T2EB_HUMAN
ID T2EB_HUMAN Reviewed; 291 AA.
AC P29084; D3DSV2; Q9H2B9;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Transcription initiation factor IIE subunit beta;
DE Short=TFIIE-beta;
DE AltName: Full=General transcription factor IIE subunit 2;
GN Name=GTF2E2; Synonyms=TF2E2;
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], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP SUBUNIT.
RX PubMed=1956398; DOI=10.1038/354369a0;
RA Peterson M.G., Inostroza J., Maxon M.E., Flores O., Admon A., Reinberg D.,
RA Tjian R.;
RT "Structure and functional properties of human general transcription factor
RT IIE.";
RL Nature 354:369-373(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=1956404; DOI=10.1038/354401a0;
RA Sumimoto H., Ohkuma Y., Sinn E., Kato H., Shimasaki S., Horikoshi M.,
RA Roeder R.G.;
RT "Conserved sequence motifs in the small subunit of human general
RT transcription factor TFIIE.";
RL Nature 354:401-404(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schertzer M., Wood S.;
RL Submitted (AUG-2000) 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].
RC TISSUE=Skin;
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 INTERACTION WITH SND1, AND SUBCELLULAR LOCATION.
RX PubMed=7651391; DOI=10.1128/mcb.15.9.4735;
RA Tong X., Drapkin R., Yalamanchili R., Mosialos G., Kieff E.;
RT "The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex
RT with a novel cellular coactivator that can interact with TFIIE.";
RL Mol. Cell. Biol. 15:4735-4744(1995).
RN [7]
RP INTERACTION WITH SUPT16H.
RX PubMed=10792464; DOI=10.1046/j.1365-2443.2000.00323.x;
RA Kang S.-W., Kuzuhara T., Horikoshi M.;
RT "Functional interaction of general transcription initiation factor TFIIE
RT with general chromatin factor SPT16/CDC68.";
RL Genes Cells 5:251-263(2000).
RN [8]
RP INTERACTION WITH ATF7IP.
RX PubMed=19106100; DOI=10.1074/jbc.m807098200;
RA Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S.,
RA Watanabe S., Saitoh N., Ito T., Nakao M.;
RT "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated
RT telomerase activity.";
RL J. Biol. Chem. 284:5165-5174(2009).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP 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 [12]
RP INVOLVEMENT IN TTD6, VARIANTS TTD6 PRO-150 AND TYR-187, AND
RP CHARACTERIZATION OF VARIANTS TTD6 PRO-150 AND TYR-187.
RX PubMed=26996949; DOI=10.1016/j.ajhg.2016.02.008;
RA Kuschal C., Botta E., Orioli D., Digiovanna J.J., Seneca S., Keymolen K.,
RA Tamura D., Heller E., Khan S.G., Caligiuri G., Lanzafame M., Nardo T.,
RA Ricotti R., Peverali F.A., Stephens R., Zhao Y., Lehmann A.R.,
RA Baranello L., Levens D., Kraemer K.H., Stefanini M.;
RT "GTF2E2 mutations destabilize the general transcription factor complex
RT TFIIE in individuals with DNA repair-proficient trichothiodystrophy.";
RL Am. J. Hum. Genet. 98:627-642(2016).
CC -!- FUNCTION: Recruits TFIIH to the initiation complex and stimulates the
CC RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase
CC activities of TFIIH. Both TFIIH and TFIIE are required for promoter
CC clearance by RNA polymerase. {ECO:0000269|PubMed:1956398,
CC ECO:0000269|PubMed:1956404}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains (PubMed:1956398).
CC Interacts with FACT subunit SUPT16H (PubMed:10792464). Interacts with
CC ATF7IP (PubMed:19106100). Interacts with SND1 (PubMed:7651391).
CC {ECO:0000269|PubMed:10792464, ECO:0000269|PubMed:19106100,
CC ECO:0000269|PubMed:1956398, ECO:0000269|PubMed:7651391}.
