DIP2A_MOUSE
ID DIP2A_MOUSE Reviewed; 1523 AA.
AC Q8BWT5; E0CXM7; Q8CHI0;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Disco-interacting protein 2 homolog A;
DE Short=DIP2 homolog A;
DE EC=6.2.1.1 {ECO:0000269|PubMed:30672040};
GN Name=Dip2a; Synonyms=Dip2, Kiaa0184;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1085.
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-1523.
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [4]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12137943; DOI=10.1016/s0378-1119(02)00694-7;
RA Mukhopadhyay M., Pelka P., DeSousa D., Kablar B., Schindler A.,
RA Rudnicki M.A., Campos A.R.;
RT "Cloning, genomic organization and expression pattern of a novel Drosophila
RT gene, the disco-interacting protein 2 (dip2), and its murine homolog.";
RL Gene 293:59-65(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, and Lung;
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 FSTL1.
RX PubMed=20054002; DOI=10.1074/jbc.m109.069468;
RA Ouchi N., Asaumi Y., Ohashi K., Higuchi A., Sono-Romanelli S., Oshima Y.,
RA Walsh K.;
RT "DIP2A functions as a FSTL1 receptor.";
RL J. Biol. Chem. 285:7127-7134(2010).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=26605542; DOI=10.1371/journal.pone.0143284;
RA Zhang L., Mabwi H.A., Palange N.J., Jia R., Ma J., Bah F.B., Sah R.K.,
RA Li D., Wang D., Bah F.B., Togo J., Jin H., Ban L., Feng X., Zheng Y.;
RT "Expression Patterns and Potential Biological Roles of Dip2a.";
RL PLoS ONE 10:e0143284-e0143284(2015).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=30672040; DOI=10.1002/cbin.11106;
RA Ma J., Chen L., He X.X., Wang Y.J., Yu H.L., He Z.X., Zhang L.Q.,
RA Zheng Y.W., Zhu X.J.;
RT "Functional prediction and characterization of Dip2 gene in mice.";
RL Cell Biol. Int. 43:421-428(2019).
RN [10]
RP FUNCTION, INTERACTION WITH CTTN AND SHANK3, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 235-PRO--PRO-238 AND 259-PRO--PRO-262.
RX PubMed=31600191; DOI=10.1371/journal.pbio.3000461;
RA Ma J., Zhang L.Q., He Z.X., He X.X., Wang Y.J., Jian Y.L., Wang X.,
RA Zhang B.B., Su C., Lu J., Huang B.Q., Zhang Y., Wang G.Y., Guo W.X.,
RA Qiu D.L., Mei L., Xiong W.C., Zheng Y.W., Zhu X.J.;
RT "Autism candidate gene DIP2A regulates spine morphogenesis via acetylation
RT of cortactin.";
RL PLoS Biol. 17:e3000461-e3000461(2019).
CC -!- FUNCTION: Catalyzes the de novo synthesis of acetyl-CoA in vitro
CC (PubMed:30672040). Promotes acetylation of CTTN, possibly by providing
CC the acetyl donor, ensuring correct dendritic spine morphology and
CC synaptic transmission (PubMed:31600191). Binds to follistatin-related
CC protein FSTL1 and may act as a cell surface receptor for FSTL1,
CC contributing to AKT activation and subsequent FSTL1-induced survival
CC and function of endothelial cells and cardiac myocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q14689, ECO:0000269|PubMed:30672040,
CC ECO:0000269|PubMed:31600191}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1;
CC Evidence={ECO:0000269|PubMed:30672040};
CC -!- SUBUNIT: Interacts with FSTL1; DIP2A may act as a cell surface receptor
CC for FSTL1 (PubMed:20054002). Interacts (via N-terminus) with CTTN (via
CC SH3 domain); the interaction promotes acetylation of CTTN and is
CC required for proper synaptic transmission (PubMed:31600191). Interacts
CC with SHANK3 (PubMed:31600191). {ECO:0000269|PubMed:20054002,
CC ECO:0000269|PubMed:31600191}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14689};
CC Peripheral membrane protein {ECO:0000305}. Mitochondrion
CC {ECO:0000269|PubMed:30672040}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:31600191}.
CC -!- TISSUE SPECIFICITY: Detected in heart, liver, spleen, lung, kidney and
CC brain with highest levels in brain (at protein level)
CC (PubMed:30672040). In adult cortex, preferentially expressed in
CC excitatory neurons (PubMed:31600191). Broadly expressed in neuronal,
CC reproductive and vascular tissues as well as in heart, kidney, liver
CC and lung with expression detected in neurons, mesenchyme, endothelium,
CC smooth muscle cells and cardiomyocytes (PubMed:26605542). Expressed in
CC ectoderm-derived tissues in the developing embryo (PubMed:26605542).
