RM02_HUMAN
ID RM02_HUMAN Reviewed; 305 AA.
AC Q5T653; B2RC56; Q8WUL1; Q96Q56; Q9Y311;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=39S ribosomal protein L2, mitochondrial;
DE Short=L2mt;
DE Short=MRP-L2;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL2m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL2; ORFNames=CGI-22;
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].
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 [LARGE SCALE MRNA].
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and 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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-305.
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 [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 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 [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: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. {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, 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 universal ribosomal protein uL2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27731.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF132956; AAD27731.1; ALT_FRAME; mRNA.
DR EMBL; AK314948; BAG37453.1; -; mRNA.
DR EMBL; AL355385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013685; AAH13685.1; -; mRNA.
DR EMBL; BC020212; AAH20212.1; -; mRNA.
DR EMBL; AB051617; BAB54945.1; -; Genomic_DNA.
DR CCDS; CCDS34454.1; -.
DR RefSeq; NP_001287777.1; NM_001300848.1.
DR RefSeq; NP_057034.2; NM_015950.4.
DR PDB; 3J7Y; EM; 3.40 A; D=1-305.
DR PDB; 3J9M; EM; 3.50 A; D=1-305.
DR PDB; 5OOL; EM; 3.06 A; D=1-305.
DR PDB; 5OOM; EM; 3.03 A; D=1-305.
DR PDB; 6I9R; EM; 3.90 A; D=1-305.
DR PDB; 6NU2; EM; 3.90 A; D=61-296.
DR PDB; 6NU3; EM; 4.40 A; D=1-305.
DR PDB; 6VLZ; EM; 2.97 A; D=1-305.
DR PDB; 6VMI; EM; 2.96 A; D=1-305.
DR PDB; 6ZM5; EM; 2.89 A; D=1-305.
DR PDB; 6ZM6; EM; 2.59 A; D=1-305.
DR PDB; 6ZS9; EM; 4.00 A; XD=1-305.
DR PDB; 6ZSA; EM; 4.00 A; XD=1-305.
DR PDB; 6ZSB; EM; 4.50 A; XD=1-305.
DR PDB; 6ZSC; EM; 3.50 A; XD=1-305.
DR PDB; 6ZSD; EM; 3.70 A; XD=1-305.
DR PDB; 6ZSE; EM; 5.00 A; XD=1-305.
DR PDB; 6ZSG; EM; 4.00 A; XD=1-305.
DR PDB; 7A5F; EM; 4.40 A; D3=1-305.
DR PDB; 7A5G; EM; 4.33 A; D3=1-305.
DR PDB; 7A5H; EM; 3.30 A; D=1-305.
DR PDB; 7A5I; EM; 3.70 A; D3=1-305.
DR PDB; 7A5J; EM; 3.10 A; D=1-305.
DR PDB; 7A5K; EM; 3.70 A; D3=1-305.
DR PDB; 7L08; EM; 3.49 A; D=1-305.
DR PDB; 7L20; EM; 3.15 A; D=1-305.
DR PDB; 7O9K; EM; 3.10 A; D=1-305.
DR PDB; 7O9M; EM; 2.50 A; D=1-305.
DR PDB; 7ODR; EM; 2.90 A; D=1-305.
DR PDB; 7ODS; EM; 3.10 A; D=1-305.
DR PDB; 7ODT; EM; 3.10 A; D=1-305.
DR PDB; 7OF0; EM; 2.20 A; D=1-305.
DR PDB; 7OF2; EM; 2.70 A; D=1-305.
DR PDB; 7OF3; EM; 2.70 A; D=1-305.
DR PDB; 7OF4; EM; 2.70 A; D=1-305.
DR PDB; 7OF5; EM; 2.90 A; D=1-305.
DR PDB; 7OF6; EM; 2.60 A; D=1-305.
DR PDB; 7OF7; EM; 2.50 A; D=1-305.
DR PDB; 7OG4; EM; 3.80 A; XD=1-305.
DR PDB; 7OI6; EM; 5.70 A; D=1-305.
DR PDB; 7OI7; EM; 3.50 A; D=1-305.
DR PDB; 7OI8; EM; 3.50 A; D=1-305.
DR PDB; 7OI9; EM; 3.30 A; D=1-305.
DR PDB; 7OIA; EM; 3.20 A; D=1-305.
DR PDB; 7OIB; EM; 3.30 A; D=1-305.
DR PDB; 7OIC; EM; 3.10 A; D=1-305.
DR PDB; 7OID; EM; 3.70 A; D=1-305.
