SDCB1_MOUSE
ID SDCB1_MOUSE Reviewed; 299 AA.
AC O08992; A2AKJ7; Q544P5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Syntenin-1;
DE AltName: Full=Scaffold protein Pbp1;
DE AltName: Full=Syndecan-binding protein 1;
GN Name=Sdcbp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Burbelo P.D.;
RT "A new family of scaffold proteins.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hsu S.I.-H., Hentschel D.M., Bonventre J.V.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Amnion, Bone marrow, Heart, Kidney, Liver, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH PDCD6IP, DOMAIN LYPX(N)L MOTIF, AND MUTAGENESIS OF
RP 4-ALA--ALA-5; 47-ALA--ALA-48 AND 51-ALA--ALA-52.
RX PubMed=22660413; DOI=10.1038/ncb2502;
RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A.,
RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P.,
RA David G.;
RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
RL Nat. Cell Biol. 14:677-685(2012).
RN [8]
RP FUNCTION.
RX PubMed=26539120; DOI=10.3389/fphar.2015.00241;
RA Kashyap R., Roucourt B., Lembo F., Fares J., Carcavilla A.M., Restouin A.,
RA Zimmermann P., Ghossoub R.;
RT "Syntenin controls migration, growth, proliferation, and cell cycle
RT progression in cancer cells.";
RL Front. Pharmacol. 6:241-241(2015).
RN [9]
RP INTERACTION WITH SMO.
RX PubMed=25644602; DOI=10.1101/gad.252676.114;
RA Chong Y.C., Mann R.K., Zhao C., Kato M., Beachy P.A.;
RT "Bifurcating action of Smoothened in Hedgehog signaling is mediated by
RT Dlg5.";
RL Genes Dev. 29:262-276(2015).
CC -!- FUNCTION: Multifunctional adapter protein involved in diverse array of
CC functions including trafficking of transmembrane proteins, neuro and
CC immunomodulation, exosome biogenesis, and tumorigenesis. Positively
CC regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced
CC epithelial-to-mesenchymal transition (EMT) and cell migration in
CC various cell types. May increase TGFB1 signaling by enhancing cell-
CC surface expression of TGFR1 by preventing the interaction between TGFR1
CC and CAV1 and subsequent CAV1-dependent internalization and degradation
CC of TGFR1. In concert with SDC1/4 and PDCD6IP, regulates exosome
CC biogenesis (By similarity). Regulates migration, growth, proliferation,
CC and cell cycle progression in a variety of cancer types
CC (PubMed:26539120). In adherens junctions may function to couple
CC syndecans to cytoskeletal proteins or signaling components. Seems to
CC couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also
CC play a role in vesicular trafficking. Seems to be required for the
CC targeting of TGFA to the cell surface in the early secretory pathway
CC (By similarity). {ECO:0000250|UniProtKB:O00560,
CC ECO:0000269|PubMed:26539120}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with SDC1, SDC2, SDC3, SDC4,
CC NRXN2, EPHA7, EPHB1, NF2 isoform 1, TGFA, IL5RA, NFASC, SDCBP2 and
CC PTPRJ (By similarity). Interacts with PDCD6IP (PubMed:22660413). Forms
CC a complex with PDCD6IP and SDC2 (By similarity). Interacts (via C-
CC terminus) with TGFBR1 (By similarity). Binds to FZD7; this interaction
CC is increased by inositol trisphosphate (IP3) (By similarity). Interacts
CC with SMO (PubMed:25644602). {ECO:0000250|UniProtKB:O00560,
CC ECO:0000250|UniProtKB:Q9JI92, ECO:0000269|PubMed:22660413,
CC ECO:0000269|PubMed:25644602}.
CC -!- INTERACTION:
CC O08992; P52795: Efnb1; NbExp=3; IntAct=EBI-538265, EBI-8107507;
CC O08992; Q9WU78: Pdcd6ip; NbExp=3; IntAct=EBI-538265, EBI-641897;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:O00560}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:O00560}. Cell membrane
CC {ECO:0000250|UniProtKB:O00560}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O00560}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O00560}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O00560}. Nucleus {ECO:0000250|UniProtKB:O00560}.