CC Expressed in the developing nervous system (PubMed:12137943).
CC {ECO:0000269|PubMed:12137943, ECO:0000269|PubMed:26605542,
CC ECO:0000269|PubMed:30672040, ECO:0000269|PubMed:31600191}.
CC -!- DEVELOPMENTAL STAGE: In brain, expressed from embryo to adult with a
CC constant increase during postnatal development in the cerebral cortex
CC (at protein level) (PubMed:31600191). Expressed at all stages of
CC embryonic development, including 7 dpc, 11 dpc, 15 dpc and 17 dpc
CC (PubMed:12137943). Higher level of expression is seen at later stages
CC of embryonic development (PubMed:12137943). In 9.5 dpc embryos,
CC expression is diffusely distributed in the regions of the brain, optic
CC vesicles, otic vesicles, cervical and upper thoracic segments of the
CC spinal cord (PubMed:12137943). The expression is more intense in the
CC dorsal portions of the central nervous system (CNS) (PubMed:12137943).
CC In the brain, expression is localized in prosencephalon, mesencephalon
CC and rhombencephalon (PubMed:12137943). In 10.5 embryos, expression area
CC is more restricted, but still within the CNS and the sense organs. The
CC spinal cord expression disappears (PubMed:12137943).
CC {ECO:0000269|PubMed:12137943, ECO:0000269|PubMed:31600191}.
CC -!- DISRUPTION PHENOTYPE: Defects in dendritic spine morphogenesis along
CC with thin postsynaptic density and reduced synaptic transmission of
CC pyramidal neurons (PubMed:31600191). Reduced postsynaptic density
CC protein levels of Grin1/Nmdar1, Grin2a/NR2A, Grin2b/NR2B and
CC Gria1/GluR1 (PubMed:31600191). Significantly reduced acetylation of
CC Cttn (PubMed:31600191). Autism-like behaviors including excessive
CC repetitive self-grooming, reduced vocalization time and impaired social
CC interaction (PubMed:31600191). {ECO:0000269|PubMed:31600191}.
CC -!- SIMILARITY: Belongs to the DIP2 family. {ECO:0000305}.
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DR EMBL; AC140851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC141477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK050040; BAC34043.2; -; mRNA.
DR EMBL; AB093213; BAC41397.2; -; mRNA.
DR RefSeq; NP_001074888.2; NM_001081419.2.
DR AlphaFoldDB; Q8BWT5; -.
DR SMR; Q8BWT5; -.
DR STRING; 10090.ENSMUSP00000101057; -.
DR iPTMnet; Q8BWT5; -.
DR PhosphoSitePlus; Q8BWT5; -.
DR MaxQB; Q8BWT5; -.
DR PaxDb; Q8BWT5; -.
DR PeptideAtlas; Q8BWT5; -.
DR PRIDE; Q8BWT5; -.
DR ProteomicsDB; 279414; -.
DR Antibodypedia; 24717; 152 antibodies from 20 providers.
DR Ensembl; ENSMUST00000160048; ENSMUSP00000125184; ENSMUSG00000020231.
DR GeneID; 64451; -.
DR KEGG; mmu:64451; -.
DR CTD; 23181; -.
DR MGI; MGI:2385920; Dip2a.
DR VEuPathDB; HostDB:ENSMUSG00000020231; -.
DR eggNOG; KOG3628; Eukaryota.
DR GeneTree; ENSGT00950000182997; -.
DR HOGENOM; CLU_001345_0_0_1; -.
DR InParanoid; Q8BWT5; -.
DR OrthoDB; 539697at2759; -.
DR BioGRID-ORCS; 64451; 9 hits in 74 CRISPR screens.
DR ChiTaRS; Dip2a; mouse.
DR PRO; PR:Q8BWT5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BWT5; protein.
DR Bgee; ENSMUSG00000020231; Expressed in substantia nigra and 228 other tissues.
DR ExpressionAtlas; Q8BWT5; baseline and differential.
DR Genevisible; Q8BWT5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IDA:FlyBase.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IDA:UniProtKB.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:2000758; P:positive regulation of peptidyl-lysine acetylation; IMP:UniProtKB.
DR CDD; cd05905; Dip2; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.12780; -; 2.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR037337; Dip2-like_dom.
DR InterPro; IPR010506; DMAP1-bd.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF06464; DMAP_binding; 1.
DR SMART; SM01137; DMAP_binding; 1.
