ID   RM22_HUMAN              Reviewed;         206 AA.
AC   Q9NWU5; A6NGJ8; Q5H9Q1; Q96Q51; Q9P006;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   23-FEB-2022, entry version 154.
DE   RecName: Full=39S ribosomal protein L22, mitochondrial;
DE            Short=L22mt;
DE            Short=MRP-L22;
DE   AltName: Full=39S ribosomal protein L25, mitochondrial;
DE            Short=L25mt;
DE            Short=MRP-L25;
DE   AltName: Full=Mitochondrial large ribosomal subunit protein uL22m {ECO:0000303|PubMed:25278503};
DE   Flags: Precursor;
GN   Name=MRPL22; Synonyms=MRPL25, RPML25; ORFNames=HSPC158;
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).
RC   TISSUE=Umbilical cord blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for 300
RT   previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT   cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Carcinoma;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Retina;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin;
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 170-206.
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 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   [8]
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   [9] {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   [10] {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   -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC       LSU) (PubMed:28892042, PubMed:25278503). Mature mammalian 55S
CC       mitochondrial ribosomes consist of a small (28S) and a large (39S)
CC       subunit. The 28S small subunit contains a 12S ribosomal RNA (12S mt-
CC       rRNA) and 30 different proteins. The 39S large subunit contains a 16S
CC       rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA (mt-
CC       tRNA(Val)), which plays an integral structural role, and 52 different
CC       proteins. {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:28892042}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC       ECO:0000269|PubMed:28892042}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9NWU5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NWU5-2; Sequence=VSP_021745;
CC       Name=3;
CC         IsoId=Q9NWU5-3; Sequence=VSP_044501;
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF29122.1; Type=Frameshift; Evidence={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; AF161507; AAF29122.1; ALT_FRAME; mRNA.
DR   EMBL; AK000601; BAA91282.1; -; mRNA.
DR   EMBL; AK302784; BAG63988.1; -; mRNA.
DR   EMBL; CR933679; CAI45973.1; -; mRNA.
DR   EMBL; AC008410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC008421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC012565; AAH12565.1; -; mRNA.
DR   EMBL; AB051622; BAB54950.1; -; Genomic_DNA.
DR   CCDS; CCDS4331.1; -. [Q9NWU5-1]
DR   CCDS; CCDS43391.1; -. [Q9NWU5-3]
DR   RefSeq; NP_001014990.1; NM_001014990.2. [Q9NWU5-3]
DR   RefSeq; NP_054899.2; NM_014180.3. [Q9NWU5-1]
DR   PDB; 3J7Y; EM; 3.40 A; T=1-206.
DR   PDB; 5OOL; EM; 3.06 A; T=1-206.
DR   PDB; 5OOM; EM; 3.03 A; T=1-206.
DR   PDB; 6NU2; EM; 3.90 A; T=41-206.
DR   PDB; 6NU3; EM; 4.40 A; T=1-206.
DR   PDB; 6ZM5; EM; 2.89 A; T=1-206.
DR   PDB; 6ZM6; EM; 2.59 A; T=1-206.
DR   PDB; 6ZSA; EM; 4.00 A; XT=1-206.
DR   PDB; 6ZSB; EM; 4.50 A; XT=1-206.
DR   PDB; 6ZSC; EM; 3.50 A; XT=1-206.
DR   PDB; 6ZSD; EM; 3.70 A; XT=1-206.
DR   PDB; 6ZSE; EM; 5.00 A; XT=1-206.
DR   PDB; 6ZSG; EM; 4.00 A; XT=1-206.
DR   PDB; 7A5F; EM; 4.40 A; T3=1-206.
DR   PDB; 7A5G; EM; 4.33 A; T3=1-206.
DR   PDB; 7ODR; EM; 2.90 A; T=1-206.
DR   PDB; 7ODS; EM; 3.10 A; T=1-206.
DR   PDB; 7ODT; EM; 3.10 A; T=1-206.
DR   PDB; 7OF0; EM; 2.20 A; T=1-206.
DR   PDB; 7OF2; EM; 2.70 A; T=1-206.
DR   PDB; 7OF3; EM; 2.70 A; T=1-206.
DR   PDB; 7OF4; EM; 2.70 A; T=1-206.
DR   PDB; 7OF5; EM; 2.90 A; T=1-206.
DR   PDB; 7OF6; EM; 2.60 A; T=1-206.
DR   PDB; 7OF7; EM; 2.50 A; T=1-206.
DR   PDB; 7OG4; EM; 3.80 A; XT=1-206.
DR   PDB; 7OI6; EM; 5.70 A; T=1-206.
DR   PDB; 7OI7; EM; 3.50 A; T=1-206.
DR   PDB; 7OI8; EM; 3.50 A; T=1-206.
DR   PDB; 7OI9; EM; 3.30 A; T=1-206.
DR   PDB; 7OIA; EM; 3.20 A; T=1-206.
DR   PDB; 7OIB; EM; 3.30 A; T=1-206.
DR   PDB; 7OIC; EM; 3.10 A; T=1-206.
DR   PDB; 7OID; EM; 3.70 A; T=1-206.
DR   PDB; 7OIE; EM; 3.50 A; T=1-206.
DR   PDBsum; 3J7Y; -.
DR   PDBsum; 5OOL; -.
DR   PDBsum; 5OOM; -.
DR   PDBsum; 6NU2; -.
DR   PDBsum; 6NU3; -.
DR   PDBsum; 6ZM5; -.
