TAF13_HUMAN
ID TAF13_HUMAN Reviewed; 124 AA.
AC Q15543; B2R5E5; Q5TYV6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Transcription initiation factor TFIID subunit 13 {ECO:0000305};
DE AltName: Full=Transcription initiation factor TFIID 18 kDa subunit {ECO:0000303|PubMed:7729427};
DE Short=TAF(II)18 {ECO:0000303|PubMed:9695952};
DE Short=TAFII-18 {ECO:0000305};
DE Short=TAFII18 {ECO:0000303|PubMed:7729427};
GN Name=TAF13 {ECO:0000312|HGNC:HGNC:11546};
GN Synonyms=TAF2K {ECO:0000312|HGNC:HGNC:11546},
GN TAFII18 {ECO:0000303|PubMed:7729427};
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].
RX PubMed=7729427; DOI=10.1002/j.1460-2075.1995.tb07138.x;
RA Mengus G., May M., Jacq X., Staub A., Tora L., Chambon P., Davidson I.;
RT "Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three
RT subunits of the human transcription factor TFIID.";
RL EMBO J. 14:1520-1531(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Substantia nigra;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 INVOLVEMENT IN MRT60, VARIANTS MRT60 HIS-31 AND LYS-40, AND
RP CHARACTERIZATION OF VARIANTS MRT60 HIS-31 AND LYS-40.
RX PubMed=28257693; DOI=10.1016/j.ajhg.2017.01.032;
RA Tawamie H., Martianov I., Wohlfahrt N., Buchert R., Mengus G., Uebe S.,
RA Janiri L., Hirsch F.W., Schumacher J., Ferrazzi F., Sticht H., Reis A.,
RA Davidson I., Colombo R., Abou Jamra R.;
RT "Hypomorphic Pathogenic variants in TAF13 are associated with autosomal-
RT recessive intellectual disability and microcephaly.";
RL Am. J. Hum. Genet. 100:555-561(2017).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 31-75 IN COMPLEX WITH TAF11,
RP DOMAIN, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9695952; DOI=10.1016/s0092-8674(00)81423-3;
RA Birck C., Poch O., Romier C., Ruff M., Mengus G., Lavigne A.C.,
RA Davidson I., Moras D.;
RT "Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by
RT atypical evolutionary conserved motifs also found in the SPT3 family.";
RL Cell 94:239-249(1998).
RN [8] {ECO:0007744|PDB:7EDX, ECO:0007744|PDB:7EG7, ECO:0007744|PDB:7EG8, ECO:0007744|PDB:7EG9, ECO:0007744|PDB:7EGA, ECO:0007744|PDB:7EGB, ECO:0007744|PDB:7EGC, ECO:0007744|PDB:7EGD, ECO:0007744|PDB:7EGE, ECO:0007744|PDB:7EGF}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.16 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE TFIID COMPLEX, AND SUBUNIT.
RX PubMed=33795473; DOI=10.1126/science.aba8490;
RA Chen X., Qi Y., Wu Z., Wang X., Li J., Zhao D., Hou H., Li Y., Yu Z.,
RA Liu W., Wang M., Ren Y., Li Z., Yang H., Xu Y.;
RT "Structural insights into preinitiation complex assembly on core
RT promoters.";
RL Science 372:0-0(2021).
CC -!- FUNCTION: The TFIID basal transcription factor complex plays a major
CC role in the initiation of RNA polymerase II (Pol II)-dependent
CC transcription (PubMed:33795473, PubMed:9695952). TFIID recognizes and
CC binds promoters via its subunit TBP, a TATA-box-binding protein, and
CC promotes assembly of the pre-initiation complex (PIC)
CC (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated
CC factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7,
CC TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). TAF13,
CC together with TAF11 and TBP, play key roles during promoter binding by
CC the TFIID and TFIIA transcription factor complexes (PubMed:33795473).
CC {ECO:0000269|PubMed:33795473, ECO:0000269|PubMed:9695952}.