DR PROSITE; PS51912; DMAP1_BIND; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Developmental protein; Ligase; Membrane;
KW Mitochondrion; Neurogenesis; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..1523
FT /note="Disco-interacting protein 2 homolog A"
FT /id="PRO_0000079907"
FT DOMAIN 9..105
FT /note="DMAP1-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT REGION 72..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 235..238
FT /note="PXXP motif; required for interaction with CTTN"
FT /evidence="ECO:0000269|PubMed:31600191"
FT MOTIF 259..262
FT /note="PXXP motif; required for interaction with CTTN"
FT /evidence="ECO:0000269|PubMed:31600191"
FT COMPBIAS 83..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14689"
FT MUTAGEN 235..238
FT /note="PKRP->AKRA: Significantly reduced interaction with
FT CTTN; when associated with 259-ANQA-262."
FT /evidence="ECO:0000269|PubMed:31600191"
FT MUTAGEN 259..262
FT /note="PNQP->ANQA: Significantly reduced interaction with
FT CTTN; when associated with 235-AKRA-238."
FT /evidence="ECO:0000269|PubMed:31600191"
FT CONFLICT 42..54
FT /note="RAKLLARYIPLIQ -> SRATNSRDERFRS (in Ref. 3;
FT BAC41397)"
FT /evidence="ECO:0000305"
FT CONFLICT 996
FT /note="H -> R (in Ref. 2; BAC34043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1523 AA; 165255 MW; E5D54BF7E988D065 CRC64;
MADRGCPLEA APLPAEVLES LAELELELSE GDITQKGYEK KRAKLLARYI PLIQDVHTEA
VQAALAKYKE RKMPMPSKRR SALVHSSVET YTPPDTSSAS EDEGSLRRPG RLTSTLLQSH
SGIEPWLDRV IQGSSTSSSA SSTSSHPGGR PAAAPSASTA LAGLTAHAHI DLHSAPPDVT
TGLVEHSSYE RPQMASVRGI PRGHGRNVLE TADGVPVNSR VSSKIQQLLN TLKRPKRPPL
KEFFVDDFEE LLEVQQPDPN QPKPEGDQMA VLKGEPLSVG TNGPLSLLAA LQLWGTTQPK
APCLTALDTA GKATCTLTYG KLWSRSLKLA YTLLNKLTSK NEPLLNPGDR VALVFPNSDP
VMFMVAFYGC LLAELVPVPI EVPLTRKDAG SQQVGFLLGS CGVTLALTTD ACQKGLPKAP
TGEVATFKGW PPLAWLVIDG KHLTRPPKDW YPLAQDTGSR TAYIEYKTSK EGSTVGVTVS
HSSLLAQCQA LTQACGYTEA ETLTNVLDFK RDAGLWHGVL TSVMNRMHVI TIPYALMKVN
PLSWIQKVCS YKARAALVKS RDMHWSLLAQ RGQRDVCLSS LRMLIVADGA NPWSISSCDA
FLNVFQSRGL RPEVICPCAS SPEALTVAIR RPPDLGGPPP RKAVLSMNGL SYGVIRVDTE
EKLSVLTVQD VGQVMPGASV CVVKVDGAPY LCKTDEIGEI CVNSVATGTA YYGLLGITKN
TFETVPVTAD GVPVSDRPFT RTGLLGFIGP DNLVFVVGKL DGLMVVGVRR HNADDIVATA
LAVEPMKFVY RGRIAVFSVT VLHDDRIVLV AEQRPDASEE DSFQWMSRVL QAIDSIHQVG
VYCLALVPAN TLPKAPLGGI HISETKQRFL EGTLHPCNVL MCPHTCVTNL PKPRQKQPEV
GPASMIVGNL VAGKRIAQAS GRELAHLEDS DQARKFLFLA DVLQWRAHTT PDHPLFLLLN
AKGTVTSTAT CIQLHKRAER VAAALMEKGR LDAGDHVALV YPPGVDLIAA FYGCLYCGCV
PVTVRPPHPQ NLGTTLPTVK MIVEVSKSAC VLSTQAITRL LKSKEAAAAV DVRTWPTILD
TDDIPKKKVA SIFRPPSPDV LAYLDFSVST TGILAGVKMS HAATSALCRS IKLQCELYPS
RQIAICLDPY CGLGFALWCL CSVYSGHQSV LVPPLELESN VSLWLSAVSQ YKARVTFCSY
SVMEMCTKGL GAQTGALRMK GVNLSCVRTC MVVAEERPRI SLTQSFSKLF KDLGLPARAV
STTFGCRVNV AICLQGTTGP DPTTVYVDMR ALRHDRVRLV ERGSPHSLPL MESGKILPGV
KVIIAHTETK GPLGDSHLGE IWVSSPHNAT GYYTVYGEET LHADHFSARL SFGDTQTIWA
RTGYLGFLRR TELTDASGER HDALYVVGSL DETLELRGMR YHPIDIETSV IRAHRSIAEC
AVFTWTNLLV VVVELDGLEQ DALDLVALVT NVVLEEHYLV VGVVVIVDPG VIPINSRGEK
QRMHLRDGFL ADQLDPIYVA YNM
