RM37_HUMAN
ID RM37_HUMAN Reviewed; 423 AA.
AC Q9BZE1; Q96Q67; Q9BWR1; Q9P0P3;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=39S ribosomal protein L37, mitochondrial;
DE Short=L37mt;
DE Short=MRP-L37;
DE AltName: Full=39S ribosomal protein L2, mitochondrial;
DE Short=L2mt;
DE Short=MRP-L2;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL37 {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL37; Synonyms=MRPL2, RPML2; ORFNames=HSPC235;
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], AND VARIANT SER-366.
RC TISSUE=Skeletal muscle;
RA Levshenkova E.V., Bashirova A.A., Markelov M.L., Frolova E.I.;
RT "Novel gene located on human chromosome 1.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-366.
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-322 AND SER-366.
RG NIEHS SNPs program;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-423.
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: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 [11] {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:25838379, PubMed:25278503). 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. mL37 forms a heterodimer with mL65.
CC {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC ECO:0000269|PubMed:28892042}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL37 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36155.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mrpl37/";
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DR EMBL; AF325707; AAG52881.1; -; mRNA.
DR EMBL; AF151069; AAF36155.1; ALT_FRAME; mRNA.
DR EMBL; DQ205685; ABA27099.1; -; Genomic_DNA.
DR EMBL; AL357673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000041; AAH00041.1; -; mRNA.
DR EMBL; AB051344; BAB54934.1; -; Genomic_DNA.
DR CCDS; CCDS589.1; -.
DR RefSeq; NP_057575.2; NM_016491.3.
DR PDB; 3J7Y; EM; 3.40 A; 5=1-423.
DR PDB; 3J9M; EM; 3.50 A; 5=1-423.
DR PDB; 5OOL; EM; 3.06 A; 5=1-423.
DR PDB; 5OOM; EM; 3.03 A; 5=1-423.
DR PDB; 6I9R; EM; 3.90 A; 5=1-423.
DR PDB; 6NU2; EM; 3.90 A; 5=31-422.
DR PDB; 6NU3; EM; 4.40 A; 5=30-423.
DR PDB; 6VLZ; EM; 2.97 A; 5=1-423.
DR PDB; 6VMI; EM; 2.96 A; 5=1-423.
DR PDB; 6ZM5; EM; 2.89 A; 5=1-423.
DR PDB; 6ZM6; EM; 2.59 A; 5=1-423.
DR PDB; 6ZS9; EM; 4.00 A; 5=1-423.
DR PDB; 6ZSA; EM; 4.00 A; 5=1-423.
DR PDB; 6ZSB; EM; 4.50 A; 5=1-423.
DR PDB; 6ZSC; EM; 3.50 A; 5=1-423.
DR PDB; 6ZSD; EM; 3.70 A; 5=1-423.
DR PDB; 6ZSE; EM; 5.00 A; 5=1-423.
DR PDB; 6ZSG; EM; 4.00 A; 5=1-423.
DR PDB; 7A5F; EM; 4.40 A; 53=1-423.
DR PDB; 7A5G; EM; 4.33 A; 53=1-423.
DR PDB; 7A5H; EM; 3.30 A; 5=1-423.
DR PDB; 7A5I; EM; 3.70 A; 53=1-423.
DR PDB; 7A5J; EM; 3.10 A; 5=1-423.
DR PDB; 7A5K; EM; 3.70 A; 53=1-423.
DR PDB; 7L08; EM; 3.49 A; 5=1-423.
DR PDB; 7L20; EM; 3.15 A; 5=1-423.
DR PDB; 7O9K; EM; 3.10 A; 5=1-423.
DR PDB; 7O9M; EM; 2.50 A; 5=1-423.
DR PDB; 7ODR; EM; 2.90 A; 5=1-423.
DR PDB; 7ODS; EM; 3.10 A; 5=1-423.
DR PDB; 7ODT; EM; 3.10 A; 5=1-423.
DR PDB; 7OF0; EM; 2.20 A; 5=1-423.
DR PDB; 7OF2; EM; 2.70 A; 5=1-423.
DR PDB; 7OF3; EM; 2.70 A; 5=1-423.
DR PDB; 7OF4; EM; 2.70 A; 5=1-423.
DR PDB; 7OF5; EM; 2.90 A; 5=1-423.
DR PDB; 7OF6; EM; 2.60 A; 5=1-423.
DR PDB; 7OF7; EM; 2.50 A; 5=1-423.
DR PDB; 7OG4; EM; 3.80 A; 5=1-423.
DR PDB; 7OI6; EM; 5.70 A; 5=1-423.
DR PDB; 7OI7; EM; 3.50 A; 5=1-423.
DR PDB; 7OI8; EM; 3.50 A; 5=1-423.
DR PDB; 7OI9; EM; 3.30 A; 5=1-423.
DR PDB; 7OIA; EM; 3.20 A; 5=1-423.
DR PDB; 7OIB; EM; 3.30 A; 5=1-423.
DR PDB; 7OIC; EM; 3.10 A; 5=1-423.
