GMEB1_HUMAN
ID GMEB1_HUMAN Reviewed; 573 AA.
AC Q9Y692; B1AT48; Q9NWH1; Q9UKD0;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Glucocorticoid modulatory element-binding protein 1;
DE Short=GMEB-1;
DE AltName: Full=DNA-binding protein p96PIF;
DE AltName: Full=Parvovirus initiation factor p96;
DE Short=PIF p96;
GN Name=GMEB1;
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).
RC TISSUE=Cervix carcinoma;
RX PubMed=10386584; DOI=10.1016/s0014-5793(99)00634-1;
RA Theriault J.R., Charette S.J., Lambert H., Landry J.;
RT "Cloning and characterization of hGMEB1, a novel glucocorticoid modulatory
RT element binding protein.";
RL FEBS Lett. 452:170-176(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PROTEIN SEQUENCE OF 159-172.
RC TISSUE=Cervix carcinoma;
RX PubMed=10523663; DOI=10.1128/mcb.19.11.7741;
RA Christensen J., Cotmore S.F., Tattersall P.;
RT "Two new members of the emerging KDWK family of combinatorial transcription
RT modulators bind as a heterodimer to flexibly spaced PuCGPy half-sites.";
RL Mol. Cell. Biol. 19:7741-7750(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Heart;
RX PubMed=10894151; DOI=10.1210/mend.14.7.0494;
RA Kaul S., Blackford J.A. Jr., Chen J., Ogryzko V.V., Simons S.S. Jr.;
RT "Properties of the glucocorticoid modulatory element binding proteins GMEB-
RT 1 and -2: potential new modifiers of glucocorticoid receptor
RT transactivation and members of the family of KDWK proteins.";
RL Mol. Endocrinol. 14:1010-1027(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trophoblast;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 87-182, DNA-BINDING, AND
RP ZINC-BINDING.
RX PubMed=12702733; DOI=10.1210/me.2002-0409;
RA Surdo P.L., Bottomley M.J., Sattler M., Scheffzek K.;
RT "Crystal structure and nuclear magnetic resonance analyses of the SAND
RT domain from glucocorticoid modulatory element binding protein-1 reveals
RT deoxyribonucleic acid and zinc binding regions.";
RL Mol. Endocrinol. 17:1283-1295(2003).
CC -!- FUNCTION: Trans-acting factor that binds to glucocorticoid modulatory
CC elements (GME) present in the TAT (tyrosine aminotransferase) promoter
CC and increases sensitivity to low concentrations of glucocorticoids.
CC Binds also to the transferrin receptor promoter. Essential auxiliary
CC factor for the replication of parvoviruses.
CC -!- SUBUNIT: Homodimer, and heterodimer of GMEB1 and GMEB2. GMEB1 and GMEB2
CC form the parvovirus initiator complex (PIF). Interacts with the
CC glucocorticoid receptor (NR3C1) and NCOA2/TIF2 (By similarity). May
CC interact with HSP27 and CREB-binding protein (CBP). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y692; Q13114: TRAF3; NbExp=2; IntAct=EBI-2339665, EBI-357631;
CC Q9Y692-2; Q9Y692-2: GMEB1; NbExp=2; IntAct=EBI-21554939, EBI-21554939;
CC Q9Y692-2; O88873: Gmeb2; Xeno; NbExp=5; IntAct=EBI-21554939, EBI-25780616;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=May be also cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y692-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y692-2; Sequence=VSP_005970;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF099013; AAD39355.1; -; mRNA.
DR EMBL; AF173868; AAD51352.1; -; mRNA.
DR EMBL; AF203694; AAG01189.1; -; mRNA.
DR EMBL; AK000892; BAA91410.1; -; mRNA.
DR EMBL; AL645729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07677.1; -; Genomic_DNA.
DR EMBL; BC001473; AAH01473.1; -; mRNA.
DR CCDS; CCDS327.1; -. [Q9Y692-1]
DR CCDS; CCDS328.1; -. [Q9Y692-2]
DR RefSeq; NP_001306603.1; NM_001319674.1. [Q9Y692-2]
DR RefSeq; NP_006573.2; NM_006582.3. [Q9Y692-1]
DR RefSeq; NP_077808.1; NM_024482.2. [Q9Y692-2]
DR RefSeq; XP_011538820.1; XM_011540518.2. [Q9Y692-1]
DR RefSeq; XP_011538821.1; XM_011540519.2. [Q9Y692-1]
DR RefSeq; XP_011538823.1; XM_011540521.2. [Q9Y692-2]
DR RefSeq; XP_016855576.1; XM_017000087.1. [Q9Y692-1]
DR PDB; 1OQJ; X-ray; 1.55 A; A/B=89-182.
DR PDBsum; 1OQJ; -.
DR AlphaFoldDB; Q9Y692; -.
DR SMR; Q9Y692; -.
DR BioGRID; 115930; 38.
DR IntAct; Q9Y692; 27.
DR MINT; Q9Y692; -.
DR STRING; 9606.ENSP00000294409; -.
DR GlyGen; Q9Y692; 13 sites, 2 O-linked glycans (13 sites).
DR iPTMnet; Q9Y692; -.
DR PhosphoSitePlus; Q9Y692; -.
DR BioMuta; GMEB1; -.
DR DMDM; 22001627; -.
DR EPD; Q9Y692; -.
DR jPOST; Q9Y692; -.
DR MassIVE; Q9Y692; -.
DR MaxQB; Q9Y692; -.
DR PaxDb; Q9Y692; -.