CC -!- SUBUNIT: Component of the TFIID basal transcription factor complex,
CC composed of TATA-box-binding protein TBP, and a number of TBP-
CC associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5,
CC TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13
CC (PubMed:33795473). Interacts with TBP, and more strongly with TAF10 and
CC TAF11 (PubMed:9695952). {ECO:0000269|PubMed:33795473,
CC ECO:0000269|PubMed:9695952}.
CC -!- INTERACTION:
CC Q15543; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-1026992, EBI-742948;
CC Q15543; Q5JR59-3: MTUS2; NbExp=4; IntAct=EBI-1026992, EBI-11522433;
CC Q15543; Q15544: TAF11; NbExp=2; IntAct=EBI-1026992, EBI-1027005;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9695952}.
CC -!- DOMAIN: The binding of TAF10 and TAF11 requires distinct domains of
CC TAF13. {ECO:0000269|PubMed:9695952}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 60
CC (MRT60) [MIM:617432]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRT60
CC patients display mild intellectual disability, delayed psychomotor
CC development, learning difficulties, and poor overall growth with
CC variable microcephaly. {ECO:0000269|PubMed:28257693}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TAF13 family. {ECO:0000305}.
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DR EMBL; X84003; CAA58827.1; -; mRNA.
DR EMBL; AK312158; BAG35092.1; -; mRNA.
DR EMBL; BX679664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56354.1; -; Genomic_DNA.
DR EMBL; BC121180; AAI21181.1; -; mRNA.
DR CCDS; CCDS30788.1; -.
DR PIR; S54782; S54782.
DR RefSeq; NP_005636.1; NM_005645.3.
DR PDB; 1BH8; X-ray; 3.00 A; A=31-75.
DR PDB; 1BH9; X-ray; 2.60 A; A=31-75.
DR PDB; 6MZD; EM; 9.80 A; S=1-124.
DR PDB; 6MZL; EM; 23.00 A; S=1-124.
DR PDB; 7EDX; EM; 4.50 A; m=1-124.
DR PDB; 7EG7; EM; 6.20 A; m=1-124.
DR PDB; 7EG8; EM; 7.40 A; m=1-124.
DR PDB; 7EG9; EM; 3.70 A; m=1-124.
DR PDB; 7EGA; EM; 4.10 A; m=1-124.
DR PDB; 7EGB; EM; 3.30 A; m=1-124.
DR PDB; 7EGC; EM; 3.90 A; m=1-124.
DR PDB; 7EGD; EM; 6.75 A; m=1-124.
DR PDB; 7EGE; EM; 9.00 A; m=1-124.
DR PDB; 7EGF; EM; 3.16 A; m=1-124.
DR PDB; 7EGI; EM; 9.82 A; m=1-124.
DR PDB; 7EGJ; EM; 8.64 A; m=1-124.
DR PDB; 7ENA; EM; 4.07 A; Dm=1-124.
DR PDB; 7ENC; EM; 4.13 A; Dm=1-124.
DR PDBsum; 1BH8; -.
DR PDBsum; 1BH9; -.
DR PDBsum; 6MZD; -.
DR PDBsum; 6MZL; -.
DR PDBsum; 7EDX; -.
DR PDBsum; 7EG7; -.
DR PDBsum; 7EG8; -.
DR PDBsum; 7EG9; -.
DR PDBsum; 7EGA; -.
DR PDBsum; 7EGB; -.
DR PDBsum; 7EGC; -.
DR PDBsum; 7EGD; -.
DR PDBsum; 7EGE; -.
DR PDBsum; 7EGF; -.
DR PDBsum; 7EGI; -.
DR PDBsum; 7EGJ; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR AlphaFoldDB; Q15543; -.
DR SMR; Q15543; -.
DR BioGRID; 112747; 29.
DR ComplexPortal; CPX-915; General transcription factor complex TFIID.
DR ComplexPortal; CPX-930; General transcription factor complex TFIID, TAF4B variant.
DR CORUM; Q15543; -.
DR DIP; DIP-900N; -.
DR IntAct; Q15543; 11.
DR STRING; 9606.ENSP00000355051; -.
DR iPTMnet; Q15543; -.
DR PhosphoSitePlus; Q15543; -.
DR BioMuta; TAF13; -.
DR DMDM; 3024706; -.
DR EPD; Q15543; -.
DR jPOST; Q15543; -.