DR   PDBsum; 6ZM6; -.
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; 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   SMR; Q9NWU5; -.
DR   BioGRID; 118862; 194.
DR   ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR   CORUM; Q9NWU5; -.
DR   IntAct; Q9NWU5; 38.
DR   MINT; Q9NWU5; -.
DR   STRING; 9606.ENSP00000431040; -.
DR   GlyGen; Q9NWU5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NWU5; -.
DR   MetOSite; Q9NWU5; -.
DR   PhosphoSitePlus; Q9NWU5; -.
DR   SwissPalm; Q9NWU5; -.
DR   BioMuta; MRPL22; -.
DR   DMDM; 74753031; -.
DR   EPD; Q9NWU5; -.
DR   jPOST; Q9NWU5; -.
DR   MassIVE; Q9NWU5; -.
DR   MaxQB; Q9NWU5; -.
DR   PaxDb; Q9NWU5; -.
DR   PeptideAtlas; Q9NWU5; -.
DR   PRIDE; Q9NWU5; -.
DR   ProteomicsDB; 1134; -.
DR   ProteomicsDB; 82983; -. [Q9NWU5-1]
DR   ProteomicsDB; 82984; -. [Q9NWU5-2]
DR   TopDownProteomics; Q9NWU5-1; -. [Q9NWU5-1]
DR   Antibodypedia; 28351; 116 antibodies from 18 providers.
DR   DNASU; 29093; -.
DR   Ensembl; ENST00000265229; ENSP00000265229; ENSG00000082515. [Q9NWU5-3]
DR   Ensembl; ENST00000523037; ENSP00000431040; ENSG00000082515.
DR   GeneID; 29093; -.
DR   KEGG; hsa:29093; -.
DR   MANE-Select; ENST00000523037.6; ENSP00000431040.1; NM_014180.4; NP_054899.2.
DR   UCSC; uc003lvy.5; human. [Q9NWU5-1]
DR   CTD; 29093; -.
DR   GeneCards; MRPL22; -.
DR   HGNC; HGNC:14480; MRPL22.
DR   HPA; ENSG00000082515; Low tissue specificity.
DR   MIM; 611835; gene.
DR   neXtProt; NX_Q9NWU5; -.
DR   OpenTargets; ENSG00000082515; -.
DR   PharmGKB; PA30952; -.
DR   VEuPathDB; HostDB:ENSG00000082515; -.
DR   eggNOG; KOG1711; Eukaryota.
DR   GeneTree; ENSGT00390000002110; -.
DR   HOGENOM; CLU_100005_1_0_1; -.
DR   InParanoid; Q9NWU5; -.
DR   OrthoDB; 1054896at2759; -.
DR   PhylomeDB; Q9NWU5; -.
DR   TreeFam; TF315111; -.
DR   PathwayCommons; Q9NWU5; -.
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; Q9NWU5; -.
DR   SIGNOR; Q9NWU5; -.
DR   BioGRID-ORCS; 29093; 221 hits in 1061 CRISPR screens.
DR   ChiTaRS; MRPL22; human.
DR   GeneWiki; MRPL22; -.
DR   GenomeRNAi; 29093; -.
DR   Pharos; Q9NWU5; Tdark.
DR   PRO; PR:Q9NWU5; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9NWU5; protein.
DR   Bgee; ENSG00000082515; Expressed in heart and 238 other tissues.
DR   ExpressionAtlas; Q9NWU5; baseline and differential.
DR   Genevisible; Q9NWU5; HS.
DR   GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0042255; P:ribosome assembly; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd00336; Ribosomal_L22; 1.
DR   Gene3D; 3.90.470.10; -; 1.
DR   InterPro; IPR001063; Ribosomal_L22.
DR   InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR   InterPro; IPR005727; Ribosomal_L22_bac/chlpt-type.
DR   PANTHER; PTHR13501; PTHR13501; 1.
DR   Pfam; PF00237; Ribosomal_L22; 1.
DR   SUPFAM; SSF54843; SSF54843; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Mitochondrion; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..40
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           41..206
FT                   /note="39S ribosomal protein L22, mitochondrial"
FT                   /id="PRO_0000261644"
FT   VAR_SEQ         1..80
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044501"
FT   VAR_SEQ         2..87
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_021745"
FT   VARIANT         154
FT                   /note="G -> S (in dbSNP:rs3749671)"
FT                   /id="VAR_029471"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   HELIX           47..50
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   STRAND          66..76
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   HELIX           81..87
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   TURN            88..90
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   HELIX           93..100
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   HELIX           106..126
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   STRAND          131..140
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   STRAND          147..150
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   STRAND          154..156
FT                   /evidence="ECO:0007829|PDB:5OOL"
FT   STRAND          160..163
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   STRAND          166..176
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   HELIX           186..199
FT                   /evidence="ECO:0007829|PDB:5OOM"
SQ   SEQUENCE   206 AA;  23641 MW;  EDF999932609F05D CRC64;
     MAAAVLGQLG ALWIHNLRSR GKLALGVLPQ SYIHTSASLD ISRKWEKKNK IVYPPQLPGE
     PRRPAEIYHC RRQIKYSKDK MWYLAKLIRG MSIDQALAQL EFNDKKGAKI IKEVLLEAQD
     MAVRDHNVEF RSNLYIAEST SGRGQCLKRI RYHGRGRFGI MEKVYCHYFV KLVEGPPPPP
     EPPKTAVAHA KEYIQQLRSR TIVHTL
//