CC -!- INTERACTION:
CC P29084; Q8IYI6: EXOC8; NbExp=5; IntAct=EBI-2853321, EBI-742102;
CC P29084; P29083: GTF2E1; NbExp=6; IntAct=EBI-2853321, EBI-5462215;
CC P29084; Q92993: KAT5; NbExp=3; IntAct=EBI-2853321, EBI-399080;
CC P29084; P23508: MCC; NbExp=2; IntAct=EBI-2853321, EBI-307531;
CC P29084; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2853321, EBI-79165;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7651391}.
CC -!- DISEASE: Trichothiodystrophy 6, non-photosensitive (TTD6) [MIM:616943]:
CC A form of trichothiodystrophy, a disease characterized by sulfur-
CC deficient brittle hair and multisystem variable abnormalities. The
CC spectrum of clinical features varies from mild disease with only hair
CC involvement to severe disease with cutaneous, neurologic and profound
CC developmental defects. Ichthyosis, intellectual and developmental
CC disabilities, decreased fertility, abnormal characteristics at birth,
CC ocular abnormalities, short stature, and infections are common
CC manifestations. There are both photosensitive and non-photosensitive
CC forms of the disorder. TTD6 patients do not manifest cutaneous
CC photosensitivity. Inheritance pattern has been reported to be autosomal
CC recessive. {ECO:0000269|PubMed:26996949}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TFIIE beta subunit family.
CC {ECO:0000255|PROSITE-ProRule:PRU00682}.
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DR EMBL; S67861; AAB20414.1; -; mRNA.
DR EMBL; X63469; CAA45069.1; -; mRNA.
DR EMBL; AF292062; AAG39077.1; -; Genomic_DNA.
DR EMBL; AF292056; AAG39077.1; JOINED; Genomic_DNA.
DR EMBL; AF292057; AAG39077.1; JOINED; Genomic_DNA.
DR EMBL; AF292058; AAG39077.1; JOINED; Genomic_DNA.
DR EMBL; AF292059; AAG39077.1; JOINED; Genomic_DNA.
DR EMBL; AF292060; AAG39077.1; JOINED; Genomic_DNA.
DR EMBL; AF292061; AAG39077.1; JOINED; Genomic_DNA.
DR EMBL; CH471080; EAW63446.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63449.1; -; Genomic_DNA.
DR EMBL; BC030572; AAH30572.1; -; mRNA.
DR CCDS; CCDS6078.1; -.
DR PIR; S29292; S29292.
DR RefSeq; NP_002086.1; NM_002095.5.
DR RefSeq; XP_016868852.1; XM_017013363.1.
DR RefSeq; XP_016868853.1; XM_017013364.1.
DR PDB; 1D8J; NMR; -; A=66-146.
DR PDB; 1D8K; NMR; -; A=66-146.
DR PDB; 5GPY; X-ray; 2.10 A; B=141-244.
DR PDB; 5IY6; EM; 7.20 A; R=1-291.
DR PDB; 5IY7; EM; 8.60 A; R=1-291.
DR PDB; 5IY8; EM; 7.90 A; R=1-291.
DR PDB; 5IY9; EM; 6.30 A; R=1-291.
DR PDB; 5IYA; EM; 5.40 A; R=1-291.
DR PDB; 5IYB; EM; 3.90 A; R=1-291.
DR PDB; 5IYC; EM; 3.90 A; R=1-291.
DR PDB; 5IYD; EM; 3.90 A; R=1-291.
DR PDB; 6O9L; EM; 7.20 A; R=1-291.
DR PDB; 7EG9; EM; 3.70 A; V=1-291.
DR PDB; 7EGA; EM; 4.10 A; V=1-291.
DR PDB; 7EGB; EM; 3.30 A; V=1-291.
DR PDB; 7EGC; EM; 3.90 A; V=1-291.
