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RM13_HUMAN
ID   RM13_HUMAN              Reviewed;         178 AA.
AC   Q9BYD1; B2R4R8; Q9UI04;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 172.
DE   RecName: Full=39S ribosomal protein L13, mitochondrial;
DE            Short=L13mt;
DE            Short=MRP-L13;
DE   AltName: Full=Mitochondrial large ribosomal subunit protein uL13m {ECO:0000303|PubMed:25278503};
GN   Name=MRPL13;
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].
RX   PubMed=11279069; DOI=10.1074/jbc.m100432200;
RA   Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA   Watanabe K.;
RT   "Structural compensation for the deficit of rRNA with proteins in the
RT   mammalian mitochondrial ribosome. Systematic analysis of protein components
RT   of the large ribosomal subunit from mammalian mitochondria.";
RL   J. Biol. Chem. 276:21724-21736(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal gland;
RA   Ren S., Jiang C., Huang C., Li Y., Lin W., Zhou J., Yu Y., Xu S., Wang Y.,
RA   Han Z., Chen Z., Fu G.;
RT   "A novel gene expressed in human adrenal gland.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
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].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Placenta;
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   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   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [8] {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   [9] {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   [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:25278503, PubMed:25838379, PubMed:28892042). Mature
CC       mammalian 55S mitochondrial ribosomes consist of a small (28S) and a
CC       large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA
CC       (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains
CC       a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA
CC       (mt-tRNA(Val)), which plays an integral structural role, and 52
CC       different proteins (PubMed:25278503, PubMed:25838379). Interacts with
CC       OXA1L (By similarity). {ECO:0000250|UniProtKB:Q3SYS1,
CC       ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC       ECO:0000269|PubMed:28892042}.
CC   -!- INTERACTION:
CC       Q9BYD1; P42858: HTT; NbExp=3; IntAct=EBI-1054936, EBI-466029;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC       ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL13 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF17202.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB049640; BAB40845.1; -; mRNA.
DR   EMBL; AF112214; AAF17202.1; ALT_FRAME; mRNA.
DR   EMBL; AK311924; BAG34865.1; -; mRNA.
DR   EMBL; CH471060; EAW92004.1; -; Genomic_DNA.
DR   EMBL; BC009190; AAH09190.1; -; mRNA.
DR   EMBL; BC021744; AAH21744.1; -; mRNA.
DR   CCDS; CCDS6332.1; -.
DR   RefSeq; NP_054797.2; NM_014078.5.
DR   PDB; 3J7Y; EM; 3.40 A; K=1-178.
DR   PDB; 3J9M; EM; 3.50 A; K=1-178.
DR   PDB; 5OOL; EM; 3.06 A; K=1-178.
DR   PDB; 5OOM; EM; 3.03 A; K=1-178.
DR   PDB; 6I9R; EM; 3.90 A; K=1-178.
DR   PDB; 6NU2; EM; 3.90 A; K=2-178.
DR   PDB; 6NU3; EM; 4.40 A; K=1-178.
DR   PDB; 6VLZ; EM; 2.97 A; K=1-178.
DR   PDB; 6VMI; EM; 2.96 A; K=1-178.
DR   PDB; 6ZM5; EM; 2.89 A; K=2-178.
DR   PDB; 6ZM6; EM; 2.59 A; K=2-178.
DR   PDB; 6ZS9; EM; 4.00 A; XK=1-178.
DR   PDB; 6ZSA; EM; 4.00 A; XK=1-178.
DR   PDB; 6ZSB; EM; 4.50 A; XK=1-178.
DR   PDB; 6ZSC; EM; 3.50 A; XK=1-178.
DR   PDB; 6ZSD; EM; 3.70 A; XK=1-178.
DR   PDB; 6ZSE; EM; 5.00 A; XK=1-178.
DR   PDB; 6ZSG; EM; 4.00 A; XK=1-178.
DR   PDB; 7A5F; EM; 4.40 A; K3=1-178.
DR   PDB; 7A5G; EM; 4.33 A; K3=1-178.
DR   PDB; 7A5H; EM; 3.30 A; K=1-178.
DR   PDB; 7A5I; EM; 3.70 A; K3=1-178.
DR   PDB; 7A5J; EM; 3.10 A; K=1-178.
DR   PDB; 7A5K; EM; 3.70 A; K3=1-178.
DR   PDB; 7L08; EM; 3.49 A; K=1-178.
DR   PDB; 7L20; EM; 3.15 A; K=1-178.
DR   PDB; 7O9K; EM; 3.10 A; K=1-178.
DR   PDB; 7O9M; EM; 2.50 A; K=1-178.
DR   PDB; 7ODR; EM; 2.90 A; K=1-178.
DR   PDB; 7ODS; EM; 3.10 A; K=1-178.
DR   PDB; 7ODT; EM; 3.10 A; K=1-178.
DR   PDB; 7OF0; EM; 2.20 A; K=1-178.
DR   PDB; 7OF2; EM; 2.70 A; K=1-178.
DR   PDB; 7OF3; EM; 2.70 A; K=1-178.
DR   PDB; 7OF4; EM; 2.70 A; K=1-178.
DR   PDB; 7OF5; EM; 2.90 A; K=1-178.
DR   PDB; 7OF6; EM; 2.60 A; K=1-178.
DR   PDB; 7OF7; EM; 2.50 A; K=1-178.
DR   PDB; 7OG4; EM; 3.80 A; XK=1-178.
DR   PDB; 7OI6; EM; 5.70 A; K=1-178.
DR   PDB; 7OI7; EM; 3.50 A; K=1-178.
DR   PDB; 7OI8; EM; 3.50 A; K=1-178.
DR   PDB; 7OI9; EM; 3.30 A; K=1-178.
