TF3C2_HUMAN
ID TF3C2_HUMAN Reviewed; 911 AA.
AC Q8WUA4; D6W557; Q16632; Q9BWI7;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=General transcription factor 3C polypeptide 2;
DE AltName: Full=TF3C-beta;
DE AltName: Full=Transcription factor IIIC 110 kDa subunit;
DE Short=TFIIIC 110 kDa subunit;
DE Short=TFIIIC110;
DE AltName: Full=Transcription factor IIIC subunit beta;
GN Name=GTF3C2; Synonyms=KIAA0011;
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), PROTEIN SEQUENCE OF 41-62; 338-354;
RP 642-654 AND 757-774, AND IDENTIFICATION OF SUBUNITS OF TFIIIC2 COMPLEX.
RX PubMed=7729686; DOI=10.1101/gad.9.6.675;
RA Sinn E., Wang Z., Kovelman R., Roeder R.G.;
RT "Cloning and characterization of a TFIIIC2 subunit (TFIIIC beta) whose
RT presence correlates with activation of RNA polymerase III-mediated
RT transcription by adenovirus E1A expression and serum factors.";
RL Genes Dev. 9:675-685(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Colon;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 620-911.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
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., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-167, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND THR-895, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-167; SER-871;
RP SER-892 AND SER-893, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-220 AND SER-892, AND
RP IDENTIFICATION 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., 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-167; SER-597;
RP SER-871; THR-895 AND SER-901, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-260 AND SER-901, AND
RP IDENTIFICATION BY 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 [16]
RP IDENTIFICATION BY 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., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA 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: Required for RNA polymerase III-mediated transcription.
CC Component of TFIIIC that initiates transcription complex assembly on
CC tRNA and is required for transcription of 5S rRNA and other stable
CC nuclear and cytoplasmic RNAs. May play a direct role in stabilizing
CC interactions of TFIIIC2 with TFIIIC1.
CC -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6.
CC -!- INTERACTION:
CC Q8WUA4; P42345: MTOR; NbExp=3; IntAct=EBI-1237062, EBI-359260;
CC Q8WUA4; Q8N122: RPTOR; NbExp=3; IntAct=EBI-1237062, EBI-1567928;
CC Q8WUA4-2; Q08AM6: VAC14; NbExp=3; IntAct=EBI-11957962, EBI-2107455;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WUA4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WUA4-2; Sequence=VSP_010566, VSP_010567;
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DR EMBL; D13636; BAA02800.1; -; mRNA.
DR EMBL; BT009799; AAP88801.1; -; mRNA.
DR EMBL; CH471053; EAX00595.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00596.1; -; Genomic_DNA.
DR EMBL; BC000212; AAH00212.1; -; mRNA.
DR EMBL; BC020981; AAH20981.1; -; mRNA.
DR EMBL; AF054988; AAC09349.1; -; mRNA.
DR CCDS; CCDS1749.1; -. [Q8WUA4-1]
DR PIR; A56465; A56465.
DR RefSeq; NP_001030598.1; NM_001035521.2. [Q8WUA4-1]
DR RefSeq; NP_001305838.1; NM_001318909.1. [Q8WUA4-1]
DR RefSeq; NP_001512.1; NM_001521.3. [Q8WUA4-1]
DR AlphaFoldDB; Q8WUA4; -.
DR BioGRID; 109231; 168.
DR CORUM; Q8WUA4; -.
DR DIP; DIP-38213N; -.
DR IntAct; Q8WUA4; 69.
DR MINT; Q8WUA4; -.
DR STRING; 9606.ENSP00000352536; -.
DR GlyGen; Q8WUA4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WUA4; -.
DR MetOSite; Q8WUA4; -.
DR PhosphoSitePlus; Q8WUA4; -.
DR SwissPalm; Q8WUA4; -.
DR BioMuta; GTF3C2; -.
DR DMDM; 48428661; -.
DR EPD; Q8WUA4; -.
DR jPOST; Q8WUA4; -.
DR MassIVE; Q8WUA4; -.
DR MaxQB; Q8WUA4; -.
DR PaxDb; Q8WUA4; -.
DR PeptideAtlas; Q8WUA4; -.
DR PRIDE; Q8WUA4; -.
DR ProteomicsDB; 74647; -. [Q8WUA4-1]
DR ProteomicsDB; 74648; -. [Q8WUA4-2]
DR Antibodypedia; 13626; 208 antibodies from 28 providers.
DR DNASU; 2976; -.
DR Ensembl; ENST00000264720.7; ENSP00000264720.3; ENSG00000115207.14. [Q8WUA4-1]
DR Ensembl; ENST00000359541.6; ENSP00000352536.2; ENSG00000115207.14. [Q8WUA4-1]
DR GeneID; 2976; -.
DR KEGG; hsa:2976; -.
DR MANE-Select; ENST00000264720.8; ENSP00000264720.3; NM_001035521.3; NP_001030598.1.
