ID ZN574_HUMAN Reviewed; 896 AA.
AC Q6ZN55; Q6IPE0; Q6ZN10; Q7L5Z5; Q8NCE3; Q9H6N0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 10-MAY-2017, entry version 118.
DE RecName: Full=Zinc finger protein 574;
GN Name=ZNF574;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Cerebellum, Hepatoma, and Teratocarcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; THR-724 AND
RP SER-728, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; SER-298; SER-717
RP AND SER-728, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717 AND SER-728, AND
RP IDENTIFICATION 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-164, AND
RP IDENTIFICATION BY 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 [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-832, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.O113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
RA Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA Vemulapalli V., Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZN55-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZN55-2; Sequence=VSP_022878;
CC Note=No experimental confirmation available.;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK025712; BAB15225.1; -; mRNA.
DR EMBL; AK074788; BAC11210.1; -; mRNA.
DR EMBL; AK131369; BAD18520.1; -; mRNA.
DR EMBL; AK131418; BAD18565.1; -; mRNA.
DR EMBL; BC001184; AAH01184.2; -; mRNA.
DR EMBL; BC071962; AAH71962.1; -; mRNA.
DR CCDS; CCDS12596.1; -. [Q6ZN55-1]
DR RefSeq; NP_001317448.1; NM_001330519.1.
DR RefSeq; NP_073589.4; NM_022752.5. [Q6ZN55-1]
DR RefSeq; XP_005259216.1; XM_005259159.2. [Q6ZN55-1]
DR RefSeq; XP_011525530.1; XM_011527228.2. [Q6ZN55-1]
DR RefSeq; XP_011525531.1; XM_011527229.2. [Q6ZN55-1]
DR RefSeq; XP_011525532.1; XM_011527230.2. [Q6ZN55-1]
DR UniGene; Hs.13323; -.
DR ProteinModelPortal; Q6ZN55; -.
DR SMR; Q6ZN55; -.
DR BioGrid; 122276; 36.
DR IntAct; Q6ZN55; 3.
DR STRING; 9606.ENSP00000351939; -.
DR iPTMnet; Q6ZN55; -.
DR PhosphoSitePlus; Q6ZN55; -.
DR BioMuta; ZNF574; -.
DR DMDM; 125991263; -.
DR EPD; Q6ZN55; -.
DR MaxQB; Q6ZN55; -.
DR PaxDb; Q6ZN55; -.
DR PeptideAtlas; Q6ZN55; -.
DR PRIDE; Q6ZN55; -.
DR Ensembl; ENST00000359044; ENSP00000351939; ENSG00000105732. [Q6ZN55-1]
DR Ensembl; ENST00000600245; ENSP00000469029; ENSG00000105732. [Q6ZN55-1]
DR GeneID; 64763; -.
DR KEGG; hsa:64763; -.
DR UCSC; uc002osk.6; human. [Q6ZN55-1]
DR CTD; 64763; -.
DR GeneCards; ZNF574; -.
DR HGNC; HGNC:26166; ZNF574.
DR HPA; HPA023196; -.
DR HPA; HPA057274; -.
DR neXtProt; NX_Q6ZN55; -.
DR OpenTargets; ENSG00000105732; -.
DR PharmGKB; PA134916492; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; COG5048; LUCA.
DR GeneTree; ENSGT00670000098063; -.
DR HOGENOM; HOG000065747; -.
DR HOVERGEN; HBG103121; -.
DR InParanoid; Q6ZN55; -.
DR PhylomeDB; Q6ZN55; -.
DR TreeFam; TF350791; -.
DR ChiTaRS; ZNF574; human.
DR GenomeRNAi; 64763; -.
DR PRO; PR:Q6ZN55; -.
DR Proteomes; UP000005640; Chromosome 19.
DR Bgee; ENSG00000105732; -.
DR CleanEx; HS_ZNF574; -.
DR ExpressionAtlas; Q6ZN55; baseline and differential.
DR Genevisible; Q6ZN55; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00355; ZnF_C2H2; 20.
DR SUPFAM; SSF57667; SSF57667; 13.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 18.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; DNA-binding; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1 896 Zinc finger protein 574.
FT /FTId=PRO_0000274861.
FT ZN_FING 16 38 C2H2-type 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 76 98 C2H2-type 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 126 148 C2H2-type 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 214 236 C2H2-type 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 309 331 C2H2-type 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 336 358 C2H2-type 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 364 386 C2H2-type 7. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 392 413 C2H2-type 8. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 466 489 C2H2-type 9. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 495 517 C2H2-type 10; degenerate.
FT {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT ZN_FING 523 545 C2H2-type 11. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 551 573 C2H2-type 12. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 579 601 C2H2-type 13. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 607 630 C2H2-type 14. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 636 659 C2H2-type 15; degenerate.
FT {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT ZN_FING 667 689 C2H2-type 16. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 738 760 C2H2-type 17. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 766 788 C2H2-type 18. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 794 816 C2H2-type 19. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 822 844 C2H2-type 20. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT COMPBIAS 419 451 Pro-rich.
FT COMPBIAS 657 733 Ala-rich.
FT MOD_RES 113 113 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 164 164 Phosphoserine.
FT {ECO:0000244|PubMed:16964243,
FT ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 298 298 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:21406692}.
FT MOD_RES 717 717 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:20068231}.
FT MOD_RES 724 724 Phosphothreonine.
FT {ECO:0000244|PubMed:16964243}.
FT MOD_RES 728 728 Phosphoserine.
