ID DLRB1_HUMAN Reviewed; 96 AA. AC Q9NP97; B1AKR5; Q5TC72; Q96IV3; Q9NQM2; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 194. DE RecName: Full=Dynein light chain roadblock-type 1; DE AltName: Full=Bithoraxoid-like protein; DE Short=BLP; DE AltName: Full=Dynein light chain 2A, cytoplasmic; DE AltName: Full=Dynein-associated protein Km23; DE AltName: Full=Roadblock domain-containing protein 1; GN Name=DYNLRB1 {ECO:0000312|HGNC:HGNC:15468}; GN Synonyms=BITH, DNCL2A, DNLC2A, ROBLD1; ORFNames=HSPC162; 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), AND TISSUE SPECIFICITY. RC TISSUE=Liver, and Testis; RX PubMed=11750132; DOI=10.1016/s0378-1119(01)00787-9; RA Jiang J., Yu L., Huang X., Chen X., Li D., Zhang Y., Tang L., Zhao S.; RT "Identification of two novel human dynein light chain genes, DNLC2A and RT DNLC2B, and their expression changes in hepatocellular carcinoma tissues RT from 68 Chinese patients."; RL Gene 281:103-113(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hematopoietic stem cell; RA Gu J., Huang Q., Yu Y., Xu S., Han Z., Fu G., Zhou J., Wang Y., Huang C., RA Ren S., Tu Y., Chen Z.; RT "Novel genes expressed in hematopoietic stem/progenitor cells from RT myelodysplastic syndrome patients."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Fracchiolla N.S., Cortelezzi A., Lambertenghi-Deliliers G.; RT "BitH, a human homolog of bithorax Drosophila melanogaster gene, on RT chromosome 20q."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Placenta; RA Tang Q., Staub C.M., Mulder K.M.; RT "Km23: role in growth factor signaling."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Kidney, and Lymph; 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 PROTEIN SEQUENCE OF 2-10. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [9] RP PROTEIN SEQUENCE OF 16-52 AND 59-70, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [10] RP INTERACTION WITH DYNC1I1 AND DYNC1I2. RX PubMed=12077152; DOI=10.1074/jbc.m205510200; RA Susalka S.J., Nikulina K., Salata M.W., Vaughan P.S., King S.M., RA Vaughan K.T., Pfister K.K.; RT "The roadblock light chain binds a novel region of the cytoplasmic Dynein RT intermediate chain."; RL J. Biol. Chem. 277:32939-32946(2002). RN [11] RP INTERACTION WITH RAP6A AND RAP6B. RX PubMed=18044744; DOI=10.1002/cm.20254; RA Wanschers B.F.J., van de Vorstenbosch R., Wijers M., Wieringa B., RA King S.M., Fransen J.; RT "Rab6 family proteins interact with the dynein light chain protein RT DYNLRB1."; RL Cell Motil. Cytoskeleton 65:183-196(2008). RN [12] 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [14] RP STRUCTURE BY NMR, AND SUBUNIT. RX PubMed=16083906; DOI=10.1016/j.jmb.2005.07.002; RA Ilangovan U., Ding W., Zhong Y., Wilson C.L., Groppe J.C., Trbovich J.T., RA Zuniga J., Demeler B., Tang Q., Gao G., Mulder K.M., Hinck A.P.; RT "Structure and dynamics of the homodimeric dynein light chain km23."; RL J. Mol. Biol. 352:338-354(2005). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT. RX PubMed=16970917; DOI=10.1016/j.bbrc.2006.08.161; RA Liu J.F., Wang Z.X., Wang X.Q., Tang Q., An X.M., Gui L.L., Liang D.C.; RT "Crystal structure of human dynein light chain Dnlc2A: structural insights RT into the interaction with IC74."; RL Biochem. Biophys. Res. Commun. 