RT16_HUMAN
ID RT16_HUMAN Reviewed; 137 AA.
AC Q9Y3D3; B4E032; Q96Q60;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=28S ribosomal protein S16, mitochondrial;
DE Short=MRP-S16;
DE Short=S16mt;
DE AltName: Full=Mitochondrial small ribosomal subunit protein bS16m {ECO:0000303|PubMed:25838379};
DE Flags: Precursor;
GN Name=MRPS16; Synonyms=RPMS16; ORFNames=CGI-132;
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] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11402041; DOI=10.1074/jbc.m103236200;
RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA Watanabe K.;
RT "Proteomic analysis of the mammalian mitochondrial ribosome. Identification
RT of protein components in the 28S small subunit.";
RL J. Biol. Chem. 276:33181-33195(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-35.
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 [7]
RP IDENTIFICATION.
RX PubMed=11279123; DOI=10.1074/jbc.m100727200;
RA Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.;
RT "The small subunit of the mammalian mitochondrial ribosome: identification
RT of the full complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:19363-19374(2001).
RN [8]
RP INVOLVEMENT IN COXPD2.
RX PubMed=15505824; DOI=10.1002/ana.20282;
RA Miller C., Saada A., Shaul N., Shabtai N., Ben-Shalom E., Shaag A.,
RA Hershkovitz E., Elpeleg O.;
RT "Defective mitochondrial translation caused by a ribosomal protein (MRPS16)
RT mutation.";
RL Ann. Neurol. 56:734-738(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
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 [15] {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).
CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt-
CC SSU). 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. bS16m has a zinc binding site.
CC {ECO:0000269|PubMed:25838379}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y3D3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3D3-2; Sequence=VSP_056498;
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 2 (COXPD2)
CC [MIM:610498]: A mitochondrial disease resulting in fatal neonatal
CC metabolic acidosis with agenesis of the corpus callosum.
CC {ECO:0000269|PubMed:15505824}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family.
CC {ECO:0000305}.
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DR EMBL; AF151890; AAD34127.1; -; mRNA.
DR EMBL; AB049948; BAB41001.1; -; mRNA.
DR EMBL; AK303204; BAG64294.1; -; mRNA.
DR EMBL; AC016394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021106; AAH21106.1; -; mRNA.
DR EMBL; AB051351; BAB54941.1; -; Genomic_DNA.
DR CCDS; CCDS7323.1; -. [Q9Y3D3-1]
DR RefSeq; NP_057149.1; NM_016065.3. [Q9Y3D3-1]
DR PDB; 3J9M; EM; 3.50 A; AM=1-137.
DR PDB; 6NU2; EM; 3.90 A; AM=10-125.
DR PDB; 6NU3; EM; 4.40 A; AM=1-137.
DR PDB; 6RW4; EM; 2.97 A; M=1-137.
DR PDB; 6RW5; EM; 3.14 A; M=1-137.
DR PDB; 6VLZ; EM; 2.97 A; AM=1-137.
DR PDB; 6VMI; EM; 2.96 A; AM=1-137.
DR PDB; 6ZM5; EM; 2.89 A; AM=1-137.
DR PDB; 6ZM6; EM; 2.59 A; AM=1-137.
DR PDB; 6ZS9; EM; 4.00 A; AM=1-137.
DR PDB; 6ZSA; EM; 4.00 A; AM=1-136.
DR PDB; 6ZSB; EM; 4.50 A; AM=1-137.
DR PDB; 6ZSC; EM; 3.50 A; AM=1-137.
DR PDB; 6ZSD; EM; 3.70 A; AM=1-137.
DR PDB; 6ZSE; EM; 5.00 A; AM=1-137.
DR PDB; 6ZSG; EM; 4.00 A; AM=1-137.
DR PDB; 7A5F; EM; 4.40 A; M6=1-137.
DR PDB; 7A5G; EM; 4.33 A; M6=1-137.
DR PDB; 7A5I; EM; 3.70 A; M6=1-137.
DR PDB; 7A5K; EM; 3.70 A; M6=1-137.
DR PDB; 7L08; EM; 3.49 A; AM=1-137.
DR PDB; 7OG4; EM; 3.80 A; AM=1-137.
DR PDBsum; 3J9M; -.
DR PDBsum; 6NU2; -.
DR PDBsum; 6NU3; -.
DR PDBsum; 6RW4; -.
DR PDBsum; 6RW5; -.
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; 7A5I; -.
DR PDBsum; 7A5K; -.
DR PDBsum; 7L08; -.
DR PDBsum; 7OG4; -.
DR AlphaFoldDB; Q9Y3D3; -.
DR SMR; Q9Y3D3; -.