DR PDB; 7OID; EM; 3.70 A; 5=1-423.
DR PDB; 7OIE; EM; 3.50 A; 5=1-423.
DR PDB; 7PD3; EM; 3.40 A; 5=1-423.
DR PDB; 7QH6; EM; 3.08 A; 5=1-423.
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; Q9BZE1; -.
DR SMR; Q9BZE1; -.
DR BioGRID; 119410; 223.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9BZE1; -.
DR DIP; DIP-59718N; -.
DR IntAct; Q9BZE1; 58.
DR MINT; Q9BZE1; -.
DR STRING; 9606.ENSP00000354086; -.
DR GlyGen; Q9BZE1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BZE1; -.
DR PhosphoSitePlus; Q9BZE1; -.
DR SwissPalm; Q9BZE1; -.
DR BioMuta; MRPL37; -.
DR DMDM; 152083350; -.
DR EPD; Q9BZE1; -.
DR jPOST; Q9BZE1; -.
DR MassIVE; Q9BZE1; -.
DR MaxQB; Q9BZE1; -.
DR PaxDb; Q9BZE1; -.
DR PeptideAtlas; Q9BZE1; -.
DR PRIDE; Q9BZE1; -.
DR ProteomicsDB; 79819; -.
DR Antibodypedia; 19283; 80 antibodies from 23 providers.
DR DNASU; 51253; -.
DR Ensembl; ENST00000360840.9; ENSP00000354086.5; ENSG00000116221.15.
DR GeneID; 51253; -.
DR KEGG; hsa:51253; -.
DR MANE-Select; ENST00000360840.9; ENSP00000354086.5; NM_016491.4; NP_057575.2.
DR UCSC; uc001cxa.4; human.
DR CTD; 51253; -.
DR DisGeNET; 51253; -.
DR GeneCards; MRPL37; -.
DR HGNC; HGNC:14034; MRPL37.
DR HPA; ENSG00000116221; Low tissue specificity.
DR MIM; 611843; gene.
DR neXtProt; NX_Q9BZE1; -.
DR OpenTargets; ENSG00000116221; -.
DR PharmGKB; PA30968; -.
DR VEuPathDB; HostDB:ENSG00000116221; -.
DR eggNOG; ENOG502QQAQ; Eukaryota.
DR GeneTree; ENSGT00390000000867; -.
DR HOGENOM; CLU_037022_1_0_1; -.
DR InParanoid; Q9BZE1; -.
DR OMA; TTWNRES; -.
DR PhylomeDB; Q9BZE1; -.
DR TreeFam; TF323297; -.
DR PathwayCommons; Q9BZE1; -.
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; Q9BZE1; -.
DR SIGNOR; Q9BZE1; -.
DR BioGRID-ORCS; 51253; 321 hits in 1079 CRISPR screens.
DR ChiTaRS; MRPL37; human.
DR GeneWiki; MRPL37; -.
DR GenomeRNAi; 51253; -.
DR Pharos; Q9BZE1; Tdark.
DR PRO; PR:Q9BZE1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BZE1; protein.
DR Bgee; ENSG00000116221; Expressed in gastrocnemius and 183 other tissues.
DR ExpressionAtlas; Q9BZE1; baseline and differential.
DR Genevisible; Q9BZE1; 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; NAS: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; NAS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR InterPro; IPR010793; Ribosomal_L37/S30.
DR Pfam; PF07147; PDCD9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..423
FT /note="39S ribosomal protein L37, mitochondrial"
FT /id="PRO_0000045905"
FT VARIANT 322
FT /note="L -> V (in dbSNP:rs2275408)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025269"
FT VARIANT 366
FT /note="C -> S (in dbSNP:rs13571)"
FT /evidence="ECO:0000269|PubMed:11042152, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.3"
FT /id="VAR_025270"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5OOL"
FT TURN 60..64
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:3J7Y"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 173..189
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 306..328
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 335..362
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 372..382
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 408..419
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 423 AA; 48117 MW; 9556DAF4349F6EEB CRC64;
MALASGPARR ALAGSGQLGL GGFGAPRRGA YEWGVRSTRK SEPPPLDRVY EIPGLEPITF
AGKMHFVPWL ARPIFPPWDR GYKDPRFYRS PPLHEHPLYK DQACYIFHHR CRLLEGVKQA
LWLTKTKLIE GLPEKVLSLV DDPRNHIENQ DECVLNVISH ARLWQTTEEI PKRETYCPVI
VDNLIQLCKS QILKHPSLAR RICVQNSTFS ATWNRESLLL QVRGSGGARL STKDPLPTIA
SREEIEATKN HVLETFYPIS PIIDLHECNI YDVKNDTGFQ EGYPYPYPHT LYLLDKANLR
PHRLQPDQLR AKMILFAFGS ALAQARLLYG NDAKVLEQPV VVQSVGTDGR VFHFLVFQLN
TTDLDCNEGV KNLAWVDSDQ LLYQHFWCLP VIKKRVVVEP VGPVGFKPET FRKFLALYLH
GAA