349:1125-1129(2006). RN [16] {ECO:0007744|PDB:6F1T, ECO:0007744|PDB:6F1Z, ECO:0007744|PDB:6F38, ECO:0007744|PDB:6F3A} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), AND SUBUNIT. RX PubMed=29420470; DOI=10.1038/nature25462; RA Urnavicius L., Lau C.K., Elshenawy M.M., Morales-Rios E., Motz C., RA Yildiz A., Carter A.P.; RT "Cryo-EM shows how dynactin recruits two dyneins for faster movement."; RL Nature 554:202-206(2018). RN [17] {ECO:0007744|PDB:7Z8F} RP STRUCTURE BY ELECTRON MICROSCOPY (20.00 ANGSTROMS), AND SUBUNIT. RX PubMed=36071160; DOI=10.1038/s41586-022-05186-y; RA Chaaban S., Carter A.P.; RT "Structure of dynein-dynactin on microtubules shows tandem adaptor RT binding."; RL Nature 610:212-216(2022). CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of CC the cytoplasmic dynein 1 complex that are thought to be involved in CC linking dynein to cargos and to adapter proteins that regulate dynein CC function. Cytoplasmic dynein 1 acts as a motor for the intracellular CC retrograde motility of vesicles and organelles along microtubules. CC {ECO:0000305|PubMed:36071160}. CC -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two CC catalytic heavy chains (HCs) and a number of non-catalytic subunits CC presented by intermediate chains (ICs), light intermediate chains CC (LICs) and light chains (LCs); the composition seems to vary in respect CC to the IC, LIC and LC composition. The heavy chain homodimer serves as CC a scaffold for the probable homodimeric assembly of the respective non- CC catalytic subunits. The ICs and LICs bind directly to the HC dimer and CC the LCs assemble on the IC dimer (PubMed:16083906, PubMed:16970917, CC PubMed:29420470, PubMed:36071160). Interacts with DYNLRB2. Interacts CC with DYNC1I1 and DYNC1I2 (PubMed:12077152). Interacts with RAB6A CC isoform 1 (GTP-bound); the interaction is direct. Interacts with RAB6A CC isoform 2 (GDP-bound); the interaction is direct. Interacts with RAB6B CC (GDP-bound) (PubMed:18044744). {ECO:0000269|PubMed:12077152, CC ECO:0000269|PubMed:16083906, ECO:0000269|PubMed:16970917, CC ECO:0000269|PubMed:18044744, ECO:0000269|PubMed:29420470, CC ECO:0000269|PubMed:36071160}. CC -!- INTERACTION: CC Q9NP97; O75575-2: CRCP; NbExp=3; IntAct=EBI-372128, EBI-12880830; CC Q9NP97; Q13409: DYNC1I2; NbExp=5; IntAct=EBI-372128, EBI-742998; CC Q9NP97; P43356: MAGEA2B; NbExp=3; IntAct=EBI-372128, EBI-5650739; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000305|PubMed:36071160}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=Q9NP97-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NP97-2; Sequence=VSP_007236, VSP_007237; CC -!- TISSUE SPECIFICITY: High expression in heart, liver, brain and CC pancreas; moderate in placenta, skeletal muscle and kidney; low in CC lung, prostate, testis, small intestine and colon. Isoform 1 expression CC is up-regulated in 64% hepatocellular carcinoma (HCC) patients. CC {ECO:0000269|PubMed:11750132}. CC -!