RM41_HUMAN
ID RM41_HUMAN Reviewed; 137 AA.
AC Q8IXM3; Q96Q49;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=39S ribosomal protein L41, mitochondrial;
DE Short=L41mt;
DE Short=MRP-L41;
DE AltName: Full=39S ribosomal protein L27 homolog;
DE AltName: Full=Bcl-2-interacting mitochondrial ribosomal protein L41;
DE AltName: Full=Cell proliferation-inducing gene 3 protein;
DE AltName: Full=MRP-L27 homolog;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL41 {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL41; Synonyms=BMRP, MRPL27, RPML27; ORFNames=PIG3;
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 [LARGE SCALE MRNA].
RA Kim J.W.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-135.
RX PubMed=11543634; DOI=10.1006/geno.2001.6622;
RA Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S.,
RA Watanabe K., Tanaka T.;
RT "The human mitochondrial ribosomal protein genes: mapping of 54 genes to
RT the chromosomes and implications for human disorders.";
RL Genomics 77:65-70(2001).
RN [5]
RP IDENTIFICATION.
RX PubMed=11551941; DOI=10.1074/jbc.m106510200;
RA Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M.,
RA Moseley A., Spremulli L.L.;
RT "The large subunit of the mammalian mitochondrial ribosome. Analysis of the
RT complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:43958-43969(2001).
RN [6]
RP INTERACTION WITH BCL2, AND TISSUE SPECIFICITY.
RX PubMed=15547950; DOI=10.1002/jcb.20292;
RA Chintharlapalli S.R., Jasti M., Malladi S., Parsa K.V.L., Ballestero R.P.,
RA Gonzalez-Garcia M.;
RT "BMRP is a Bcl-2 binding protein that induces apoptosis.";
RL J. Cell. Biochem. 94:611-626(2005).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16024796; DOI=10.1128/mcb.25.15.6603-6616.2005;
RA Yoo Y.A., Kim M.J., Park J.K., Chung Y.M., Lee J.H., Chi S.-G., Kim J.S.,
RA Yoo Y.D.;
RT "Mitochondrial ribosomal protein L41 suppresses cell growth in association
RT with p53 and p27Kip1.";
RL Mol. Cell. Biol. 25:6603-6616(2005).
RN [8]
RP FUNCTION.
RX PubMed=16256947; DOI=10.1016/j.bbrc.2005.10.064;
RA Kim M.J., Yoo Y.A., Kim H.J., Kang S., Kim Y.G., Kim J.S., Yoo Y.D.;
RT "Mitochondrial ribosomal protein L41 mediates serum starvation-induced
RT cell-cycle arrest through an increase of p21(WAF1/CIP1).";
RL Biochem. Biophys. Res. Commun. 338:1179-1184(2005).
RN [9]
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 [10]
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 [11] {ECO:0007744|PDB:3J7Y}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25278503; DOI=10.1126/science.1258026;
RA Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C., Murshudov G.,
RA Scheres S.H., Ramakrishnan V.;
RT "Structure of the large ribosomal subunit from human mitochondria.";
RL Science 346:718-722(2014).
RN [12] {ECO:0007744|PDB:3J9M}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25838379; DOI=10.1126/science.aaa1193;
RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.;
RT "Ribosome. The structure of the human mitochondrial ribosome.";
RL Science 348:95-98(2015).
RN [13] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=28892042; DOI=10.1038/nsmb.3464;
RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J.,
RA Amunts A., Ramakrishnan V.;
RT "Structures of the human mitochondrial ribosome in native states of
RT assembly.";
RL Nat. Struct. Mol. Biol. 24:866-869(2017).
CC -!- FUNCTION: Component of the mitochondrial ribosome large subunit
CC (PubMed:28892042, PubMed:25838379, PubMed:25278503). Also involved in
CC apoptosis and cell cycle (PubMed:16024796, PubMed:16256947). Enhances
CC p53/TP53 stability, thereby contributing to p53/TP53-induced apoptosis
CC in response to growth-inhibitory condition. Enhances p53/TP53
CC translocation to the mitochondria. Has the ability to arrest the cell
CC cycle at the G1 phase, possibly by stabilizing the CDKN1A and CDKN1B
CC (p27Kip1) proteins (PubMed:16024796). {ECO:0000269|PubMed:16024796,
CC ECO:0000269|PubMed:16256947, ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC LSU). Mature mammalian 55S mitochondrial ribosomes consist of a small
CC (28S) and a large (39S) subunit. The 28S small subunit contains a 12S
CC ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large
CC subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial
CC valine transfer RNA (mt-tRNA(Val)), which plays an integral structural
CC role, and 52 different proteins (PubMed:11551941, PubMed:25278503,
CC PubMed:25838379). Interacts with BCL2 (PubMed:15547950).
CC {ECO:0000269|PubMed:15547950, ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000305|PubMed:11551941}.
CC -!- INTERACTION:
CC Q8IXM3; Q6PL24: TMED8; NbExp=3; IntAct=EBI-912501, EBI-11603430;
CC Q8IXM3; Q969Q1: TRIM63; NbExp=2; IntAct=EBI-912501, EBI-5661333;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16024796,
CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC ECO:0000269|PubMed:28892042}.
