PSA1_MOUSE
ID PSA1_MOUSE Reviewed; 263 AA.
AC Q9R1P4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Proteasome subunit alpha type-1;
DE AltName: Full=Macropain subunit C2;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C2;
DE AltName: Full=Proteasome component C2;
DE AltName: Full=Proteasome nu chain;
GN Name=Psma1;
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 STRAIN=B10.A;
RX PubMed=10436176; DOI=10.1007/s002510050562;
RA Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N.,
RA Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J.;
RT "The complete primary structure of mouse 20S proteasomes.";
RL Immunogenetics 49:835-842(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=10873386; DOI=10.1006/geno.2000.6217;
RA Hopitzan A., Himmelbauer H., Spevak W., Castanon M.J.;
RT "The mouse Psma1 gene coding for the alpha-type C2 proteasome subunit:
RT structural and functional analysis, mapping, and colocalization with Pde3b
RT on mouse chromosome 7.";
RL Genomics 66:313-323(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [4]
RP PROTEIN SEQUENCE OF 63-82 AND 97-107, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP FUNCTION.
RX PubMed=12874245; DOI=10.4049/jimmunol.171.3.1515;
RA Qureshi N., Perera P.-Y., Shen J., Zhang G., Lenschat A., Splitter G.,
RA Morrison D.C., Vogel S.N.;
RT "The proteasome as a lipopolysaccharide-binding protein in macrophages:
RT differential effects of proteasome inhibition on lipopolysaccharide-induced
RT signaling events.";
RL J. Immunol. 171:1515-1525(2003).
RN [6]
RP IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7;
RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.;
RT "Mapping the murine cardiac 26S proteasome complexes.";
RL Circ. Res. 99:362-371(2006).
RN [7]
RP FUNCTION.
RX PubMed=16581775; DOI=10.1128/mcb.26.8.2999-3007.2006;
RA Khor B., Bredemeyer A.L., Huang C.-Y., Turnbull I.R., Evans R.,
RA Maggi L.B. Jr., White J.M., Walker L.M., Carnes K., Hess R.A.,
RA Sleckman B.P.;
RT "Proteasome activator PA200 is required for normal spermatogenesis.";
RL Mol. Cell. Biol. 26:2999-3007(2006).
RN [8]
RP INDUCTION.
RX PubMed=16317774; DOI=10.1002/pmic.200500218;
RA Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X.,
RA Zhang X., Yang X.;
RT "The up-regulation of proteasome subunits and lysosomal proteases in
RT hepatocellular carcinomas of the HBx gene knockin transgenic mice.";
RL Proteomics 6:498-504(2006).
RN [9]
RP INDUCTION BY DITHIOLETHIONE.
RX PubMed=17521679; DOI=10.1016/j.lfs.2007.04.014;
RA Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W.;
RT "Tissue specific increase of the catalytic subunits of the 26S proteasome
RT by indirect antioxidant dithiolethione in mice: enhanced activity for
RT degradation of abnormal protein.";
RL Life Sci. 80:2411-2420(2007).
RN [10]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19526544; DOI=10.1002/pmic.200800016;
RA Martinez-Solano L., Reales-Calderon J.A., Nombela C., Molero G., Gil C.;
RT "Proteomics of RAW 264.7 macrophages upon interaction with heat-inactivated
RT Candida albicans cells unravel an anti-inflammatory response.";
RL Proteomics 9:2995-3010(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [12]
RP GLYCOSYLATION AT SER-110.
RC TISSUE=Brain, and Spleen;
RX PubMed=22556278; DOI=10.1074/mcp.m111.015966;
RA Overath T., Kuckelkorn U., Henklein P., Strehl B., Bonar D., Kloss A.,
RA Siele D., Kloetzel P.M., Janek K.;
RT "Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel
RT biotin-cystamine tag.";
RL Mol. Cell. Proteomics 11:467-477(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT,
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22341445; DOI=10.1016/j.cell.2011.12.030;
RA Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M.,
RA Groll M.;
RT "Immuno- and constitutive proteasome crystal structures reveal differences
RT in substrate and inhibitor specificity.";
RL Cell 148:727-738(2012).
CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC proteolytic degradation of most intracellular proteins. This complex
CC plays numerous essential roles within the cell by associating with
CC different regulatory particles. Associated with two 19S regulatory
CC particles, forms the 26S proteasome and thus participates in the ATP-
CC dependent degradation of ubiquitinated proteins. The 26S proteasome
CC plays a key role in the maintenance of protein homeostasis by removing
CC misfolded or damaged proteins that could impair cellular functions, and
CC by removing proteins whose functions are no longer required. Associated
CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC independent protein degradation. This type of proteolysis is required
CC in several pathways including spermatogenesis (20S-PA200 complex) or
CC generation of a subset of MHC class I-presented antigenic peptides
CC (20S-PA28 complex). {ECO:0000269|PubMed:12874245,
CC ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:19526544,
CC ECO:0000269|PubMed:22341445}.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC complex made of 28 subunits that are arranged in four stacked rings.
CC The two outer rings are each formed by seven alpha subunits, and the
CC two inner rings are formed by seven beta subunits. The proteolytic
CC activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7
CC (PubMed:16857966). Interacts with NOTCH3 (By similarity). Interacts
CC with ZFAND1 (By similarity). {ECO:0000250|UniProtKB:P25786,
CC ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}.
