PRD14_HUMAN
ID PRD14_HUMAN Reviewed; 571 AA.
AC Q9GZV8; Q86UX9;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=PR domain zinc finger protein 14;
DE EC=2.1.1.-;
DE AltName: Full=PR domain-containing protein 14;
GN Name=PRDM14;
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].
RA Yang X.-H., Huang S.;
RT "A family of novel PR-domain (PRDM) genes as candidate tumor suppressors.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-244.
RC TISSUE=Ovary;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17942894; DOI=10.1158/0008-5472.can-06-4111;
RA Nishikawa N., Toyota M., Suzuki H., Honma T., Fujikane T., Ohmura T.,
RA Nishidate T., Ohe-Toyota M., Maruyama R., Sonoda T., Sasaki Y., Urano T.,
RA Imai K., Hirata K., Tokino T.;
RT "Gene amplification and overexpression of PRDM14 in breast cancers.";
RL Cancer Res. 67:9649-9657(2007).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20953172; DOI=10.1038/nature09531;
RA Chia N.Y., Chan Y.S., Feng B., Lu X., Orlov Y.L., Moreau D., Kumar P.,
RA Yang L., Jiang J., Lau M.S., Huss M., Soh B.S., Kraus P., Li P., Lufkin T.,
RA Lim B., Clarke N.D., Bard F., Ng H.H.;
RT "A genome-wide RNAi screen reveals determinants of human embryonic stem
RT cell identity.";
RL Nature 468:316-320(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP INTERACTION WITH CBFA2T2.
RX PubMed=27281218; DOI=10.1038/nature18004;
RA Tu S., Narendra V., Yamaji M., Vidal S.E., Rojas L.A., Wang X., Kim S.Y.,
RA Garcia B.A., Tuschl T., Stadtfeld M., Reinberg D.;
RT "Co-repressor CBFA2T2 regulates pluripotency and germline development.";
RL Nature 534:387-390(2016).
CC -!- FUNCTION: Transcription factor that has both positive and negative
CC roles on transcription. Required for the maintenance of embryonic stem
CC cell identity and the reacquisition of pluripotency in somatic cells.
CC May play an essential role in germ cell development at 2 levels: the
CC reacquisition of potential pluripotency, including SOX2 up-regulation,
CC and successful epigenetic reprogramming, characterized by EHMT1
CC repression. Its association with CBFA2T2 is required for the functions
CC in pluripotency and germ cell formation (By similarity). Directly up-
CC regulates the expression of pluripotency gene POU5F1 through its
CC proximal enhancer. Binds to the DNA consensus sequence 5'-GGTC[TC]CTAA-
CC 3'. {ECO:0000250|UniProtKB:E9Q3T6, ECO:0000269|PubMed:17942894,
CC ECO:0000269|PubMed:20953172}.
CC -!- SUBUNIT: Interacts with CBFA2T2. {ECO:0000269|PubMed:27281218}.
CC -!- INTERACTION:
CC Q9GZV8; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-3957793, EBI-11096309;
CC Q9GZV8; Q99996-2: AKAP9; NbExp=3; IntAct=EBI-3957793, EBI-9641546;
CC Q9GZV8; P29972: AQP1; NbExp=3; IntAct=EBI-3957793, EBI-745213;
CC Q9GZV8; Q8N5M1: ATPAF2; NbExp=10; IntAct=EBI-3957793, EBI-1166928;
CC Q9GZV8; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-3957793, EBI-742750;
CC Q9GZV8; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-3957793, EBI-745073;
CC Q9GZV8; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-3957793, EBI-3866279;
CC Q9GZV8; O43439: CBFA2T2; NbExp=12; IntAct=EBI-3957793, EBI-748628;
CC Q9GZV8; O43439-4: CBFA2T2; NbExp=6; IntAct=EBI-3957793, EBI-11954144;
CC Q9GZV8; Q96GN5: CDCA7L; NbExp=6; IntAct=EBI-3957793, EBI-5278764;
CC Q9GZV8; Q02930-3: CREB5; NbExp=3; IntAct=EBI-3957793, EBI-10192698;
CC Q9GZV8; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-3957793, EBI-9679045;
CC Q9GZV8; O60573: EIF4E2; NbExp=3; IntAct=EBI-3957793, EBI-398610;
CC Q9GZV8; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-3957793, EBI-744099;
CC Q9GZV8; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-3957793, EBI-1384254;
CC Q9GZV8; O95995: GAS8; NbExp=3; IntAct=EBI-3957793, EBI-1052570;