DR PDB; 7ENA; EM; 4.07 A; EB=1-291.
DR PDB; 7ENC; EM; 4.13 A; EB=1-291.
DR PDB; 7LBM; EM; 4.80 A; R=1-291.
DR PDB; 7NVR; EM; 4.50 A; X=1-291.
DR PDB; 7NVS; EM; 2.80 A; X=1-291.
DR PDB; 7NVT; EM; 2.90 A; X=1-291.
DR PDB; 7NVU; EM; 2.50 A; X=1-291.
DR PDB; 7NVY; EM; 7.30 A; X=1-291.
DR PDB; 7NVZ; EM; 7.20 A; X=1-291.
DR PDB; 7NW0; EM; 6.60 A; X=1-291.
DR PDBsum; 1D8J; -.
DR PDBsum; 1D8K; -.
DR PDBsum; 5GPY; -.
DR PDBsum; 5IY6; -.
DR PDBsum; 5IY7; -.
DR PDBsum; 5IY8; -.
DR PDBsum; 5IY9; -.
DR PDBsum; 5IYA; -.
DR PDBsum; 5IYB; -.
DR PDBsum; 5IYC; -.
DR PDBsum; 5IYD; -.
DR PDBsum; 6O9L; -.
DR PDBsum; 7EG9; -.
DR PDBsum; 7EGA; -.
DR PDBsum; 7EGB; -.
DR PDBsum; 7EGC; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR PDBsum; 7NVS; -.
DR PDBsum; 7NVT; -.
DR PDBsum; 7NVU; -.
DR PDBsum; 7NVY; -.
DR PDBsum; 7NVZ; -.
DR PDBsum; 7NW0; -.
DR AlphaFoldDB; P29084; -.
DR BMRB; P29084; -.
DR SMR; P29084; -.
DR BioGRID; 109216; 163.
DR CORUM; P29084; -.
DR DIP; DIP-716N; -.
DR IntAct; P29084; 92.
DR MINT; P29084; -.
DR STRING; 9606.ENSP00000348168; -.
DR GlyGen; P29084; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P29084; -.
DR MetOSite; P29084; -.
DR PhosphoSitePlus; P29084; -.
DR BioMuta; GTF2E2; -.
DR DMDM; 135232; -.
DR EPD; P29084; -.
DR jPOST; P29084; -.
DR MassIVE; P29084; -.
DR MaxQB; P29084; -.
DR PaxDb; P29084; -.
DR PeptideAtlas; P29084; -.
DR PRIDE; P29084; -.
DR ProteomicsDB; 54518; -.
DR Antibodypedia; 4040; 289 antibodies from 32 providers.
DR DNASU; 2961; -.
DR Ensembl; ENST00000355904.9; ENSP00000348168.4; ENSG00000197265.9.
DR GeneID; 2961; -.
DR KEGG; hsa:2961; -.
DR MANE-Select; ENST00000355904.9; ENSP00000348168.4; NM_002095.6; NP_002086.1.
DR UCSC; uc003xig.4; human.
DR CTD; 2961; -.
DR DisGeNET; 2961; -.
DR GeneCards; GTF2E2; -.
DR HGNC; HGNC:4651; GTF2E2.
DR HPA; ENSG00000197265; Low tissue specificity.
DR MalaCards; GTF2E2; -.
DR MIM; 189964; gene.
DR MIM; 616943; phenotype.
DR neXtProt; NX_P29084; -.
DR OpenTargets; ENSG00000197265; -.
DR Orphanet; 33364; Trichothiodystrophy.
DR PharmGKB; PA29037; -.
DR VEuPathDB; HostDB:ENSG00000197265; -.
DR eggNOG; KOG3095; Eukaryota.
DR GeneTree; ENSGT00390000011749; -.
DR HOGENOM; CLU_086770_0_0_1; -.
DR InParanoid; P29084; -.
DR OMA; NTDHSNG; -.
