TRI26_HUMAN
ID TRI26_HUMAN Reviewed; 539 AA.
AC Q12899; A6NG96; Q5SRL2;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Tripartite motif-containing protein 26;
DE EC=2.3.2.27 {ECO:0000269|PubMed:26611359};
DE AltName: Full=Acid finger protein;
DE Short=AFP;
DE AltName: Full=RING finger protein 95;
DE AltName: Full=Zinc finger protein 173;
GN Name=TRIM26; Synonyms=RNF95, ZNF173;
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=8530076; DOI=10.1006/geno.1995.1236;
RA Chu T.W., Capossela A., Coleman R., Goei V.L., Nallur G., Gruen J.R.;
RT "Cloning of a new 'finger' protein gene (ZNF173) within the class I region
RT of the human MHC.";
RL Genomics 29:229-239(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
RT "Genome diversity in HLA: a new strategy for detection of genetic
RT polymorphisms in expressed genes within the HLA class III and class I
RT regions.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and 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 [8]
RP INTERACTION WITH INCA1.
RX PubMed=21750715; DOI=10.1371/journal.pone.0021505;
RA Zhang F., Baeumer N., Rode M., Ji P., Zhang T., Berdel W.E.,
RA Mueller-Tidow C.;
RT "The inhibitor of growth protein 5 (ING5) depends on INCA1 as a co-factor
RT for its antiproliferative effects.";
RL PLoS ONE 6:E21505-E21505(2011).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25763818; DOI=10.1371/journal.ppat.1004726;
RA Wang P., Zhao W., Zhao K., Zhang L., Gao C.;
RT "TRIM26 negatively regulates interferon-beta production and antiviral
RT response through polyubiquitination and degradation of nuclear IRF3.";
RL PLoS Pathog. 11:E1004726-E1004726(2015).
RN [10]
RP FUNCTION, INTERACTION WITH TBK1, AND UBIQUITINATION.
RX PubMed=26611359; DOI=10.1093/jmcb/mjv068;
RA Ran Y., Zhang J., Liu L.L., Pan Z.Y., Nie Y., Zhang H.Y., Wang Y.Y.;
RT "Autoubiquitination of TRIM26 links TBK1 to NEMO in RLR-mediated innate
RT antiviral immune response.";
RL J. Mol. Cell Biol. 8:31-43(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which regulates the IFN-beta
CC production and antiviral response downstream of various DNA-encoded
CC pattern-recognition receptors (PRRs). Promotes nuclear IRF3
CC ubiquitination and proteasomal degradation. Bridges together TBK1 and
CC NEMO during the innate response to viral infection leading to the
CC activation of TBK1. {ECO:0000269|PubMed:25763818,
CC ECO:0000269|PubMed:26611359}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:26611359};
CC -!- SUBUNIT: Interacts with TBK1; this interaction bridges together TBK1
CC and NEMO in order to activate TBK1 (PubMed:26611359). Interacts with
CC INCA1 (PubMed:21750715). {ECO:0000269|PubMed:21750715,
CC ECO:0000269|PubMed:26611359}.
CC -!- INTERACTION:
CC Q12899; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-2341136, EBI-10181188;
CC Q12899; Q86UB2: BIVM; NbExp=3; IntAct=EBI-2341136, EBI-12191873;
CC Q12899; O95208-2: EPN2; NbExp=3; IntAct=EBI-2341136, EBI-12135243;
CC Q12899; I6L9I8: EPN3; NbExp=3; IntAct=EBI-2341136, EBI-12866582;
CC Q12899; Q0VD86: INCA1; NbExp=2; IntAct=EBI-2341136, EBI-6509505;
CC Q12899; O75367: MACROH2A1; NbExp=3; IntAct=EBI-2341136, EBI-2868511;
CC Q12899; P43360: MAGEA6; NbExp=4; IntAct=EBI-2341136, EBI-1045155;
CC Q12899; Q9NVV9: THAP1; NbExp=6; IntAct=EBI-2341136, EBI-741515;
CC Q12899; Q08117: TLE5; NbExp=3; IntAct=EBI-2341136, EBI-717810;
CC Q12899; Q08117-2: TLE5; NbExp=3; IntAct=EBI-2341136, EBI-11741437;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25763818}. Nucleus
CC {ECO:0000269|PubMed:25763818}. Note=Viral infection mediates TRIM26
CC nuclear translocation. {ECO:0000269|PubMed:25763818}.