CC Melanosome {ECO:0000250|UniProtKB:O00560}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O00560}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O00560}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:O00560}. Membrane raft
CC {ECO:0000250|UniProtKB:O00560}. Note=Mainly membrane-associated.
CC Localized to adherens junctions, focal adhesions and endoplasmic
CC reticulum. Colocalized with actin stress fibers. Also found in the
CC nucleus. Identified by mass spectrometry in melanosome fractions from
CC stage I to stage IV. Associated to the plasma membrane in the presence
CC of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2) (By
CC similarity). {ECO:0000250|UniProtKB:O00560}.
CC -!- PTM: Phosphorylated on tyrosine residues. {ECO:0000250}.
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DR EMBL; AF003693; AAB61293.1; -; mRNA.
DR EMBL; AK028429; BAC25946.1; -; mRNA.
DR EMBL; AK033412; BAC28275.1; -; mRNA.
DR EMBL; AK146085; BAE26889.1; -; mRNA.
DR EMBL; AK150278; BAE29434.1; -; mRNA.
DR EMBL; AK150321; BAE29466.1; -; mRNA.
DR EMBL; AK150623; BAE29713.1; -; mRNA.
DR EMBL; AK150721; BAE29799.1; -; mRNA.
DR EMBL; AK150801; BAE29864.1; -; mRNA.
DR EMBL; AK152017; BAE30879.1; -; mRNA.
DR EMBL; AK152434; BAE31216.1; -; mRNA.
DR EMBL; AK152552; BAE31306.1; -; mRNA.
DR EMBL; AK159677; BAE35280.1; -; mRNA.
DR EMBL; AK167513; BAE39588.1; -; mRNA.
DR EMBL; AK168004; BAE39992.1; -; mRNA.
DR EMBL; AK168777; BAE40613.1; -; mRNA.
DR EMBL; AK169219; BAE40990.1; -; mRNA.
DR EMBL; AK169687; BAE41305.1; -; mRNA.
DR EMBL; AK171162; BAE42284.1; -; mRNA.
DR EMBL; AL772306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019400; AAH19400.1; -; mRNA.
DR CCDS; CCDS51110.1; -.
DR RefSeq; NP_001091697.1; NM_001098227.1.
DR RefSeq; NP_058087.2; NM_016807.2.
DR RefSeq; XP_006538147.1; XM_006538084.3.
DR AlphaFoldDB; O08992; -.
DR SMR; O08992; -.
DR BioGRID; 207300; 28.
DR ComplexPortal; CPX-3283; Syndecan-1-syntenin-1-ALIX complex.
DR IntAct; O08992; 9.
DR MINT; O08992; -.
DR STRING; 10090.ENSMUSP00000029912; -.
DR ChEMBL; CHEMBL4739669; -.
DR iPTMnet; O08992; -.
DR PhosphoSitePlus; O08992; -.
DR EPD; O08992; -.
DR MaxQB; O08992; -.
DR PaxDb; O08992; -.
DR PeptideAtlas; O08992; -.
DR PRIDE; O08992; -.
DR ProteomicsDB; 255376; -.
DR Antibodypedia; 3216; 535 antibodies from 38 providers.
DR DNASU; 53378; -.
DR Ensembl; ENSMUST00000029912; ENSMUSP00000029912; ENSMUSG00000028249.
DR GeneID; 53378; -.
DR KEGG; mmu:53378; -.
DR UCSC; uc008rxn.1; mouse.
DR CTD; 6386; -.
DR MGI; MGI:1337026; Sdcbp.
DR VEuPathDB; HostDB:ENSMUSG00000028249; -.
DR eggNOG; KOG0849; Eukaryota.
DR GeneTree; ENSGT00940000154502; -.
DR InParanoid; O08992; -.
DR OMA; EIKQRIC; -.
