorylation; when associated with A-
FT 797 and A-983.
FT {ECO:0000269|PubMed:19448668}.
FT MUTAGEN 797 797 T->A: Impaired HIPK2-mediated
FT phosphorylation; when associated with A-
FT 795 and A-983.
FT {ECO:0000269|PubMed:19448668}.
FT MUTAGEN 983 983 T->A: Impaired HIPK2-mediated
FT phosphorylation; when associated with A-
FT 795 and A-797.
FT {ECO:0000269|PubMed:19448668}.
FT CONFLICT 188 188 P -> S (in Ref. 6; AAH43352).
FT {ECO:0000305}.
FT CONFLICT 674 674 R -> C (in Ref. 6; AAH43352).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 765 792 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 339 359 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 337 364 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 365 388 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 234 262 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 726 753 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 337 359 ismart:ZnF_C2H2 [T]
FT MYHIT 726 748 ismart:ZnF_C2H2 [T]
FT MYHIT 30 187 ismart:BTB [T]
FT MYHIT 311 331 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 20 60 ipfam:BTB [T]
FT MYHIT 367 388 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 765 787 ismart:ZnF_C2H2 [T]
FT MYHIT 728 748 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 309 336 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 767 787 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 365 388 ismart:ZnF_C2H2 [T]
FT MYHIT 30 152 iprf:BTB [T]
FT MYHIT 234 254 ismart:ZnF_C2H2 [T]
FT MYHIT 309 331 ismart:ZnF_C2H2 [T]
SQ SEQUENCE 1013 AA; 105114 MW; CA4AB6A5230C2F52 CRC64;
MPPPAEVTDP SHAPAVLRQL NEQRLRGLFC DVTLIAGDTK FPAHRSVLAA SSPFFREALL
TSAPLPLPPA TGGAAPNPAT TTAASSSSSS SSSSSSSSSS ASSSSSSSSS SPPPASPPAS
SPPRVLELPG VPAAAFSDVL NFIYSARLAL PGGGGDGAAV AEIGALGRRL GISRLQGLGE
GGDAWVPPTP APMATSQPEE DSFGPGPRPA GEWEGDRAEA QAPDLQCSLP RRPLPCPQCG
KSFIHPKRLQ THEAQCRRGA STRGSTGLGA GGAGPGGPAG VDASALPPPV GFRGGPEHVV
KVVGGHVLYV CAACERSYVT LSSLKRHSNV HSWRRKYPCR YCEKVFALAE YRTKHEVWHT
GERRYQCIFC WETFVTYYNL KTHQRAFHGI SPGLLASEKT PNGGYKPKLN TLKLYRLLPM
RAAKRPYKTY SQGAPEAPLS PTLNTPAPVA MPASPPPGPP PAPEPGPPPS VITFAHPAPS
VIVHGGSSSG GGGSGTASTG GSQAASVITY TAPPRPPKKR EYPPPPPEPA ATPTSPATAV
SPATAAGPAM ATTTEEAKGR NPRAGRTLTY TAKPVGGIGG GGGPPTGAGR GPSQLQAPPP
LCQITVRIGE EAIVKRRISE TDLRPGELSG EEMEESEEDE EEEDEEEEEE DEEESKAGGE
DQLWRPYYSY KPKRKAGAAG GASVGGSGLP RGRRPPRWRQ KLERRSWEET PAAESPAGRA
RTERRHRCGD CAQTFTTLRK LRKHQEAHGG GSHSSRAGRR PSTRFTCPHC AKVCKTAAAL
SRHGQRHAAE RPGGTPTPVI AYSKGSAGTR PGDVKEEAPQ EMQVSSSSGE AGGGSTAAEE
ASETASLQDP IISGGEEPPV VASGGSYVYP PVQEFPLALI GGGREPGGGR GKSGSEGPVG
AGEGDRMEGI GAAKVTFYPE PYPLVYGPQL LAAYPYNFSN LAALPVALNM VLPDEKGAGA
LPFLPGVFGY AVNPQAAPPA PPTPPPPTLP PPIPPKGEGE RAGVERTQKG DVG
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