RL21_HUMAN
ID RL21_HUMAN Reviewed; 160 AA.
AC P46778; Q16699;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=60S ribosomal protein L21;
DE AltName: Full=Large ribosomal subunit protein eL21 {ECO:0000303|PubMed:24524803};
GN Name=RPL21;
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 [MRNA].
RC TISSUE=Colon;
RX PubMed=7772601; DOI=10.1016/0167-4781(95)00045-i;
RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10
RT and S29 human ribosomal protein mRNAs.";
RL Biochim. Biophys. Acta 1262:64-68(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7581362; DOI=10.1093/hmg/4.8.1259;
RA Harshman K., Bell R., Rosenthal J., Katcher H., Miki Y., Swenson J.,
RA Gholami Z., Frye C., Ding W., Dayananth P., Eddington K., Norris F.H.,
RA Bristow P.K., Phelps R., Hattier T., Stone S., Shaffer D., Bayer S.,
RA Hussey C., Tran T., Lai M., Rosteck P.R. Jr., Skolnick M.H.,
RA Shattuck-Eidens D., Kamb A.;
RT "Comparison of the positional cloning methods used to isolate the BRCA1
RT gene.";
RL Hum. Mol. Genet. 4:1259-1266(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative analysis of
RT 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lymph, Muscle, Pancreas, Prostate, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-160.
RC TISSUE=Brain;
RX PubMed=7951316; DOI=10.1038/ng0894-472;
RA Albertsen H.M., Smith S.A., Mazoyer S., Fujimoto E., Stevens J.,
RA Williams B., Rodriguez P., Cropp C.S., Slijepcevic P., Carlson M.,
RA Robertson M., Bradley P., Lawrence E., Harrington T., Sheng Z.M.,
RA Hoopes R., Sternberg N., Brothman A., Callahan R., Ponder B.A.J., White R.;
RT "A physical map and candidate genes in the BRCA1 region on chromosome
RT 17q12-21.";
RL Nat. Genet. 7:472-479(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 124-154.
RX PubMed=9582194; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [7]
RP PROTEIN SEQUENCE OF 2-15, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP AND SUBUNIT.
RX PubMed=12962325; DOI=10.1023/a:1025068419698;
RA Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
RA Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of the
RT human large cytoplasmic ribosomal subunit proteins by mass spectrometry and
RT Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [8]
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 [9]
RP INVOLVEMENT IN HYPT12, AND VARIANT HYPT12 GLN-32.
RX PubMed=21412954; DOI=10.1002/humu.21503;
RA Zhou C., Zang D., Jin Y., Wu H., Liu Z., Du J., Zhang J.;
RT "Mutation in ribosomal protein L21 underlies hereditary hypotrichosis
RT simplex.";
RL Hum. Mutat. 32:710-714(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [12]
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 [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [14] {ECO:0007744|PDB:5AJ0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=25957688; DOI=10.1016/j.cell.2015.03.052;
RA Behrmann E., Loerke J., Budkevich T.V., Yamamoto K., Schmidt A.,
RA Penczek P.A., Vos M.R., Burger J., Mielke T., Scheerer P., Spahn C.M.;
RT "Structural snapshots of actively translating human ribosomes.";
RL Cell 161:845-857(2015).
RN [15] {ECO:0007744|PDB:4UG0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=25901680; DOI=10.1038/nature14427;
RA Khatter H., Myasnikov A.G., Natchiar S.K., Klaholz B.P.;
RT "Structure of the human 80S ribosome.";
RL Nature 520:640-645(2015).
RN [16] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:25957688, PubMed:25901680). The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell (PubMed:12962325, PubMed:23636399,
CC PubMed:25957688, PubMed:25901680). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:25901680, ECO:0000269|PubMed:25957688,
CC ECO:0000305|PubMed:12962325}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:25957688, PubMed:25901680).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680,
CC ECO:0000269|PubMed:25957688, ECO:0000305|PubMed:12962325}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25957688}.
CC Cytoplasm {ECO:0000305|PubMed:23636399, ECO:0000305|PubMed:25901680}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P49666}. Note=Detected on
CC cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are
CC associated with the rough endoplasmic reticulum (By similarity).
CC {ECO:0000250|UniProtKB:P49666, ECO:0000269|PubMed:25957688}.