DR PeptideAtlas; Q9Y692; -.
DR PRIDE; Q9Y692; -.
DR ProteomicsDB; 86625; -. [Q9Y692-1]
DR ProteomicsDB; 86626; -. [Q9Y692-2]
DR Antibodypedia; 30978; 170 antibodies from 25 providers.
DR DNASU; 10691; -.
DR Ensembl; ENST00000294409.2; ENSP00000294409.2; ENSG00000162419.13. [Q9Y692-1]
DR Ensembl; ENST00000361872.8; ENSP00000355186.4; ENSG00000162419.13. [Q9Y692-2]
DR Ensembl; ENST00000373816.6; ENSP00000362922.1; ENSG00000162419.13. [Q9Y692-2]
DR GeneID; 10691; -.
DR KEGG; hsa:10691; -.
DR MANE-Select; ENST00000373816.6; ENSP00000362922.1; NM_001319674.2; NP_001306603.1. [Q9Y692-2]
DR UCSC; uc001bqz.4; human. [Q9Y692-1]
DR CTD; 10691; -.
DR DisGeNET; 10691; -.
DR GeneCards; GMEB1; -.
DR HGNC; HGNC:4370; GMEB1.
DR HPA; ENSG00000162419; Low tissue specificity.
DR MIM; 604409; gene.
DR neXtProt; NX_Q9Y692; -.
DR OpenTargets; ENSG00000162419; -.
DR PharmGKB; PA28755; -.
DR VEuPathDB; HostDB:ENSG00000162419; -.
DR eggNOG; KOG4333; Eukaryota.
DR GeneTree; ENSGT00410000025596; -.
DR HOGENOM; CLU_030344_1_0_1; -.
DR InParanoid; Q9Y692; -.
DR OMA; MVNPVEL; -.
DR OrthoDB; 692814at2759; -.
DR PhylomeDB; Q9Y692; -.
DR TreeFam; TF317090; -.
DR PathwayCommons; Q9Y692; -.
DR SignaLink; Q9Y692; -.
DR BioGRID-ORCS; 10691; 29 hits in 1103 CRISPR screens.
DR ChiTaRS; GMEB1; human.
DR EvolutionaryTrace; Q9Y692; -.
DR GeneWiki; GMEB1; -.
DR GenomeRNAi; 10691; -.
DR Pharos; Q9Y692; Tbio.
DR PRO; PR:Q9Y692; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y692; protein.
DR Bgee; ENSG00000162419; Expressed in endothelial cell and 181 other tissues.
DR ExpressionAtlas; Q9Y692; baseline and differential.
DR Genevisible; Q9Y692; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; TAS:ARUK-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0051008; F:Hsp27 protein binding; IPI:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.10.390.10; -; 1.
DR InterPro; IPR024830; GMEB1/2.
DR InterPro; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR000770; SAND_dom.
DR PANTHER; PTHR10417; PTHR10417; 1.
DR Pfam; PF01342; SAND; 1.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF63763; SSF63763; 1.
DR PROSITE; PS50864; SAND; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..573
FT /note="Glucocorticoid modulatory element-binding protein 1"
FT /id="PRO_0000074089"
FT DOMAIN 82..166
FT /note="SAND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT REGION 370..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 321..367
FT /evidence="ECO:0000255"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 139
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT BINDING 143
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT BINDING 146
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT BINDING 157
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 44..53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10523663,
FT ECO:0000303|PubMed:10894151, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_005970"
FT VARIANT 14
FT /note="V -> A (in dbSNP:rs11557120)"
FT /id="VAR_051894"
FT CONFLICT 401
FT /note="Q -> E (in Ref. 1; AAD39355)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="V -> M (in Ref. 4; BAA91410)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="T -> I (in Ref. 4; BAA91410)"
FT /evidence="ECO:0000305"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1OQJ"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1OQJ"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1OQJ"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1OQJ"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1OQJ"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:1OQJ"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1OQJ"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:1OQJ"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1OQJ"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:1OQJ"
FT TURN 168..172
FT /evidence="ECO:0007829|PDB:1OQJ"
SQ SEQUENCE 573 AA; 62591 MW; 8175B0730F1550B8 CRC64;
MANAEVSVPV GDVVVVPTEG NEGENPEDTK TQVILQLQPV QQGLFIDGHF YNRIYEAGSE
NNTAVVAVET HTIHKIEEGI DTGTIEANED MEIAYPITCG ESKAILLWKK FVCPGINVKC
VKFNDQLISP KHFVHLAGKS TLKDWKRAIR LGGIMLRKMM DSGQIDFYQH DKVCSNTCRS
TKFDLLISSA RAPVPGQQTS VVQTPTSADG SITQIAISEE SMEEAGLEWN SALTAAVTMA
TEEGVKKDSE EISEDTLMFW KGIADVGLME EVVCNIQKEI EELLRGVQQR LIQAPFQVTD
AAVLNNVAHT FGLMDTVKKV LDNRRNQVEQ GEEQFLYTLT DLERQLEEQK KQGQDHRLKS
QTVQNVVLMP VSTPKPPKRP RLQRPASTTV LSPSPPVQQP QFTVISPITI TPVGQSFSMG
NIPVATLSQG SSPVTVHTLP SGPQLFRYAT VVSSAKSSSP DTVTIHPSSS LALLSSTAMQ
DGSTLGNMTT MVSPVELVAM ESGLTSAIQA VESTSEDGQT IIEIDPAPDP EAEDTEGKAV
ILETELRTEE KVVAEMEEHQ HQVHNVEIVV LED