CC Q9GZV8; P55040: GEM; NbExp=3; IntAct=EBI-3957793, EBI-744104;
CC Q9GZV8; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-3957793, EBI-748515;
CC Q9GZV8; Q9NWQ4: GPATCH2L; NbExp=3; IntAct=EBI-3957793, EBI-5666657;
CC Q9GZV8; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-3957793, EBI-11959863;
CC Q9GZV8; Q96MH2: HEXIM2; NbExp=4; IntAct=EBI-3957793, EBI-5460660;
CC Q9GZV8; P09067: HOXB5; NbExp=3; IntAct=EBI-3957793, EBI-3893317;
CC Q9GZV8; P31273: HOXC8; NbExp=3; IntAct=EBI-3957793, EBI-1752118;
CC Q9GZV8; Q9UBY9: HSPB7; NbExp=3; IntAct=EBI-3957793, EBI-739361;
CC Q9GZV8; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-3957793, EBI-2556193;
CC Q9GZV8; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-3957793, EBI-739832;
CC Q9GZV8; Q5JRA6-2: MIA3; NbExp=3; IntAct=EBI-3957793, EBI-10244342;
CC Q9GZV8; Q9BYC8: MRPL32; NbExp=3; IntAct=EBI-3957793, EBI-7825220;
CC Q9GZV8; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-3957793, EBI-2858213;
CC Q9GZV8; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-3957793, EBI-11022007;
CC Q9GZV8; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-3957793, EBI-12000762;
CC Q9GZV8; O43741: PRKAB2; NbExp=4; IntAct=EBI-3957793, EBI-1053424;
CC Q9GZV8; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-3957793, EBI-1567797;
CC Q9GZV8; P25786: PSMA1; NbExp=3; IntAct=EBI-3957793, EBI-359352;
CC Q9GZV8; O75771: RAD51D; NbExp=3; IntAct=EBI-3957793, EBI-1055693;
CC Q9GZV8; P98175: RBM10; NbExp=6; IntAct=EBI-3957793, EBI-721525;
CC Q9GZV8; Q9P2K3: RCOR3; NbExp=3; IntAct=EBI-3957793, EBI-743428;
CC Q9GZV8; Q06455-2: RUNX1T1; NbExp=6; IntAct=EBI-3957793, EBI-11984663;
CC Q9GZV8; Q06455-4: RUNX1T1; NbExp=3; IntAct=EBI-3957793, EBI-10224192;
CC Q9GZV8; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-3957793, EBI-6257312;
CC Q9GZV8; Q9BWG6: SCNM1; NbExp=5; IntAct=EBI-3957793, EBI-748391;
CC Q9GZV8; P09234: SNRPC; NbExp=3; IntAct=EBI-3957793, EBI-766589;
CC Q9GZV8; Q9Y4C2-2: TCAF1; NbExp=3; IntAct=EBI-3957793, EBI-11974855;
CC Q9GZV8; Q15561: TEAD4; NbExp=3; IntAct=EBI-3957793, EBI-747736;
CC Q9GZV8; Q8WW24: TEKT4; NbExp=6; IntAct=EBI-3957793, EBI-750487;
CC Q9GZV8; Q08117-2: TLE5; NbExp=5; IntAct=EBI-3957793, EBI-11741437;
CC Q9GZV8; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-3957793, EBI-725997;
CC Q9GZV8; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-3957793, EBI-744794;
CC Q9GZV8; Q5I0X7: TTC32; NbExp=3; IntAct=EBI-3957793, EBI-8636434;
CC Q9GZV8; P42681: TXK; NbExp=3; IntAct=EBI-3957793, EBI-7877438;
CC Q9GZV8; O75604: USP2; NbExp=3; IntAct=EBI-3957793, EBI-743272;
CC Q9GZV8; Q64LD2-2: WDR25; NbExp=3; IntAct=EBI-3957793, EBI-12032042;
CC Q9GZV8; P15622-3: ZNF250; NbExp=3; IntAct=EBI-3957793, EBI-10177272;
CC Q9GZV8; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-3957793, EBI-6427977;
CC Q9GZV8; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-3957793, EBI-5667516;
CC Q9GZV8; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-3957793, EBI-3957603;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17942894}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic stem cells. Tends to be
CC overexpressed in breast cancer (at protein level).
CC {ECO:0000269|PubMed:17942894, ECO:0000269|PubMed:20953172}.
CC -!- DOMAIN: The first 5 zinc fingers, but not the last one, are required
CC for DNA-binding and transcriptional activity.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AF319458; AAG39635.1; -; mRNA.
DR EMBL; AK022595; BAB14120.1; -; mRNA.
DR EMBL; BC052311; AAH52311.1; -; mRNA.
DR CCDS; CCDS6206.1; -.
DR RefSeq; NP_078780.1; NM_024504.3.
DR AlphaFoldDB; Q9GZV8; -.
DR SMR; Q9GZV8; -.
DR BioGRID; 122025; 80.
DR DIP; DIP-58143N; -.
DR IntAct; Q9GZV8; 81.
DR MINT; Q9GZV8; -.