CC -!- DISEASE: Hypotrichosis 12 (HYPT12) [MIM:615885]: A form of
CC hypotrichosis, a condition characterized by the presence of less than
CC the normal amount of hair and abnormal hair follicles and shafts, which
CC are thin and atrophic. The extent of scalp and body hair involvement
CC can be very variable, within as well as between families. HYPT12
CC patients have normal scalp hair density at birth. Hair loss begins
CC during the first 6 months of life and gradually progresses to nearly
CC complete loss of scalp hair. The remaining hairs grow slowly and are
CC thin, sparse, dry, and fragile. Body hair, axillary and pubic hair,
CC eyebrows and eyelashes are also sparse or absent. HYPT12 inheritance is
CC autosomal dominant. {ECO:0000269|PubMed:21412954}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family.
CC {ECO:0000305}.
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DR EMBL; X89401; CAA61582.1; -; mRNA.
DR EMBL; U14967; AAA85655.1; -; mRNA.
DR EMBL; AB061826; BAB79464.1; -; Genomic_DNA.
DR EMBL; BC001603; AAH01603.1; -; mRNA.
DR EMBL; BC007505; AAH07505.1; -; mRNA.
DR EMBL; BC062981; AAH62981.1; -; mRNA.
DR EMBL; BC070184; AAH70184.1; -; mRNA.
DR EMBL; BC070323; AAH70323.1; -; mRNA.
DR EMBL; BC070330; AAH70330.1; -; mRNA.
DR EMBL; U25789; AAA93231.1; -; mRNA.
DR EMBL; L38826; AAA80462.1; -; Genomic_DNA.
DR EMBL; AB007176; BAA25835.1; -; Genomic_DNA.
DR CCDS; CCDS9320.1; -.
DR PIR; S55913; S55913.
DR RefSeq; NP_000973.2; NM_000982.3.
DR PDB; 4UG0; EM; -; LT=1-160.
DR PDB; 4V6X; EM; 5.00 A; CT=1-160.
DR PDB; 5AJ0; EM; 3.50 A; AT=1-160.
DR PDB; 5LKS; EM; 3.60 A; LT=1-160.
DR PDB; 5T2C; EM; 3.60 A; N=1-160.
DR PDB; 6IP5; EM; 3.90 A; 2N=1-160.
DR PDB; 6IP6; EM; 4.50 A; 2N=1-160.
DR PDB; 6IP8; EM; 3.90 A; 2N=1-160.
DR PDB; 6LQM; EM; 3.09 A; c=1-160.
DR PDB; 6LSR; EM; 3.13 A; c=1-160.
DR PDB; 6LSS; EM; 3.23 A; c=1-160.
DR PDB; 6LU8; EM; 3.13 A; c=1-160.
DR PDB; 6OLE; EM; 3.10 A; U=2-158.
DR PDB; 6OLF; EM; 3.90 A; U=2-158.
DR PDB; 6OLG; EM; 3.40 A; AT=2-158.
DR PDB; 6OLI; EM; 3.50 A; U=2-158.
DR PDB; 6OLZ; EM; 3.90 A; AT=2-158.
DR PDB; 6OM0; EM; 3.10 A; U=2-158.
DR PDB; 6OM7; EM; 3.70 A; U=2-158.
DR PDB; 6QZP; EM; 2.90 A; LT=2-160.
DR PDB; 6W6L; EM; 3.84 A; U=1-160.
DR PDB; 6XA1; EM; 2.80 A; LT=2-160.
DR PDB; 6Y0G; EM; 3.20 A; LT=1-160.
DR PDB; 6Y2L; EM; 3.00 A; LT=1-160.
DR PDB; 6Y57; EM; 3.50 A; LT=1-160.
DR PDB; 6Y6X; EM; 2.80 A; LT=2-160.
DR PDB; 6Z6L; EM; 3.00 A; LT=1-160.
DR PDB; 6Z6M; EM; 3.10 A; LT=1-160.
DR PDB; 6Z6N; EM; 2.90 A; LT=1-160.
DR PDB; 6ZM7; EM; 2.70 A; LT=1-160.
DR PDB; 6ZME; EM; 3.00 A; LT=1-160.
DR PDB; 6ZMI; EM; 2.60 A; LT=1-160.
DR PDB; 6ZMO; EM; 3.10 A; LT=1-160.
DR PDB; 7BHP; EM; 3.30 A; LT=1-160.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6W6L; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; P46778; -.
DR SMR; P46778; -.
DR BioGRID; 112064; 291.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P46778; -.
DR IntAct; P46778; 73.
DR MINT; P46778; -.
DR STRING; 9606.ENSP00000346027; -.
DR GlyGen; P46778; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P46778; -.
DR MetOSite; P46778; -.
DR PhosphoSitePlus; P46778; -.
DR SwissPalm; P46778; -.