DR MassIVE; Q15543; -.
DR MaxQB; Q15543; -.
DR PaxDb; Q15543; -.
DR PeptideAtlas; Q15543; -.
DR PRIDE; Q15543; -.
DR ProteomicsDB; 60625; -.
DR Antibodypedia; 33744; 163 antibodies from 23 providers.
DR DNASU; 6884; -.
DR Ensembl; ENST00000338366.6; ENSP00000355051.4; ENSG00000197780.11.
DR GeneID; 6884; -.
DR KEGG; hsa:6884; -.
DR MANE-Select; ENST00000338366.6; ENSP00000355051.4; NM_005645.4; NP_005636.1.
DR UCSC; uc001dwm.2; human.
DR CTD; 6884; -.
DR DisGeNET; 6884; -.
DR GeneCards; TAF13; -.
DR HGNC; HGNC:11546; TAF13.
DR HPA; ENSG00000197780; Low tissue specificity.
DR MalaCards; TAF13; -.
DR MIM; 600774; gene.
DR MIM; 617432; phenotype.
DR neXtProt; NX_Q15543; -.
DR OpenTargets; ENSG00000197780; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR PharmGKB; PA36321; -.
DR VEuPathDB; HostDB:ENSG00000197780; -.
DR eggNOG; KOG3901; Eukaryota.
DR GeneTree; ENSGT00390000012981; -.
DR HOGENOM; CLU_076665_4_0_1; -.
DR InParanoid; Q15543; -.
DR OMA; INEMCLE; -.
DR OrthoDB; 1478135at2759; -.
DR PhylomeDB; Q15543; -.
DR TreeFam; TF323609; -.
DR PathwayCommons; Q15543; -.
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-6804756; Regulation of TP53 Activity through Phosphorylation.
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; Q15543; -.
DR SIGNOR; Q15543; -.
DR BioGRID-ORCS; 6884; 273 hits in 1086 CRISPR screens.
DR ChiTaRS; TAF13; human.
DR EvolutionaryTrace; Q15543; -.
DR GeneWiki; TAF13; -.
DR GenomeRNAi; 6884; -.
DR Pharos; Q15543; Tbio.
DR PRO; PR:Q15543; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15543; protein.
DR Bgee; ENSG00000197780; Expressed in medial globus pallidus and 188 other tissues.
DR ExpressionAtlas; Q15543; baseline and differential.
DR Genevisible; Q15543; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; EXP:ComplexPortal.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:ARUK-UCL.
DR GO; GO:0017025; F:TBP-class protein binding; IPI:ARUK-UCL.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; NAS:UniProtKB.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IPI:ComplexPortal.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IC:UniProtKB.
DR CDD; cd07978; TAF13; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003195; TFIID_TAF13.
DR PANTHER; PTHR11380; PTHR11380; 1.
DR Pfam; PF02269; TFIID-18kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Intellectual disability; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..124
FT /note="Transcription initiation factor TFIID subunit 13"
FT /id="PRO_0000118910"
FT DOMAIN 31..74
FT /note="Histone-fold"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 31
FT /note="L -> H (in MRT60; impairs interaction with TAF11;
FT dbSNP:rs1060505030)"
FT /evidence="ECO:0000269|PubMed:28257693"
FT /id="VAR_079046"
FT VARIANT 40
FT /note="M -> K (in MRT60; impairs interaction with TAF11;
FT dbSNP:rs1060505029)"
FT /evidence="ECO:0000269|PubMed:28257693"
FT /id="VAR_079047"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1BH9"
FT HELIX 51..74
FT /evidence="ECO:0007829|PDB:1BH9"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:7EGF"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:7EGF"
FT HELIX 94..113
FT /evidence="ECO:0007829|PDB:7EGF"
SQ SEQUENCE 124 AA; 14287 MW; 98B62FF1BC8E7B77 CRC64;
MADEEEDPTF EEENEEIGGG AEGGQGKRKR LFSKELRCMM YGFGDDQNPY TESVDILEDL
VIEFITEMTH KAMSIGRQGR VQVEDIVFLI RKDPRKFARV KDLLTMNEEL KRARKAFDEA
NYGS