DR PDB; 7OIE; EM; 3.50 A; D=1-305.
DR PDB; 7PD3; EM; 3.40 A; D=1-305.
DR PDB; 7QH6; EM; 3.08 A; D=1-305.
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; Q5T653; -.
DR SMR; Q5T653; -.
DR BioGRID; 119260; 218.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q5T653; -.
DR IntAct; Q5T653; 46.
DR MINT; Q5T653; -.
DR STRING; 9606.ENSP00000373404; -.
DR GlyGen; Q5T653; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5T653; -.
DR MetOSite; Q5T653; -.
DR PhosphoSitePlus; Q5T653; -.
DR SwissPalm; Q5T653; -.
DR BioMuta; MRPL2; -.
DR DMDM; 118573672; -.
DR EPD; Q5T653; -.
DR jPOST; Q5T653; -.
DR MassIVE; Q5T653; -.
DR MaxQB; Q5T653; -.
DR PaxDb; Q5T653; -.
DR PeptideAtlas; Q5T653; -.
DR PRIDE; Q5T653; -.
DR ProteomicsDB; 64566; -.
DR TopDownProteomics; Q5T653; -.
DR Antibodypedia; 2348; 152 antibodies from 22 providers.
DR DNASU; 51069; -.
DR Ensembl; ENST00000388752.8; ENSP00000373404.3; ENSG00000112651.12.
DR GeneID; 51069; -.
DR KEGG; hsa:51069; -.
DR MANE-Select; ENST00000388752.8; ENSP00000373404.3; NM_015950.5; NP_057034.2.
DR UCSC; uc003ots.2; human.
DR CTD; 51069; -.
DR GeneCards; MRPL2; -.
DR HGNC; HGNC:14056; MRPL2.
DR HPA; ENSG00000112651; Low tissue specificity.
DR MIM; 611822; gene.
DR neXtProt; NX_Q5T653; -.
DR OpenTargets; ENSG00000112651; -.
DR PharmGKB; PA30949; -.
DR VEuPathDB; HostDB:ENSG00000112651; -.
DR eggNOG; KOG0438; Eukaryota.
DR GeneTree; ENSGT00940000153244; -.
DR HOGENOM; CLU_036235_1_2_1; -.
DR InParanoid; Q5T653; -.
DR OMA; CHLIHAA; -.
DR OrthoDB; 1156335at2759; -.
DR PhylomeDB; Q5T653; -.
DR TreeFam; TF314647; -.
DR PathwayCommons; Q5T653; -.
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; Q5T653; -.
DR SIGNOR; Q5T653; -.
DR BioGRID-ORCS; 51069; 262 hits in 1076 CRISPR screens.
DR ChiTaRS; MRPL2; human.
DR GenomeRNAi; 51069; -.
DR Pharos; Q5T653; Tdark.
DR PRO; PR:Q5T653; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5T653; protein.
DR Bgee; ENSG00000112651; Expressed in hindlimb stylopod muscle and 179 other tissues.
DR ExpressionAtlas; Q5T653; baseline and differential.
DR Genevisible; Q5T653; 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:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IBA:GO_Central.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..60
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 61..305
FT /note="39S ribosomal protein L2, mitochondrial"
FT /id="PRO_0000261640"
FT REGION 264..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..283
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 300
FT /note="S -> F (in dbSNP:rs10456521)"
FT /id="VAR_029470"
FT CONFLICT 11..12
FT /note="RS -> LV (in Ref. 1; AAD27731)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..224
FT /note="TA -> HS (in Ref. 1; AAD27731)"
FT /evidence="ECO:0000305"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:5OOL"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5OOL"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:7OIE"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:5OOL"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:7OIB"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:5OOL"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:5OOL"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 305 AA; 33301 MW; AE1D777E2CF9DBCB CRC64;
MALCALTRAL RSLNLAPPTV AAPAPSLFPA AQMMNNGLLQ QPSALMLLPC RPVLTSVALN
ANFVSWKSRT KYTITPVKMR KSGGRDHTGR IRVHGIGGGH KQRYRMIDFL RFRPEETKSG
PFEEKVIQVR YDPCRSADIA LVAGGSRKRW IIATENMQAG DTILNSNHIG RMAVAAREGD
AHPLGALPVG TLINNVESEP GRGAQYIRAA GTCGVLLRKV NGTAIIQLPS KRQMQVLETC
VATVGRVSNV DHNKRVIGKA GRNRWLGKRP NSGRWHRKGG WAGRKIRPLP PMKSYVKLPS
ASAQS