DR BioGRID; 119227; 180.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; Q9Y3D3; -.
DR IntAct; Q9Y3D3; 39.
DR MINT; Q9Y3D3; -.
DR STRING; 9606.ENSP00000362036; -.
DR GlyGen; Q9Y3D3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3D3; -.
DR PhosphoSitePlus; Q9Y3D3; -.
DR SwissPalm; Q9Y3D3; -.
DR BioMuta; MRPS16; -.
DR EPD; Q9Y3D3; -.
DR jPOST; Q9Y3D3; -.
DR MassIVE; Q9Y3D3; -.
DR MaxQB; Q9Y3D3; -.
DR PaxDb; Q9Y3D3; -.
DR PeptideAtlas; Q9Y3D3; -.
DR PRIDE; Q9Y3D3; -.
DR ProteomicsDB; 5646; -.
DR ProteomicsDB; 86020; -. [Q9Y3D3-1]
DR Antibodypedia; 45368; 127 antibodies from 23 providers.
DR DNASU; 51021; -.
DR Ensembl; ENST00000372945.8; ENSP00000362036.3; ENSG00000182180.14. [Q9Y3D3-1]
DR GeneID; 51021; -.
DR KEGG; hsa:51021; -.
DR MANE-Select; ENST00000372945.8; ENSP00000362036.3; NM_016065.4; NP_057149.1.
DR UCSC; uc001jts.1; human. [Q9Y3D3-1]
DR CTD; 51021; -.
DR DisGeNET; 51021; -.
DR GeneCards; MRPS16; -.
DR HGNC; HGNC:14048; MRPS16.
DR HPA; ENSG00000182180; Low tissue specificity.
DR MalaCards; MRPS16; -.
DR MIM; 609204; gene.
DR MIM; 610498; phenotype.
DR neXtProt; NX_Q9Y3D3; -.
DR OpenTargets; ENSG00000182180; -.
DR Orphanet; 254920; Combined oxidative phosphorylation defect type 2.
DR PharmGKB; PA31000; -.
DR VEuPathDB; HostDB:ENSG00000182180; -.
DR eggNOG; KOG3419; Eukaryota.
DR GeneTree; ENSGT00390000014309; -.
DR HOGENOM; CLU_100590_4_0_1; -.
DR InParanoid; Q9Y3D3; -.
DR OMA; HMSEPAA; -.
DR OrthoDB; 1630052at2759; -.
DR PhylomeDB; Q9Y3D3; -.
DR TreeFam; TF105637; -.
DR PathwayCommons; Q9Y3D3; -.
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; Q9Y3D3; -.
DR SIGNOR; Q9Y3D3; -.
DR BioGRID-ORCS; 51021; 436 hits in 1093 CRISPR screens.
DR ChiTaRS; MRPS16; human.
DR GeneWiki; MRPS16; -.
DR GenomeRNAi; 51021; -.
DR Pharos; Q9Y3D3; Tbio.
DR PRO; PR:Q9Y3D3; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9Y3D3; protein.
DR Bgee; ENSG00000182180; Expressed in mucosa of transverse colon and 188 other tissues.
DR ExpressionAtlas; Q9Y3D3; baseline and differential.
DR Genevisible; Q9Y3D3; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 3.30.1320.10; -; 1.
DR HAMAP; MF_00385; Ribosomal_S16; 1.
DR InterPro; IPR000307; Ribosomal_S16.
DR InterPro; IPR023803; Ribosomal_S16_dom_sf.
DR PANTHER; PTHR12919; PTHR12919; 1.
DR Pfam; PF00886; Ribosomal_S16; 1.
DR SUPFAM; SSF54565; SSF54565; 1.
DR TIGRFAMs; TIGR00002; S16; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Mitochondrion; Phosphoprotein;
KW Primary mitochondrial disease; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..137
FT /note="28S ribosomal protein S16, mitochondrial"
FT /id="PRO_0000030618"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT VAR_SEQ 93..137
FT /note="LAGFFPLHPMMITNAERLRRKRAREVLLASQKTDAEATDTEATET -> KTD
FT ARFPEQGEERPEQHHFPEDLAPARGRGL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056498"
FT VARIANT 12
FT /note="Y -> H (in dbSNP:rs7905009)"
FT /id="VAR_031525"
SQ SEQUENCE 137 AA; 15345 MW; C12B14B1B357F8D6 CRC64;
MVHLTTLLCK AYRGGHLTIR LALGGCTNRP FYRIVAAHNK CPRDGRFVEQ LGSYDPLPNS
HGEKLVALNL DRIRHWIGCG AHLSKPMEKL LGLAGFFPLH PMMITNAERL RRKRAREVLL
ASQKTDAEAT DTEATET