DR OrthoDB; 1035679at2759; -.
DR PhylomeDB; O08992; -.
DR TreeFam; TF327131; -.
DR Reactome; R-MMU-3928664; Ephrin signaling.
DR Reactome; R-MMU-447043; Neurofascin interactions.
DR Reactome; R-MMU-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-MMU-5675482; Regulation of necroptotic cell death.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 53378; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Sdcbp; mouse.
DR PRO; PR:O08992; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O08992; protein.
DR Bgee; ENSMUSG00000028249; Expressed in stroma of bone marrow and 253 other tissues.
DR ExpressionAtlas; O08992; baseline and differential.
DR Genevisible; O08992; MM.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005895; C:interleukin-5 receptor complex; IMP:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0046875; F:ephrin receptor binding; ISO:MGI.
DR GO; GO:0005109; F:frizzled binding; ISO:MGI.
DR GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005137; F:interleukin-5 receptor binding; IMP:UniProtKB.
DR GO; GO:0042043; F:neurexin family protein binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0045545; F:syndecan binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0002091; P:negative regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; ISO:MGI.
DR GO; GO:1903553; P:positive regulation of extracellular exosome assembly; ISO:MGI.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0099054; P:presynapse assembly; ISO:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IPI:MGI.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR030528; SDCBP.
DR PANTHER; PTHR12345:SF10; PTHR12345:SF10; 1.
DR Pfam; PF00595; PDZ; 2.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50106; PDZ; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Endoplasmic reticulum; Lipid-binding; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00560"
FT CHAIN 2..299
FT /note="Syntenin-1"
FT /id="PRO_0000184002"
FT DOMAIN 115..194
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 199..273
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 2..103
FT /note="Interaction with PDCD6IP"
FT /evidence="ECO:0000269|PubMed:22660413"
FT MOTIF 3..7
FT /note="LYPX(n)L motif 1"
FT /evidence="ECO:0000305|PubMed:22660413"
FT MOTIF 46..50
FT /note="LYPX(n)L motif 2"
FT /evidence="ECO:0000305|PubMed:22660413"
FT MOTIF 50..54
FT /note="LYPX(n)L motif 3"
FT /evidence="ECO:0000305|PubMed:22660413"
FT BINDING 251..252
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:O00560"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O00560"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00560"
FT MOD_RES 47
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O00560"
FT MUTAGEN 4..5
FT /note="YP->AA: No loss of interaction with PDCD6IP. Loss of
FT interaction with PDCD6IP; when associated with 46-A--A-47
FT and 50-A--A-51."
FT /evidence="ECO:0000269|PubMed:22660413"
FT MUTAGEN 47..48
FT /note="YP->AA: No loss of interaction with PDCD6IP. Loss of
FT interaction with PDCD6IP; when associated with 4-A--A-5 and
FT 51-A--A-52."
FT /evidence="ECO:0000269|PubMed:22660413"
FT MUTAGEN 51..52
FT /note="YP->AA: No loss of interaction with PDCD6IP. Loss of
FT interaction with PDCD6IP; when associated with 4-A--A-5 and
FT 47-A--A-48."
FT /evidence="ECO:0000269|PubMed:22660413"
SQ SEQUENCE 299 AA; 32379 MW; 04FFF7A33A7F0195 CRC64;
MSLYPSLEDL KVDKVIQAQT AYSANPASQA FVLVDASAAL PPDGNLYPKL YPELSQYMGL
SLNEAEICES MPMVSGAPAQ GQLVARPSSV NYMVAPVTGN DAGIRRAEIK QGIREVILCK
DQDGKIGLRL KSIDNGIFVQ LVQANSPASL VGLRFGDQVL QINGENCAGW SSDKAHKVLK
QAFGEKITMT IRDRPFERTV TMHKDSSGHV GFIFKSGKIT SIVKDSSAAR NGLLTDHHIC
EINGQNVIGL KDAQIADILS TAGTVVTITI MPTFIFEHII KRMAPSIMKS LMDHTIPEV