CC -!- PTM: Autoubiquitinates upon viral infection. In turn, autoubiquitinated
CC TRIM26 recruits NEMO and bridges TBK1-NEMO interaction.
CC {ECO:0000269|PubMed:26611359}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; U09825; AAA93131.1; -; mRNA.
DR EMBL; BA000025; BAB63330.1; -; Genomic_DNA.
DR EMBL; AB088090; BAC54923.1; -; Genomic_DNA.
DR EMBL; AB202086; BAE78607.1; -; Genomic_DNA.
DR EMBL; AB103596; BAF31258.1; -; Genomic_DNA.
DR EMBL; AL844220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR788282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR388382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03272.1; -; Genomic_DNA.
DR EMBL; BC024039; AAH24039.1; -; mRNA.
DR EMBL; BC032297; AAH32297.1; -; mRNA.
DR CCDS; CCDS4678.1; -.
DR RefSeq; NP_001229712.1; NM_001242783.1.
DR RefSeq; NP_003440.1; NM_003449.4.
DR RefSeq; XP_005249431.1; XM_005249374.2.
DR RefSeq; XP_005249432.1; XM_005249375.2.
DR RefSeq; XP_005249433.1; XM_005249376.2.
DR RefSeq; XP_005249434.1; XM_005249377.2.
DR RefSeq; XP_005249435.1; XM_005249378.2.
DR RefSeq; XP_006715243.1; XM_006715180.2.
DR AlphaFoldDB; Q12899; -.
DR SMR; Q12899; -.
DR BioGRID; 113515; 185.
DR DIP; DIP-52853N; -.
DR IntAct; Q12899; 75.
DR MINT; Q12899; -.
DR STRING; 9606.ENSP00000410446; -.
DR iPTMnet; Q12899; -.
DR PhosphoSitePlus; Q12899; -.
DR BioMuta; TRIM26; -.
DR DMDM; 17380344; -.
DR EPD; Q12899; -.
DR jPOST; Q12899; -.
DR MassIVE; Q12899; -.
DR PaxDb; Q12899; -.
DR PeptideAtlas; Q12899; -.
DR PRIDE; Q12899; -.
DR ProteomicsDB; 59009; -.
DR Antibodypedia; 26253; 138 antibodies from 21 providers.
DR DNASU; 7726; -.
DR Ensembl; ENST00000327357.9; ENSP00000331131.5; ENSG00000137313.15.
DR Ensembl; ENST00000383607.6; ENSP00000373102.2; ENSG00000137313.15.
DR Ensembl; ENST00000396558.5; ENSP00000379806.1; ENSG00000137313.15.
DR Ensembl; ENST00000415923.6; ENSP00000415755.2; ENSG00000231002.7.
DR Ensembl; ENST00000422349.5; ENSP00000396188.1; ENSG00000234046.7.
DR Ensembl; ENST00000425523.5; ENSP00000393011.1; ENSG00000228881.7.
DR Ensembl; ENST00000425831.5; ENSP00000394371.1; ENSG00000231641.9.
DR Ensembl; ENST00000427535.5; ENSP00000398545.1; ENSG00000234046.7.
DR Ensembl; ENST00000428486.5; ENSP00000414248.1; ENSG00000231002.7.
DR Ensembl; ENST00000432326.5; ENSP00000407876.1; ENSG00000231641.9.
DR Ensembl; ENST00000433314.5; ENSP00000402395.1; ENSG00000226060.7.
DR Ensembl; ENST00000436219.5; ENSP00000390258.1; ENSG00000230230.7.
DR Ensembl; ENST00000437089.5; ENSP00000395491.1; ENSG00000234127.9.
DR Ensembl; ENST00000438384.5; ENSP00000416737.1; ENSG00000231641.9.
DR Ensembl; ENST00000438908.5; ENSP00000409182.1; ENSG00000230230.7.
DR Ensembl; ENST00000439094.6; ENSP00000389203.2; ENSG00000228881.7.
