PSD10_MOUSE
ID PSD10_MOUSE Reviewed; 231 AA.
AC Q9Z2X2; Q8R0G2; Q9D383; Q9D7N8;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 10;
DE AltName: Full=26S proteasome regulatory subunit p28;
DE AltName: Full=Gankyrin;
GN Name=Psmd10;
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].
RC TISSUE=Placenta;
RA Higashitsuji H., Fujita J.;
RT "Cloning of mouse gankyrin containing ankyrin repeats.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Medulla oblongata, and Tongue;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Mammary tumor;
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=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC 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 FUNCTION IN AKT ACTIVATION, AND INDUCTION BY HRAS.
RX PubMed=20628200; DOI=10.1172/jci42542;
RA Man J.H., Liang B., Gu Y.X., Zhou T., Li A.L., Li T., Jin B.F., Bai B.,
RA Zhang H.Y., Zhang W.N., Li W.H., Gong W.L., Li H.Y., Zhang X.M.;
RT "Gankyrin plays an essential role in Ras-induced tumorigenesis through
RT regulation of the RhoA/ROCK pathway in mammalian cells.";
RL J. Clin. Invest. 120:2829-2841(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HUMAN AND RAT PSMC4,
RP AND DOMAINS ANKYRIN REPEATS.
RX PubMed=17292836; DOI=10.1016/j.str.2006.11.015;
RA Nakamura Y., Nakano K., Umehara T., Kimura M., Hayashizaki Y., Tanaka A.,
RA Horikoshi M., Padmanabhan B., Yokoyama S.;
RT "Structure of the oncoprotein gankyrin in complex with S6 ATPase of the 26S
RT proteasome.";
RL Structure 15:179-189(2007).
CC -!- FUNCTION: Acts as a chaperone during the assembly of the 26S
CC proteasome, specifically of the PA700/19S regulatory complex (RC). In
CC the initial step of the base subcomplex assembly is part of an
CC intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles
CC with a PSMD5:PSMC2:PSMC1:PSMD2 module (By similarity). Independently of
CC the proteasome, regulates EGF-induced AKT activation through inhibition
CC of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation.
CC Plays an important role in RAS-induced tumorigenesis. {ECO:0000250,
CC ECO:0000269|PubMed:20628200}.
CC -!- FUNCTION: Acts as an oncoprotein by being involved in negative
CC regulation of tumor suppressors RB1 and p53/TP53. Overexpression is
CC leading to phosphorylation of RB1 and proteasomal degradation of RB1.
CC Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A
CC for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the
CC mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function
CC in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in
CC p53-independent apoptosis. Involved in regulation of NF-kappa-B by
CC retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA
CC and accelerates its XPO1/CRM1-mediated nuclear export (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Part of transient complex containing PSMD10, PSMC4, PSMC5 and
CC PAAF1 formed during the assembly of the 26S proteasome. Stays
CC associated throughout the assembly of the PA700/19S RC and is released
CC upon association with the 20S core. Interacts with PSMC4. Interacts
CC with RB1. Interacts with CDK4. Interacts with MDM2. Interacts with
CC RELA. Associates with a CDK4:CCND2 serine/threonine kinase complex (By
CC similarity). Interacts with ARHGDIA and increases the interaction
CC between ARHGDIA and RHOA, hence promotes ARHGDIA inactivation of RHOA
CC and ROCK (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Z2X2; P43686: PSMC4; Xeno; NbExp=4; IntAct=EBI-8377084, EBI-743997;
CC Q9Z2X2; P06400: RB1; Xeno; NbExp=3; IntAct=EBI-8377084, EBI-491274;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by activated HRAS.
CC {ECO:0000269|PubMed:20628200}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB31128.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB022022; BAA36969.1; -; mRNA.
DR EMBL; AK009068; BAB26053.1; -; mRNA.
DR EMBL; AK018233; BAB31128.1; ALT_FRAME; mRNA.
DR EMBL; AK136400; BAE22964.1; -; mRNA.
DR EMBL; AL672306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466616; EDL23939.1; -; Genomic_DNA.
DR EMBL; BC026931; AAH26931.1; -; mRNA.
DR EMBL; BC056196; AAH56196.1; -; mRNA.
DR CCDS; CCDS30444.1; -.