DR BioMuta; RPL21; -.
DR SWISS-2DPAGE; P46778; -.
DR EPD; P46778; -.
DR jPOST; P46778; -.
DR MassIVE; P46778; -.
DR PaxDb; P46778; -.
DR PeptideAtlas; P46778; -.
DR PRIDE; P46778; -.
DR ProteomicsDB; 55760; -.
DR TopDownProteomics; P46778; -.
DR Antibodypedia; 22643; 80 antibodies from 23 providers.
DR DNASU; 6144; -.
DR Ensembl; ENST00000272274.8; ENSP00000351021.2; ENSG00000122026.11.
DR Ensembl; ENST00000311549.11; ENSP00000346027.4; ENSG00000122026.11.
DR Ensembl; ENST00000319826.8; ENSP00000370574.1; ENSG00000122026.11.
DR Ensembl; ENST00000326092.8; ENSP00000370569.1; ENSG00000122026.11.
DR GeneID; 6144; -.
DR KEGG; hsa:6144; -.
DR MANE-Select; ENST00000311549.11; ENSP00000346027.4; NM_000982.4; NP_000973.2.
DR CTD; 6144; -.
DR DisGeNET; 6144; -.
DR GeneCards; RPL21; -.
DR HGNC; HGNC:10313; RPL21.
DR HPA; ENSG00000122026; Low tissue specificity.
DR MalaCards; RPL21; -.
DR MIM; 603636; gene.
DR MIM; 615885; phenotype.
DR neXtProt; NX_P46778; -.
DR OpenTargets; ENSG00000122026; -.
DR Orphanet; 55654; Hypotrichosis simplex.
DR PharmGKB; PA34683; -.
DR VEuPathDB; HostDB:ENSG00000122026; -.
DR eggNOG; KOG1732; Eukaryota.
DR GeneTree; ENSGT00950000182922; -.
DR InParanoid; P46778; -.
DR OMA; IIYNVTP; -.
DR OrthoDB; 1455026at2759; -.
DR PhylomeDB; P46778; -.
DR TreeFam; TF314640; -.
DR PathwayCommons; P46778; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P46778; -.
DR SIGNOR; P46778; -.
DR BioGRID-ORCS; 6144; 366 hits in 952 CRISPR screens.
DR ChiTaRS; RPL21; human.
DR GeneWiki; RPL21; -.
DR GenomeRNAi; 6144; -.
DR Pharos; P46778; Tbio.
DR PRO; PR:P46778; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P46778; protein.
DR Bgee; ENSG00000122026; Expressed in calcaneal tendon and 113 other tissues.
DR ExpressionAtlas; P46778; baseline and differential.
DR Genevisible; P46778; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR Gene3D; 2.30.30.70; -; 1.
DR InterPro; IPR036948; Ribosomal_L21_sf.
DR InterPro; IPR001147; Ribosomal_L21e.
DR InterPro; IPR018259; Ribosomal_L21e_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR20981; PTHR20981; 1.
DR Pfam; PF01157; Ribosomal_L21e; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR PROSITE; PS01171; RIBOSOMAL_L21E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Disease variant;
KW Endoplasmic reticulum; Hypotrichosis; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12962325"
FT CHAIN 2..160
FT /note="60S ribosomal protein L21"
FT /id="PRO_0000149669"
FT REGION 112..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 15
FT /note="F -> S (in dbSNP:rs17085349)"
FT /id="VAR_034459"
FT VARIANT 32
FT /note="R -> Q (in HYPT12; autosomal dominant;
FT dbSNP:rs587777527)"
FT /evidence="ECO:0000269|PubMed:21412954"
FT /id="VAR_066030"
FT CONFLICT 72
FT /note="V -> A (in Ref. 2; AAA93231)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="K -> E (in Ref. 2; AAA93231)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="S -> N (in Ref. 2; AAA93231)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="N -> D (in Ref. 2; AAA93231)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="K -> E (in Ref. 2; AAA93231)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="K -> Q (in Ref. 2; AAA93231)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="Q -> H (in Ref. 5; AAA80462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 160 AA; 18565 MW; C51D0B5E8EB9D69E CRC64;
MTNTKGKRRG TRYMFSRPFR KHGVVPLATY MRIYKKGDIV DIKGMGTVQK GMPHKCYHGK
TGRVYNVTQH AVGIVVNKQV KGKILAKRIN VRIEHIKHSK SRDSFLKRVK ENDQKKKEAK
EKGTWVQLKR QPAPPREAHF VRTNGKEPEL LEPIPYEFMA