- MISCELLANEOUS: [Isoform 2]: May result from the retention of an intron CC in the cDNA. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the GAMAD family. {ECO:0000305}. 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; AF132750; AAL75951.1; -; mRNA. DR EMBL; AF165516; AAF86646.1; -; mRNA. DR EMBL; AF178431; AAK95342.1; -; mRNA. DR EMBL; AY026513; AAK18712.1; -; mRNA. DR EMBL; AF161511; AAF29126.1; -; mRNA. DR EMBL; AL109923; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL136173; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002481; AAH02481.1; -; mRNA. DR EMBL; BC007223; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS13235.1; -. [Q9NP97-1] DR RefSeq; NP_001268656.1; NM_001281727.1. DR RefSeq; NP_001268657.1; NM_001281728.1. DR RefSeq; NP_001268658.1; NM_001281729.1. DR RefSeq; NP_054902.1; NM_014183.3. [Q9NP97-1] DR RefSeq; NP_808852.1; NM_177953.2. DR PDB; 1Z09; NMR; -; A/B=1-96. DR PDB; 2B95; NMR; -; A/B=1-96. DR PDB; 2E8J; NMR; -; A/B=1-96. DR PDB; 2HZ5; X-ray; 2.10 A; A/B=1-96. DR PDB; 6F1T; EM; 3.50 A; k/l/s/t=1-96. DR PDB; 6F1Z; EM; 3.40 A; s/t=1-96. DR PDB; 6F38; EM; 6.70 A; k/l/s/t=1-96. DR PDB; 6F3A; EM; 8.20 A; k/l=1-96. DR PDB; 6RLB; EM; 4.50 A; G/H=1-96. DR PDB; 6SC2; EM; 3.90 A; G/H=1-96. DR PDB; 7Z8F; EM; 20.00 A; k/l/s/t=1-96. DR PDB; 8J07; EM; 4.10 A; k4/m4/o4/q4=1-96. DR PDBsum; 1Z09; -. DR PDBsum; 2B95; -. DR PDBsum; 2E8J; -. DR PDBsum; 2HZ5; -. DR PDBsum; 6F1T; -. DR PDBsum; 6F1Z; -. DR PDBsum; 6F38; -. DR PDBsum; 6F3A; -. DR PDBsum; 6RLB; -. DR PDBsum; 6SC2; -. DR PDBsum; 7Z8F; -. DR PDBsum; 8J07; -. DR AlphaFoldDB; Q9NP97; -. DR BMRB; Q9NP97; -. DR EMDB; EMD-14549; -. DR EMDB; EMD-35888; -. DR EMDB; EMD-4168; -. DR EMDB; EMD-4172; -. DR EMDB; EMD-4177; -. DR EMDB; EMD-4918; -. DR SMR; Q9NP97; -. DR BioGRID; 123715; 103. DR ComplexPortal; CPX-5025; Cytoplasmic dynein complex, variant 1. DR CORUM; Q9NP97; -. DR IntAct; Q9NP97; 35. DR MINT; Q9NP97; -. DR STRING; 9606.ENSP00000349679; -. DR iPTMnet; Q9NP97; -. DR PhosphoSitePlus; Q9NP97; -. DR BioMuta; DYNLRB1; -. DR EPD; Q9NP97; -. DR jPOST; Q9NP97; -. DR MassIVE; Q9NP97; -. DR MaxQB; Q9NP97; -. DR PaxDb; 9606-ENSP00000349679; -. DR PeptideAtlas; Q9NP97; -. DR ProteomicsDB; 81939; -. [Q9NP97-1] DR ProteomicsDB; 81940; -. [Q9NP97-2] DR Pumba; Q9NP97; -. DR TopDownProteomics; Q9NP97-1; -. [Q9NP97-1] DR TopDownProteomics; Q9NP97-2; -. [Q9NP97-2] DR Antibodypedia; 4076; 87 antibodies from 21 providers. DR DNASU; 83658; -. DR Ensembl; ENST00000300469.13; ENSP00000300469.9; ENSG00000125971.18. [Q9NP97-2] DR Ensembl; ENST00000357156.7; ENSP00000349679.2; ENSG00000125971.18. [Q9NP97-1] DR Ensembl; ENST00000480759.1; ENSP00000513022.1; ENSG00000125971.18. [Q9NP97-2] DR GeneID; 83658; -. DR KEGG; hsa:83658; -. DR MANE-Select; ENST00000357156.7; ENSP00000349679.2; NM_014183.4; NP_054902.1. DR UCSC; uc002xal.5; human. [Q9NP97-1] DR AGR; HGNC:15468; -. DR CTD; 83658; -. DR DisGeNET; 83658; -. DR GeneCards; DYNLRB1; -. DR HGNC; HGNC:15468; DYNLRB1. DR HPA; ENSG00000125971; Low tissue specificity. DR MIM; 607167; gene. DR neXtProt; NX_Q9NP97; -. DR