FT {ECO:0000244|PubMed:16964243,
FT ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:20068231}.
FT MOD_RES 832 832 Asymmetric dimethylarginine.
FT {ECO:0000244|PubMed:24129315}.
FT VAR_SEQ 1 1 M -> MPRATWANSKERSWAESERGPRDTGNGGSKAERHIQ
FT EIETGRGGDRAKAHRRQRMRLRGTERASLGPGRRLGDSRGT
FT DMPGARAQGLAAA (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_022878.
FT VARIANT 332 332 R -> Q (in dbSNP:rs3745226).
FT /FTId=VAR_030351.
FT VARIANT 711 711 T -> S (in dbSNP:rs35898322).
FT /FTId=VAR_052870.
FT VARIANT 785 785 R -> Q (in dbSNP:rs3745228).
FT /FTId=VAR_030352.
FT CONFLICT 513 513 H -> R (in Ref. 1; BAD18565).
FT {ECO:0000305}.
FT CONFLICT 811 811 E -> G (in Ref. 1; BAC11210).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 636 664 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 466 494 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 126 153 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 581 601 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 794 821 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 740 760 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 364 387 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 392 413 ismart:ZnF_C2H2 [T]
FT MYHIT 364 386 ismart:ZnF_C2H2 [T]
FT MYHIT 16 38 ismart:ZnF_C2H2 [T]
FT MYHIT 738 765 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 579 601 ismart:ZnF_C2H2 [T]
FT MYHIT 636 656 ismart:ZnF_C2H2 [T]
FT MYHIT 822 849 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 309 331 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 523 545 ismart:ZnF_C2H2 [T]
FT MYHIT 553 573 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 309 331 ismart:ZnF_C2H2 [T]
FT MYHIT 525 545 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 497 517 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 76 98 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 523 550 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 78 98 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 794 816 ismart:ZnF_C2H2 [T]
FT MYHIT 18 38 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 796 816 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 214 236 ismart:ZnF_C2H2 [T]
FT MYHIT 766 788 ismart:ZnF_C2H2 [T]
FT MYHIT 366 386 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 336 363 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 579 606 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 76 98 ismart:ZnF_C2H2 [T]
FT MYHIT 495 517 ismart:ZnF_C2H2 [T]
FT MYHIT 16 43 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 824 844 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 667 689 ismart:ZnF_C2H2 [T]
FT MYHIT 768 788 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 738 760 ismart:ZnF_C2H2 [T]
FT MYHIT 128 148 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 495 522 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 468 489 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 607 635 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 551 573 ismart:ZnF_C2H2 [T]
FT MYHIT 216 236 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 607 630 ismart:ZnF_C2H2 [T]
FT MYHIT 766 793 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 822 844 ismart:ZnF_C2H2 [T]
FT MYHIT 336 358 ismart:ZnF_C2H2 [T]
FT MYHIT 126 148 ismart:ZnF_C2H2 [T]
FT MYHIT 669 689 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 667 694 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 551 578 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 609 630 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 338 358 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 214 236 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 466 489 ismart:ZnF_C2H2 [T]
FT MYHIT 311 331 ipat:ZINC_FINGER_C2H2_1 [T]
SQ SEQUENCE 896 AA; 98900 MW; F1E3EBCC47427654 CRC64;
MTEESEETVL YIEHRYVCSE CNQLYGSLEE VLMHQNSHVP QQHFELVGVA DPGVTVATDT
ASGTGLYQTL VQESQYQCLE CGQLLMSPSQ LLEHQELHLK MMAPQEAVPA EPSPKAPPLS
SSTIHYECVD CKALFASQEL WLNHRQTHLR ATPTKAPAPV VLGSPVVLGP PVGQARVAVE
HSYRKAEEGG EGATVPSAAA TTTEVVTEVE LLLYKCSECS QLFQLPADFL EHQATHFPAP
VPESQEPALQ QEVQASSPAE VPVSQPDPLP ASDHSYELRN GEAIGRDRRG RRARRNNSGE
AGGAATQELF CSACDQLFLS PHQLQQHLRS HREGVFKCPL CSRVFPSPSS LDQHLGDHSS
ESHFLCVDCG LAFGTEALLL AHRRAHTPNP LHSCPCGKTF VNLTKFLYHR RTHGVGGVPL
PTTPVPPEEP VIGFPEPAPA ETGEPEAPEP PVSEETSAGP AAPGTYRCLL CSREFGKALQ
LTRHQRFVHR LERRHKCSIC GKMFKKKSHV RNHLRTHTGE RPFPCPDCSK PFNSPANLAR
HRLTHTGERP YRCGDCGKAF TQSSTLRQHR LVHAQHFPYR CQECGVRFHR PYRLLMHRYH
HTGEYPYKCR ECPRSFLLRR LLEVHQLVVH AGRQPHRCPS CGAAFPSSLR LREHRCAAAA
AQAPRRFECG TCGKKVGSAA RLQAHEAAHA AAGPGEVLAK EPPAPRAPRA TRAPVASPAA
LGSTATASPA APARRRGLEC SECKKLFSTE TSLQVHRRIH TGERPYPCPD CGKAFRQSTH
LKDHRRLHTG ERPFACEVCG KAFAISMRLA EHRRIHTGER PYSCPDCGKS YRSFSNLWKH
RKTHQQQHQA AVRQQLAEAE AAVGLAVMET AVEALPLVEA IEIYPLAEAE GVQISG
//
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