DR UCSC; uc002rju.3; human. [Q8WUA4-1]
DR CTD; 2976; -.
DR DisGeNET; 2976; -.
DR GeneCards; GTF3C2; -.
DR HGNC; HGNC:4665; GTF3C2.
DR HPA; ENSG00000115207; Low tissue specificity.
DR MIM; 604883; gene.
DR neXtProt; NX_Q8WUA4; -.
DR OpenTargets; ENSG00000115207; -.
DR PharmGKB; PA29053; -.
DR VEuPathDB; HostDB:ENSG00000115207; -.
DR eggNOG; ENOG502RAA6; Eukaryota.
DR GeneTree; ENSGT00390000018632; -.
DR HOGENOM; CLU_014720_0_0_1; -.
DR InParanoid; Q8WUA4; -.
DR OMA; DKGFIWQ; -.
DR OrthoDB; 885702at2759; -.
DR PhylomeDB; Q8WUA4; -.
DR TreeFam; TF314779; -.
DR PathwayCommons; Q8WUA4; -.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR SignaLink; Q8WUA4; -.
DR SIGNOR; Q8WUA4; -.
DR BioGRID-ORCS; 2976; 609 hits in 1087 CRISPR screens.
DR ChiTaRS; GTF3C2; human.
DR GeneWiki; GTF3C2; -.
DR GenomeRNAi; 2976; -.
DR Pharos; Q8WUA4; Tdark.
DR PRO; PR:Q8WUA4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WUA4; protein.
DR Bgee; ENSG00000115207; Expressed in lower esophagus mucosa and 101 other tissues.
DR ExpressionAtlas; Q8WUA4; baseline and differential.
DR Genevisible; Q8WUA4; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:HGNC-UCL.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IDA:GO_Central.
DR GO; GO:0042791; P:5S class rRNA transcription by RNA polymerase III; IC:HGNC-UCL.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:HGNC-UCL.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IC:HGNC-UCL.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; WD repeat.
FT CHAIN 1..911
FT /note="General transcription factor 3C polypeptide 2"
FT /id="PRO_0000050985"
FT REPEAT 366..426
FT /note="WD 1"
FT REPEAT 427..483
FT /note="WD 2"
FT REPEAT 484..535
FT /note="WD 3"
FT REPEAT 536..603
FT /note="WD 4"
FT REPEAT 604..654
FT /note="WD 5"
FT REPEAT 655..690
FT /note="WD 6"
FT REGION 24..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..110
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 895
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 579..585
FT /note="MVVFWNL -> KKNQNKT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010566"
FT VAR_SEQ 586..911
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010567"
FT CONFLICT 301
FT /note="N -> D (in Ref. 3; AAP88801 and 4; AAH20981)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 911 AA; 100680 MW; B59D91DE74555192 CRC64;
MDTCGVGYVA LGEAGPVGNM TVVDSPGQEV LNQLDVKTSS EMTSAEASVE MSLPTPLPGF
EDSPDQRRLP PEQESLSRLE QPDLSSEMSK VSKPRASKPG RKRGGRTRKG PKRPQQPNPP
SAPLVPGLLD QSNPLSTPMP KKRGRKSKAE LLLLKLSKDL DRPESQSPKR PPEDFETPSG
ERPRRRAAQV ALLYLQELAE ELSTALPAPV SCPEGPKVSS PTKPKKIRQP AACPGGEEVD
GAPRDEDFFL QVEAEDVEES EGPSESSSEP EPVVPRSTPR GSTSGKQKPH CRGMAPNGLP
NHIMAPVWKC LHLTKDFREQ KHSYWEFAEW IPLAWKWHLL SELEAAPYLP QEEKSPLFSV
QREGLPEDGT LYRINRFSSI TAHPERWDVS FFTGGPLWAL DWCPVPEGAG ASQYVALFSS
PDMNETHPLS QLHSGPGLLQ LWGLGTLQQE SCPGNRAHFV YGIACDNGCI WDLKFCPSGA
WELPGTPRKA PLLPRLGLLA LACSDGKVLL FSLPHPEALL AQQPPDAVKP AIYKVQCVAT
LQVGSMQATD PSECGQCLSL AWMPTRPHQH LAAGYYNGMV VFWNLPTNSP LQRIRLSDGS
LKLYPFQCFL AHDQAVRTLQ WCKANSHFLV SAGSDRKIKF WDLRRPYEPI NSIKRFLSTE
LAWLLPYNGV TVAQDNCYAS YGLCGIHYID AGYLGFKAYF TAPRKGTVWS LSGSDWLGTI
AAGDISGELI AAILPDMALN PINVKRPVER RFPIYKADLI PYQDSPEGPD HSSASSGVPN
PPKARTYTET VNHHYLLFQD TDLGSFHDLL RREPMLRMQE GEGHSQLCLD RLQLEAIHKV
RFSPNLDSYG WLVSGGQSGL VRIHFVRGLA SPLGHRMQLE SRAHFNAMFQ PSSPTRRPGF
SPTSHRLLPT P