DR   PDB; 7OIA; EM; 3.20 A; K=1-178.
DR   PDB; 7OIB; EM; 3.30 A; K=1-178.
DR   PDB; 7OIC; EM; 3.10 A; K=1-178.
DR   PDB; 7OID; EM; 3.70 A; K=1-178.
DR   PDB; 7OIE; EM; 3.50 A; K=1-178.
DR   PDB; 7PD3; EM; 3.40 A; K=1-178.
DR   PDB; 7QH6; EM; 3.08 A; K=1-178.
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; Q9BYD1; -.
DR   SMR; Q9BYD1; -.
DR   BioGRID; 118817; 226.
DR   ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR   CORUM; Q9BYD1; -.
DR   IntAct; Q9BYD1; 59.
DR   MINT; Q9BYD1; -.
DR   STRING; 9606.ENSP00000306548; -.
DR   GlyGen; Q9BYD1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BYD1; -.
DR   PhosphoSitePlus; Q9BYD1; -.
DR   BioMuta; MRPL13; -.
DR   DMDM; 22257023; -.
DR   EPD; Q9BYD1; -.
DR   jPOST; Q9BYD1; -.
DR   MassIVE; Q9BYD1; -.
DR   MaxQB; Q9BYD1; -.
DR   PaxDb; Q9BYD1; -.
DR   PeptideAtlas; Q9BYD1; -.
DR   PRIDE; Q9BYD1; -.
DR   ProteomicsDB; 79615; -.
DR   TopDownProteomics; Q9BYD1; -.
DR   Antibodypedia; 26860; 189 antibodies from 26 providers.
DR   DNASU; 28998; -.
DR   Ensembl; ENST00000306185.8; ENSP00000306548.3; ENSG00000172172.8.
DR   GeneID; 28998; -.
DR   KEGG; hsa:28998; -.
DR   MANE-Select; ENST00000306185.8; ENSP00000306548.3; NM_014078.6; NP_054797.2.
DR   UCSC; uc003ypa.4; human.
DR   CTD; 28998; -.
DR   DisGeNET; 28998; -.
DR   GeneCards; MRPL13; -.
DR   HGNC; HGNC:14278; MRPL13.
DR   HPA; ENSG00000172172; Low tissue specificity.
DR   MIM; 610200; gene.
DR   neXtProt; NX_Q9BYD1; -.
DR   OpenTargets; ENSG00000172172; -.
DR   PharmGKB; PA30942; -.
DR   VEuPathDB; HostDB:ENSG00000172172; -.
DR   eggNOG; KOG3203; Eukaryota.
DR   GeneTree; ENSGT00390000001515; -.
DR   HOGENOM; CLU_082184_1_3_1; -.
DR   InParanoid; Q9BYD1; -.
DR   OMA; DFVVIIN; -.
DR   OrthoDB; 1119705at2759; -.
DR   PhylomeDB; Q9BYD1; -.
DR   TreeFam; TF312914; -.
DR   PathwayCommons; Q9BYD1; -.
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; Q9BYD1; -.
DR   SIGNOR; Q9BYD1; -.
DR   BioGRID-ORCS; 28998; 315 hits in 1094 CRISPR screens.
DR   ChiTaRS; MRPL13; human.
DR   GenomeRNAi; 28998; -.
DR   Pharos; Q9BYD1; Tbio.
DR   PRO; PR:Q9BYD1; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9BYD1; protein.
DR   Bgee; ENSG00000172172; Expressed in mucosa of transverse colon and 191 other tissues.
DR   ExpressionAtlas; Q9BYD1; baseline and differential.
DR   Genevisible; Q9BYD1; 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:0005761; C:mitochondrial ribosome; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR   GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; NAS:UniProtKB.
DR   CDD; cd00392; Ribosomal_L13; 1.
DR   Gene3D; 3.90.1180.10; -; 1.
DR   HAMAP; MF_01366; Ribosomal_L13; 1.
DR   InterPro; IPR005822; Ribosomal_L13.
DR   InterPro; IPR005823; Ribosomal_L13_bac-type.
DR   InterPro; IPR023563; Ribosomal_L13_CS.
DR   InterPro; IPR036899; Ribosomal_L13_sf.
DR   PANTHER; PTHR11545; PTHR11545; 1.
DR   Pfam; PF00572; Ribosomal_L13; 1.
DR   PIRSF; PIRSF002181; Ribosomal_L13; 1.
DR   SUPFAM; SSF52161; SSF52161; 1.
DR   TIGRFAMs; TIGR01066; rplM_bact; 1.
DR   PROSITE; PS00783; RIBOSOMAL_L13; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Mitochondrion; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:25944712"
FT   CHAIN           2..178
FT                   /note="39S ribosomal protein L13, mitochondrial"
FT                   /id="PRO_0000133793"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:25944712"
FT   HELIX           6..14
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           28..40
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   TURN            49..52
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           71..74
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          87..91
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           92..98
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           102..111
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           118..123
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          129..131
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           135..140
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          141..144
FT                   /evidence="ECO:0007829|PDB:5OOM"
FT   TURN            155..157
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           160..165
FT                   /evidence="ECO:0007829|PDB:7OF0"
SQ   SEQUENCE   178 AA;  20692 MW;  AF4FD524CC234D52 CRC64;
     MSSFSRAPQQ WATFARIWYL LDGKMQPPGK LAAMASIRLQ GLHKPVYHAL SDCGDHVVIM
     NTRHIAFSGN KWEQKVYSSH TGYPGGFRQV TAAQLHLRDP VAIVKLAIYG MLPKNLHRRT
     MMERLHLFPD EYIPEDILKN LVEELPQPRK IPKRLDEYTQ EEIDAFPRLW TPPEDYRL
 
 
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