CC -!- INTERACTION:
CC Q9R1P4; Q91X58: Zfand2b; NbExp=2; IntAct=EBI-991653, EBI-15701753;
CC Q9R1P4; Q9UM47: NOTCH3; Xeno; NbExp=2; IntAct=EBI-991653, EBI-1236377;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25786}. Nucleus
CC {ECO:0000250|UniProtKB:P25786}. Note=Translocated from the cytoplasm
CC into the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9.
CC {ECO:0000250|UniProtKB:P25786}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:22341445}.
CC -!- INDUCTION: Up-regulated in liver tumor tissues. Up-regulated by the
CC antioxidant dithiolethione (D3T) in liver, lung and colon (at the
CC protein level). {ECO:0000269|PubMed:16317774,
CC ECO:0000269|PubMed:17521679}.
CC -!- PTM: C-terminal extension is partially cleaved off by limited
CC proteolysis leading to a conversion of the proteasome from its latent
CC into its active form.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; AF060088; AAD50533.1; -; mRNA.
DR EMBL; AJ272019; CAB95966.1; -; mRNA.
DR EMBL; AJ272272; CAB95969.1; -; Genomic_DNA.
DR EMBL; BC005762; AAH05762.1; -; mRNA.
DR CCDS; CCDS40094.1; -.
DR RefSeq; NP_036095.1; NM_011965.2.
DR PDB; 3UNB; X-ray; 2.90 A; E/S/g/u=1-263.
DR PDB; 3UNE; X-ray; 3.20 A; E/S/g/u=1-263.
DR PDB; 3UNF; X-ray; 2.90 A; E/S=1-263.
DR PDB; 3UNH; X-ray; 3.20 A; E/S=1-263.
DR PDBsum; 3UNB; -.
DR PDBsum; 3UNE; -.
DR PDBsum; 3UNF; -.
DR PDBsum; 3UNH; -.
DR AlphaFoldDB; Q9R1P4; -.
DR SMR; Q9R1P4; -.
DR BioGRID; 204991; 62.
DR CORUM; Q9R1P4; -.
DR DIP; DIP-35147N; -.
DR IntAct; Q9R1P4; 23.
DR MINT; Q9R1P4; -.
DR STRING; 10090.ENSMUSP00000033008; -.
DR MEROPS; T01.976; -.
DR GlyGen; Q9R1P4; 1 site.
DR iPTMnet; Q9R1P4; -.
DR PhosphoSitePlus; Q9R1P4; -.
DR SwissPalm; Q9R1P4; -.
DR COMPLUYEAST-2DPAGE; Q9R1P4; -.
DR REPRODUCTION-2DPAGE; IPI00283862; -.
DR REPRODUCTION-2DPAGE; Q9R1P4; -.
DR CPTAC; non-CPTAC-3602; -.
DR EPD; Q9R1P4; -.
DR jPOST; Q9R1P4; -.
DR MaxQB; Q9R1P4; -.
DR PaxDb; Q9R1P4; -.
DR PRIDE; Q9R1P4; -.
DR ProteomicsDB; 291689; -.
DR Antibodypedia; 11977; 370 antibodies from 40 providers.
DR DNASU; 26440; -.
DR Ensembl; ENSMUST00000033008; ENSMUSP00000033008; ENSMUSG00000030751.
DR GeneID; 26440; -.
DR KEGG; mmu:26440; -.
DR UCSC; uc009jhy.1; mouse.
DR CTD; 5682; -.
DR MGI; MGI:1347005; Psma1.
DR VEuPathDB; HostDB:ENSMUSG00000030751; -.
DR eggNOG; KOG0863; Eukaryota.
DR GeneTree; ENSGT00550000074855; -.
DR HOGENOM; CLU_035750_8_0_1; -.
DR InParanoid; Q9R1P4; -.
DR OMA; NTQVYGK; -.
DR OrthoDB; 1222564at2759; -.
DR PhylomeDB; Q9R1P4; -.
DR TreeFam; TF106206; -.
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; 26440; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Psma1; mouse.
DR PRO; PR:Q9R1P4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9R1P4; protein.
DR Bgee; ENSMUSG00000030751; Expressed in pharyngeal arch 2 and 285 other tissues.
DR ExpressionAtlas; Q9R1P4; baseline and differential.
DR Genevisible; Q9R1P4; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000502; C:proteasome complex; IDA:MGI.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IMP:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03749; proteasome_alpha_type_1; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR035144; Proteasome_alpha1.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF12; PTHR11599:SF12; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Glycoprotein; Immunity; Isopeptide bond; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome; Ubl conjugation.
FT CHAIN 1..263
FT /note="Proteasome subunit alpha type-1"
FT /id="PRO_0000124062"
FT REGION 232..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P18420"
FT MOD_RES 110
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25786"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 110
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000269|PubMed:22556278"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P25786"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P25786"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 78..98
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:3UNB"
SQ SEQUENCE 263 AA; 29547 MW; CC791C56AFBA8043 CRC64;
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ
KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD RPLPVSRLVS LIGSKTQIPT
QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS ANYFDCRAMS IGARSQSART YLERHMSEFM
ECNLDELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLDGLEERP
QRKAQPSQAA EEPAEKADEP MEH