DR Ensembl; ENST00000445259.6; ENSP00000407294.2; ENSG00000234046.7.
DR Ensembl; ENST00000447711.6; ENSP00000408233.2; ENSG00000226060.7.
DR Ensembl; ENST00000450392.5; ENSP00000394421.1; ENSG00000231002.7.
DR Ensembl; ENST00000453195.5; ENSP00000391879.1; ENSG00000234127.9.
DR Ensembl; ENST00000454678.7; ENSP00000410446.2; ENSG00000234127.9.
DR Ensembl; ENST00000455000.6; ENSP00000392805.2; ENSG00000230230.7.
DR Ensembl; ENST00000456093.5; ENSP00000406707.1; ENSG00000226060.7.
DR Ensembl; ENST00000456770.5; ENSP00000415328.1; ENSG00000228881.7.
DR GeneID; 7726; -.
DR KEGG; hsa:7726; -.
DR MANE-Select; ENST00000454678.7; ENSP00000410446.2; NM_003449.5; NP_003440.1.
DR UCSC; uc003npr.3; human.
DR CTD; 7726; -.
DR DisGeNET; 7726; -.
DR GeneCards; TRIM26; -.
DR HGNC; HGNC:12962; TRIM26.
DR HPA; ENSG00000234127; Low tissue specificity.
DR MIM; 600830; gene.
DR neXtProt; NX_Q12899; -.
DR OpenTargets; ENSG00000234127; -.
DR PharmGKB; PA37544; -.
DR VEuPathDB; HostDB:ENSG00000234127; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158668; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q12899; -.
DR OMA; PFFWLNW; -.
DR OrthoDB; 542578at2759; -.
DR PhylomeDB; Q12899; -.
DR TreeFam; TF342569; -.
DR PathwayCommons; Q12899; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q12899; -.
DR BioGRID-ORCS; 7726; 8 hits in 1105 CRISPR screens.
DR ChiTaRS; TRIM26; human.
DR GenomeRNAi; 7726; -.
DR Pharos; Q12899; Tbio.
DR PRO; PR:Q12899; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q12899; protein.
DR Bgee; ENSG00000234127; Expressed in granulocyte and 105 other tissues.
DR ExpressionAtlas; Q12899; baseline and differential.
DR Genevisible; Q12899; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; NAS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB.
DR Gene3D; 2.60.120.920; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Immunity; Innate immunity; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..539
FT /note="Tripartite motif-containing protein 26"
FT /id="PRO_0000056235"
FT DOMAIN 295..539
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 97..138
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 376..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 188..227
FT /evidence="ECO:0000255"
FT COMPBIAS 376..435
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VARIANT 197
FT /note="Q -> H (in dbSNP:rs17194565)"
FT /id="VAR_052138"
SQ SEQUENCE 539 AA; 62166 MW; 842A71C41F2E2348 CRC64;
MATSAPLRSL EEEVTCSICL DYLRDPVTID CGHVFCRSCT TDVRPISGSR PVCPLCKKPF
KKENIRPVWQ LASLVENIER LKVDKGRQPG EVTREQQDAK LCERHREKLH YYCEDDGKLL
CVMCRESREH RPHTAVLMEK AAQPHREKIL NHLSTLRRDR DKIQGFQAKG EADILAALKK
LQDQRQYIVA EFEQGHQFLR EREEHLLEQL AKLEQELTEG REKFKSRGVG ELARLALVIS
ELEGKAQQPA AELMQDTRDF LNRYPRKKFW VGKPIARVVK KKTGEFSDKL LSLQRGLREF
QGKLLRDLEY KTVSVTLDPQ SASGYLQLSE DWKCVTYTSL YKSAYLHPQQ FDCEPGVLGS
KGFTWGKVYW EVEVEREGWS EDEEEGDEEE EGEEEEEEEE AGYGDGYDDW ETDEDEESLG
DEEEEEEEEE EEVLESCMVG VARDSVKRKG DLSLRPEDGV WALRLSSSGI WANTSPEAEL
FPALRPRRVG IALDYEGGTV TFTNAESQEL IYTFTATFTR RLVPFLWLKW PGTRLLLRP