DR STRING; 9606.ENSP00000276594; -.
DR iPTMnet; Q9GZV8; -.
DR PhosphoSitePlus; Q9GZV8; -.
DR BioMuta; PRDM14; -.
DR DMDM; 17368925; -.
DR EPD; Q9GZV8; -.
DR jPOST; Q9GZV8; -.
DR MassIVE; Q9GZV8; -.
DR PaxDb; Q9GZV8; -.
DR PeptideAtlas; Q9GZV8; -.
DR PRIDE; Q9GZV8; -.
DR ProteomicsDB; 80159; -.
DR Antibodypedia; 12206; 425 antibodies from 34 providers.
DR DNASU; 63978; -.
DR Ensembl; ENST00000276594.3; ENSP00000276594.2; ENSG00000147596.4.
DR GeneID; 63978; -.
DR KEGG; hsa:63978; -.
DR MANE-Select; ENST00000276594.3; ENSP00000276594.2; NM_024504.4; NP_078780.1.
DR UCSC; uc003xym.3; human.
DR CTD; 63978; -.
DR DisGeNET; 63978; -.
DR GeneCards; PRDM14; -.
DR HGNC; HGNC:14001; PRDM14.
DR HPA; ENSG00000147596; Not detected.
DR MIM; 611781; gene.
DR neXtProt; NX_Q9GZV8; -.
DR OpenTargets; ENSG00000147596; -.
DR PharmGKB; PA33712; -.
DR VEuPathDB; HostDB:ENSG00000147596; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159454; -.
DR HOGENOM; CLU_034551_1_0_1; -.
DR InParanoid; Q9GZV8; -.
DR OMA; WYPIPHL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9GZV8; -.
DR TreeFam; TF106412; -.
DR PathwayCommons; Q9GZV8; -.
DR Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
DR SignaLink; Q9GZV8; -.
DR SIGNOR; Q9GZV8; -.
DR BioGRID-ORCS; 63978; 14 hits in 1091 CRISPR screens.
DR GenomeRNAi; 63978; -.
DR Pharos; Q9GZV8; Tbio.
DR PRO; PR:Q9GZV8; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9GZV8; protein.
DR Bgee; ENSG00000147596; Expressed in buccal mucosa cell and 13 other tissues.
DR ExpressionAtlas; Q9GZV8; baseline and differential.
DR Genevisible; Q9GZV8; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0034972; P:histone H3-R26 methylation; IBA:GO_Central.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR GO; GO:0060817; P:inactivation of paternal X chromosome; IEA:Ensembl.
DR GO; GO:0001827; P:inner cell mass cell fate commitment; IEA:Ensembl.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1902093; P:positive regulation of flagellated sperm motility; IEA:Ensembl.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd19198; PR-SET_PRDM14; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044408; PRDM14_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..571
FT /note="PR domain zinc finger protein 14"
FT /id="PRO_0000047771"
FT DOMAIN 251..367
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 400..424
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..455
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 461..483
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 489..511
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 517..540
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 546..568
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 129..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..384
FT /note="Interaction with CBFA2T2"
FT /evidence="ECO:0000250|UniProtKB:E9Q3T6"
FT COMPBIAS 168..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VARIANT 244
FT /note="K -> E (in dbSNP:rs3750228)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_021895"
SQ SEQUENCE 571 AA; 64062 MW; 60D5ACC96DADE500 CRC64;
MALPRPSEAV PQDKVCYPPE SSPQNLAAYY TPFPSYGHYR NSLATVEEDF QPFRQLEAAA
SAAPAMPPFP FRMAPPLLSP GLGLQREPLY DLPWYSKLPP WYPIPHVPRE VPPFLSSSHE
YAGASSEDLG HQIIGGDNES GPCCGPDTLI PPPPADASLL PEGLRTSQLL PCSPSKQSED
GPKPSNQEGK SPARFQFTEE DLHFVLYGVT PSLEHPASLH HAISGLLVPP DSSGSDSLPQ
TLDKDSLQLP EGLCLMQTVF GEVPHFGVFC SSFIAKGVRF GPFQGKVVNA SEVKTYGDNS
VMWEIFEDGH LSHFIDGKGG TGNWMSYVNC ARFPKEQNLV AVQCQGHIFY ESCKEIHQNQ
ELLVWYGDCY EKFLDIPVSL QVTEPGKQPS GPSEESAEGY RCERCGKVFT YKYYRDKHLK
YTPCVDKGDR KFPCSLCKRS FEKRDRLRIH ILHVHEKHRP HKCSTCGKCF SQSSSLNKHM
RVHSGDRPYQ CVYCTKRFTA SSILRTHIRQ HSGEKPFKCK YCGKSFASHA AHDSHVRRSH
KEDDGCSCSI CGKIFSDQET FYSHMKFHED Y