DR RefSeq; NP_001157649.1; NM_001164177.1.
DR RefSeq; NP_058579.2; NM_016883.4.
DR PDB; 2DVW; X-ray; 2.30 A; A=1-231.
DR PDB; 2DWZ; X-ray; 2.40 A; A/C=1-231.
DR PDB; 3AJI; X-ray; 2.05 A; A/C=1-231.
DR PDBsum; 2DVW; -.
DR PDBsum; 2DWZ; -.
DR PDBsum; 3AJI; -.
DR AlphaFoldDB; Q9Z2X2; -.
DR SMR; Q9Z2X2; -.
DR BioGRID; 207302; 9.
DR DIP; DIP-29273N; -.
DR IntAct; Q9Z2X2; 3.
DR MINT; Q9Z2X2; -.
DR STRING; 10090.ENSMUSP00000033805; -.
DR iPTMnet; Q9Z2X2; -.
DR PhosphoSitePlus; Q9Z2X2; -.
DR REPRODUCTION-2DPAGE; Q9Z2X2; -.
DR EPD; Q9Z2X2; -.
DR MaxQB; Q9Z2X2; -.
DR PaxDb; Q9Z2X2; -.
DR PeptideAtlas; Q9Z2X2; -.
DR PRIDE; Q9Z2X2; -.
DR ProteomicsDB; 291829; -.
DR Antibodypedia; 496; 433 antibodies from 33 providers.
DR DNASU; 53380; -.
DR Ensembl; ENSMUST00000033805; ENSMUSP00000033805; ENSMUSG00000031429.
DR GeneID; 53380; -.
DR KEGG; mmu:53380; -.
DR UCSC; uc009ulj.2; mouse.
DR CTD; 5716; -.
DR MGI; MGI:1858898; Psmd10.
DR VEuPathDB; HostDB:ENSMUSG00000031429; -.
DR eggNOG; KOG4412; Eukaryota.
DR GeneTree; ENSGT00940000153404; -.
DR InParanoid; Q9Z2X2; -.
DR OMA; WAVAYNR; -.
DR OrthoDB; 1514637at2759; -.
DR PhylomeDB; Q9Z2X2; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 53380; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Psmd10; mouse.
DR EvolutionaryTrace; Q9Z2X2; -.
DR PRO; PR:Q9Z2X2; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9Z2X2; protein.
DR Bgee; ENSMUSG00000031429; Expressed in primary oocyte and 64 other tissues.
DR ExpressionAtlas; Q9Z2X2; baseline and differential.
DR Genevisible; Q9Z2X2; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR IDEAL; IID50037; -.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR039334; PSMD10-like.
DR PANTHER; PTHR24126:SF24; PTHR24126:SF24; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Apoptosis; Chaperone; Cytoplasm; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..231
FT /note="26S proteasome non-ATPase regulatory subunit 10"
FT /id="PRO_0000067046"
FT REPEAT 3..36
FT /note="ANK 1"
FT REPEAT 37..69
FT /note="ANK 2"
FT REPEAT 70..102
FT /note="ANK 3"
FT REPEAT 103..135
FT /note="ANK 4"
FT REPEAT 136..168
FT /note="ANK 5"
FT REPEAT 169..201
FT /note="ANK 6"
FT REPEAT 202..226
FT /note="ANK 7"
FT CONFLICT 101
FT /note="A -> S (in Ref. 1; BAA36969)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="A -> S (in Ref. 1; BAA36969)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="S -> G (in Ref. 2; BAB26053)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:3AJI"
FT HELIX 214..229
FT /evidence="ECO:0007829|PDB:3AJI"
SQ SEQUENCE 231 AA; 25084 MW; BCE7B9A79C91358B CRC64;
MEGCVSNIMI CNLAYSGKLD ELKERILADK SLATRTDQDS RTALHWACSA GHTEIVEFLL
QLGVPVNDKD DAGWSPLHIA ASAGRDEIVK ALLVKGAHVN AVNQNGCTPL HYAASKNRHE
IAVMLLEGGA NPDAKDHYDA TAMHRAAAKG NLKMVHILLF YKASTNIQDT EGNTPLHLAC
DEERVEEAKF LVTQGASIYI ENKEEKTPLQ VAKGGLGLIL KRLAESEEAS M