CC -!- TISSUE SPECIFICITY: Present in kidney, liver, thymus and testis, and at
CC lower level in brain and spleen (at protein level).
CC {ECO:0000269|PubMed:15547950}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL41 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; AY232291; AAP69986.1; -; mRNA.
DR EMBL; AL365502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040035; AAH40035.1; -; mRNA.
DR EMBL; AB051625; BAB54952.1; -; Genomic_DNA.
DR CCDS; CCDS7046.1; -.
DR RefSeq; NP_115866.1; NM_032477.2.
DR PDB; 3J7Y; EM; 3.40 A; 9=1-137.
DR PDB; 3J9M; EM; 3.50 A; 9=1-137.
DR PDB; 5OOL; EM; 3.06 A; 9=1-137.
DR PDB; 5OOM; EM; 3.03 A; 9=1-137.
DR PDB; 6I9R; EM; 3.90 A; 9=1-137.
DR PDB; 6NU2; EM; 3.90 A; 9=15-137.
DR PDB; 6NU3; EM; 4.40 A; 9=1-137.
DR PDB; 6VLZ; EM; 2.97 A; 9=1-137.
DR PDB; 6VMI; EM; 2.96 A; 9=1-137.
DR PDB; 6ZM5; EM; 2.89 A; 9=1-137.
DR PDB; 6ZM6; EM; 2.59 A; 9=1-137.
DR PDB; 6ZS9; EM; 4.00 A; 9=1-137.
DR PDB; 6ZSA; EM; 4.00 A; 9=1-137.
DR PDB; 6ZSB; EM; 4.50 A; 9=1-137.
DR PDB; 6ZSC; EM; 3.50 A; 9=1-137.
DR PDB; 6ZSD; EM; 3.70 A; 9=1-137.
DR PDB; 6ZSE; EM; 5.00 A; 9=1-137.
DR PDB; 6ZSG; EM; 4.00 A; 9=1-137.
DR PDB; 7A5F; EM; 4.40 A; 93=1-137.
DR PDB; 7A5G; EM; 4.33 A; 93=1-137.
DR PDB; 7A5H; EM; 3.30 A; 9=1-137.
DR PDB; 7A5I; EM; 3.70 A; 93=1-137.
DR PDB; 7A5J; EM; 3.10 A; 9=1-137.
DR PDB; 7A5K; EM; 3.70 A; 93=1-137.
DR PDB; 7L08; EM; 3.49 A; 9=1-137.
DR PDB; 7L20; EM; 3.15 A; 9=1-137.
DR PDB; 7O9K; EM; 3.10 A; 9=1-137.
DR PDB; 7O9M; EM; 2.50 A; 9=1-137.
DR PDB; 7ODR; EM; 2.90 A; 9=1-137.
DR PDB; 7ODS; EM; 3.10 A; 9=1-137.
DR PDB; 7ODT; EM; 3.10 A; 9=1-137.
DR PDB; 7OF0; EM; 2.20 A; 9=1-137.
DR PDB; 7OF2; EM; 2.70 A; 9=1-137.
DR PDB; 7OF3; EM; 2.70 A; 9=1-137.
DR PDB; 7OF4; EM; 2.70 A; 9=1-137.
DR PDB; 7OF5; EM; 2.90 A; 9=1-137.
DR PDB; 7OF6; EM; 2.60 A; 9=1-137.
DR PDB; 7OF7; EM; 2.50 A; 9=1-137.
DR PDB; 7OG4; EM; 3.80 A; 9=1-137.
DR PDB; 7OI6; EM; 5.70 A; 9=1-137.
DR PDB; 7OI7; EM; 3.50 A; 9=1-137.
DR PDB; 7OI8; EM; 3.50 A; 9=1-137.
DR PDB; 7OI9; EM; 3.30 A; 9=1-137.
DR PDB; 7OIA; EM; 3.20 A; 9=1-137.
DR PDB; 7OIB; EM; 3.30 A; 9=1-137.
DR PDB; 7OIC; EM; 3.10 A; 9=1-137.
DR PDB; 7OID; EM; 3.70 A; 9=1-137.
DR PDB; 7OIE; EM; 3.50 A; 9=1-137.
DR PDB; 7PD3; EM; 3.40 A; 9=1-137.
DR PDB; 7QH6; EM; 3.08 A; 9=1-137.
DR PDBsum; 3J7Y; -.
DR PDBsum; 3J9M; -.
DR PDBsum; 5OOL; -.
DR PDBsum; 5OOM; -.
DR PDBsum; 6I9R; -.
DR PDBsum; 6NU2; -.
DR PDBsum; 6NU3; -.
DR PDBsum; 6VLZ; -.
DR PDBsum; 6VMI; -.
DR PDBsum; 6ZM5; -.
DR PDBsum; 6ZM6; -.
DR PDBsum; 6ZS9; -.
DR PDBsum; 6ZSA; -.
DR PDBsum; 6ZSB; -.
DR PDBsum; 6ZSC; -.
DR PDBsum; 6ZSD; -.