DR OrthoDB; 1160863at2759; -.
DR PhylomeDB; P29084; -.
DR TreeFam; TF105901; -.
DR PathwayCommons; P29084; -.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR SignaLink; P29084; -.
DR BioGRID-ORCS; 2961; 742 hits in 1093 CRISPR screens.
DR ChiTaRS; GTF2E2; human.
DR EvolutionaryTrace; P29084; -.
DR GeneWiki; GTF2E2; -.
DR GenomeRNAi; 2961; -.
DR Pharos; P29084; Tbio.
DR PRO; PR:P29084; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P29084; protein.
DR Bgee; ENSG00000197265; Expressed in adrenal tissue and 187 other tissues.
DR ExpressionAtlas; P29084; baseline and differential.
DR Genevisible; P29084; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0005673; C:transcription factor TFIIE complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ARUK-UCL.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd07977; TFIIE_beta_winged_helix; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR040501; TFA2_Winged_2.
DR InterPro; IPR016656; TFIIE-bsu.
DR InterPro; IPR003166; TFIIE_bsu_DNA-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12716; PTHR12716; 1.
DR Pfam; PF18121; TFA2_Winged_2; 1.
DR Pfam; PF02186; TFIIE_beta; 1.
DR PIRSF; PIRSF016398; TFIIE-beta; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51351; TFIIE_BETA_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..291
FT /note="Transcription initiation factor IIE subunit beta"
FT /id="PRO_0000211226"
FT DNA_BIND 66..146
FT /note="TFIIE beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00682"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..272
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D902"
FT VARIANT 133
FT /note="I -> T (in dbSNP:rs2229299)"
FT /id="VAR_052281"
FT VARIANT 150
FT /note="A -> P (in TTD6; reduction in the levels of both
FT TFIIE-alpha and TFIIE-beta subunits of the TFIIE complex in
FT patient cells; reduced phosphorylation of TFIIE-alpha
FT observed in patient cells; dbSNP:rs875989846)"
FT /evidence="ECO:0000269|PubMed:26996949"
FT /id="VAR_076893"
FT VARIANT 183
FT /note="K -> R (in dbSNP:rs2978277)"
FT /id="VAR_039003"
FT VARIANT 187
FT /note="D -> Y (in TTD6; reduction in the levels of both
FT TFIIE-alpha and TFIIE-beta subunits of the TFIIE complex in
FT patient cells; reduced phosphorylation of TFIIE-alpha
FT observed in patient cells; dbSNP:rs875989847)"
FT /evidence="ECO:0000269|PubMed:26996949"
FT /id="VAR_076894"
FT CONFLICT 53
FT /note="Q -> E (in Ref. 3; AAG39077)"
FT /evidence="ECO:0000305"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:1D8K"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:7NVU"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:7NVU"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:7NVU"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1D8K"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:7NVU"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:7NVU"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:7NVU"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:7NVU"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:7NVU"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:5GPY"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:5GPY"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:5GPY"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:5GPY"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:5GPY"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:5GPY"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:5GPY"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:5GPY"
SQ SEQUENCE 291 AA; 33044 MW; 20F6BDFF2E06E5E7 CRC64;
MDPSLLRERE LFKKRALSTP VVEKRSASSE SSSSSSKKKK TKVEHGGSSG SKQNSDHSNG
SFNLKALSGS SGYKFGVLAK IVNYMKTRHQ RGDTHPLTLD EILDETQHLD IGLKQKQWLM
TEALVNNPKI EVIDGKYAFK PKYNVRDKKA LLRLLDQHDQ RGLGGILLED IEEALPNSQK
AVKALGDQIL FVNRPDKKKI LFFNDKSCQF SVDEEFQKLW RSVTVDSMDE EKIEEYLKRQ
GISSMQESGP KKVAPIQRRK KPASQKKRRF KTHNEHLAGV LKDYSDITSS K