OpenTargets; ENSG00000125971; -. DR PharmGKB; PA27436; -. DR VEuPathDB; HostDB:ENSG00000125971; -. DR eggNOG; KOG4115; Eukaryota. DR GeneTree; ENSGT00390000011067; -. DR HOGENOM; CLU_113002_3_2_1; -. DR InParanoid; Q9NP97; -. DR OMA; LMHNLIM; -. DR OrthoDB; 36462at2759; -. DR PhylomeDB; Q9NP97; -. DR TreeFam; TF315165; -. DR PathwayCommons; Q9NP97; -. DR Reactome; R-HSA-5620924; Intraflagellar transport. DR SignaLink; Q9NP97; -. DR SIGNOR; Q9NP97; -. DR BioGRID-ORCS; 83658; 792 hits in 1128 CRISPR screens. DR ChiTaRS; DYNLRB1; human. DR EvolutionaryTrace; Q9NP97; -. DR GeneWiki; DYNLRB1; -. DR GenomeRNAi; 83658; -. DR Pharos; Q9NP97; Tbio. DR PRO; PR:Q9NP97; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q9NP97; Protein. DR Bgee; ENSG00000125971; Expressed in Brodmann (1909) area 9 and 95 other cell types or tissues. DR ExpressionAtlas; Q9NP97; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0097542; C:ciliary tip; TAS:Reactome. DR GO; GO:0005929; C:cilium; TAS:Reactome. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB. DR GO; GO:0030286; C:dynein complex; IPI:ComplexPortal. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central. DR GO; GO:0003777; F:microtubule motor activity; NAS:UniProtKB. DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central. DR GO; GO:0007632; P:visual behavior; ISS:UniProtKB. DR Gene3D; 3.30.450.30; Dynein light chain 2a, cytoplasmic; 1. DR InterPro; IPR016561; DYNLRB1/2. DR InterPro; IPR004942; Roadblock/LAMTOR2_dom. DR PANTHER; PTHR10779; DYNEIN LIGHT CHAIN ROADBLOCK; 1. DR PANTHER; PTHR10779:SF17; DYNEIN LIGHT CHAIN ROADBLOCK-TYPE 1; 1. DR Pfam; PF03259; Robl_LC7; 1. DR PIRSF; PIRSF009998; DLC7; 1. DR SMART; SM00960; Robl_LC7; 1. DR SUPFAM; SSF103196; Roadblock/LC7 domain; 1. DR Genevisible; Q9NP97; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Dynein; Microtubule; Motor protein; KW Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P62628, FT ECO:0000269|PubMed:12665801" FT CHAIN 2..96 FT /note="Dynein light chain roadblock-type 1" FT /id="PRO_0000220955" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P62628" FT VAR_SEQ 28..47 FT /note="IPIKSTMDNPTTTQYASLMH -> GWEPLGHCGDRSRPPAQGCP (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007236" FT VAR_SEQ 48..96 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007237" FT VARIANT 13 FT /note="S -> R (in dbSNP:rs1063616)" FT /id="VAR_049124" FT VARIANT 71 FT /note="I -> F (in dbSNP:rs10036)" FT /id="VAR_049125" FT HELIX 6..12 FT /evidence="ECO:0007829|PDB:2HZ5" FT STRAND 14..16 FT /evidence="ECO:0007829|PDB:6F1T" FT STRAND 17..23 FT /evidence="ECO:0007829|PDB:2HZ5" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:6F1Z" FT STRAND 29..34 FT /evidence="ECO:0007829|PDB:2HZ5" FT HELIX 36..60 FT /evidence="ECO:0007829|PDB:2HZ5" FT STRAND 66..75 FT /evidence="ECO:0007829|PDB:2HZ5" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:2HZ5" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:2HZ5" SQ SEQUENCE 96 AA; 10922 MW; AAE1EFCD372897B3 CRC64; MAEVEETLKR LQSQKGVQGI IVVNTEGIPI KSTMDNPTTT QYASLMHSFI LKARSTVRDI DPQNDLTFLR IRSKKNEIMV APDKDYFLIV IQNPTE //