DR PDBsum; 6ZSE; -.
DR PDBsum; 6ZSG; -.
DR PDBsum; 7A5F; -.
DR PDBsum; 7A5G; -.
DR PDBsum; 7A5H; -.
DR PDBsum; 7A5I; -.
DR PDBsum; 7A5J; -.
DR PDBsum; 7A5K; -.
DR PDBsum; 7L08; -.
DR PDBsum; 7L20; -.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7ODR; -.
DR PDBsum; 7ODS; -.
DR PDBsum; 7ODT; -.
DR PDBsum; 7OF0; -.
DR PDBsum; 7OF2; -.
DR PDBsum; 7OF3; -.
DR PDBsum; 7OF4; -.
DR PDBsum; 7OF5; -.
DR PDBsum; 7OF6; -.
DR PDBsum; 7OF7; -.
DR PDBsum; 7OG4; -.
DR PDBsum; 7OI6; -.
DR PDBsum; 7OI7; -.
DR PDBsum; 7OI8; -.
DR PDBsum; 7OI9; -.
DR PDBsum; 7OIA; -.
DR PDBsum; 7OIB; -.
DR PDBsum; 7OIC; -.
DR PDBsum; 7OID; -.
DR PDBsum; 7OIE; -.
DR PDBsum; 7PD3; -.
DR PDBsum; 7QH6; -.
DR AlphaFoldDB; Q8IXM3; -.
DR SMR; Q8IXM3; -.
DR BioGRID; 122363; 200.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q8IXM3; -.
DR IntAct; Q8IXM3; 82.
DR MINT; Q8IXM3; -.
DR STRING; 9606.ENSP00000360498; -.
DR iPTMnet; Q8IXM3; -.
DR PhosphoSitePlus; Q8IXM3; -.
DR BioMuta; MRPL41; -.
DR DMDM; 74750734; -.
DR EPD; Q8IXM3; -.
DR jPOST; Q8IXM3; -.
DR MassIVE; Q8IXM3; -.
DR MaxQB; Q8IXM3; -.
DR PaxDb; Q8IXM3; -.
DR PeptideAtlas; Q8IXM3; -.
DR PRIDE; Q8IXM3; -.
DR ProteomicsDB; 71029; -.
DR TopDownProteomics; Q8IXM3; -.
DR Antibodypedia; 19072; 161 antibodies from 23 providers.
DR DNASU; 64975; -.
DR Ensembl; ENST00000371443.6; ENSP00000360498.5; ENSG00000182154.8.
DR GeneID; 64975; -.
DR KEGG; hsa:64975; -.
DR MANE-Select; ENST00000371443.6; ENSP00000360498.5; NM_032477.3; NP_115866.1.
DR UCSC; uc004cnh.5; human.
DR CTD; 64975; -.
DR DisGeNET; 64975; -.
DR GeneCards; MRPL41; -.
DR HGNC; HGNC:14492; MRPL41.
DR HPA; ENSG00000182154; Tissue enhanced (brain, skeletal muscle).
DR MIM; 611846; gene.
DR neXtProt; NX_Q8IXM3; -.
DR OpenTargets; ENSG00000182154; -.
DR PharmGKB; PA30973; -.
DR VEuPathDB; HostDB:ENSG00000182154; -.
DR eggNOG; KOG4756; Eukaryota.
DR GeneTree; ENSGT00390000013158; -.
DR HOGENOM; CLU_155983_0_0_1; -.
DR InParanoid; Q8IXM3; -.
DR OMA; RSHNKGR; -.
DR OrthoDB; 1294210at2759; -.
DR PhylomeDB; Q8IXM3; -.
DR TreeFam; TF325007; -.
DR PathwayCommons; Q8IXM3; -.
DR Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR SignaLink; Q8IXM3; -.
DR SIGNOR; Q8IXM3; -.
DR BioGRID-ORCS; 64975; 516 hits in 1088 CRISPR screens.
DR ChiTaRS; MRPL41; human.
DR GeneWiki; Mitochondrial_ribosomal_protein_L41; -.
DR GenomeRNAi; 64975; -.
DR Pharos; Q8IXM3; Tbio.
DR PRO; PR:Q8IXM3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8IXM3; protein.
DR Bgee; ENSG00000182154; Expressed in apex of heart and 180 other tissues.
DR Genevisible; Q8IXM3; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; IDA:UniProtKB.
DR InterPro; IPR019189; Ribosomal_L27/L41_mit.
DR PANTHER; PTHR21338; PTHR21338; 1.
DR Pfam; PF09809; MRP-L27; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cell cycle; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 14..137
FT /note="39S ribosomal protein L41, mitochondrial"
FT /id="PRO_0000273228"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5OOM"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:3J7Y"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 137 AA; 15383 MW; 25A9F3105ABF1189 CRC64;
MGVLAAAARC LVRGADRMSK WTSKRGPRSF RGRKGRGAKG IGFLTSGWRF VQIKEMVPEF
VVPDLTGFKL KPYVSYLAPE SEETPLTAAQ LFSEAVAPAI EKDFKDGTFD PDNLEKYGFE
PTQEGKLFQL YPRNFLR
