RM38_HUMAN
ID RM38_HUMAN Reviewed; 380 AA.
AC Q96DV4; B3KN96; Q96Q66; Q9P0B9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=39S ribosomal protein L38, mitochondrial;
DE Short=L38mt;
DE Short=MRP-L38;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL38 {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL38; ORFNames=HSPC262;
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 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-197.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 207-346 (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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. mL38 is located at the central protuberance.
CC {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC ECO:0000269|PubMed:28892042}.
CC -!- INTERACTION:
CC Q96DV4; Q9BRR9: ARHGAP9; NbExp=3; IntAct=EBI-720441, EBI-750254;
CC Q96DV4; O95817: BAG3; NbExp=3; IntAct=EBI-720441, EBI-747185;
CC Q96DV4; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-720441, EBI-745073;
CC Q96DV4; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-720441, EBI-744556;
CC Q96DV4; Q86UT8: CENATAC; NbExp=3; IntAct=EBI-720441, EBI-11028020;
CC Q96DV4; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-720441, EBI-744099;
CC Q96DV4; Q8TAE8: GADD45GIP1; NbExp=4; IntAct=EBI-720441, EBI-372506;
CC Q96DV4; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-720441, EBI-11163335;
CC Q96DV4; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-720441, EBI-2341787;
CC Q96DV4; Q13064: MKRN3; NbExp=3; IntAct=EBI-720441, EBI-2340269;
CC Q96DV4; Q9H0U6: MRPL18; NbExp=4; IntAct=EBI-720441, EBI-2560240;
CC Q96DV4; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-720441, EBI-5662487;
CC Q96DV4; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-720441, EBI-2557469;
CC Q96DV4; Q53GL6: RALY; NbExp=3; IntAct=EBI-720441, EBI-9512693;
CC Q96DV4; P26373: RPL13; NbExp=2; IntAct=EBI-720441, EBI-356849;
CC Q96DV4; Q7Z6J9: TSEN54; NbExp=3; IntAct=EBI-720441, EBI-2559824;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96DV4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DV4-2; Sequence=VSP_056090;
CC -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein
CC family. Mitochondrion-specific ribosomal protein mL38 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13311.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK024058; BAG51258.1; -; mRNA.
DR EMBL; AC087289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013311; AAH13311.1; ALT_INIT; mRNA.
DR EMBL; AB051345; BAB54935.1; -; Genomic_DNA.
DR EMBL; AF161380; AAF28940.1; -; mRNA.
DR CCDS; CCDS11733.2; -. [Q96DV4-1]
DR RefSeq; NP_115867.2; NM_032478.3. [Q96DV4-1]
DR PDB; 3J7Y; EM; 3.40 A; 6=1-380.
DR PDB; 3J9M; EM; 3.50 A; 6=1-380.
DR PDB; 5OOL; EM; 3.06 A; 6=1-380.
DR PDB; 5OOM; EM; 3.03 A; 6=1-380.
DR PDB; 6I9R; EM; 3.90 A; 6=1-380.
DR PDB; 6NU2; EM; 3.90 A; 6=27-380.
DR PDB; 6NU3; EM; 4.40 A; 6=1-380.
DR PDB; 6VLZ; EM; 2.97 A; 6=1-380.
DR PDB; 6VMI; EM; 2.96 A; 6=1-380.
DR PDB; 6ZM5; EM; 2.89 A; 6=1-380.
DR PDB; 6ZM6; EM; 2.59 A; 6=1-380.
DR PDB; 6ZS9; EM; 4.00 A; 6=1-380.
DR PDB; 6ZSA; EM; 4.00 A; 6=1-380.
DR PDB; 6ZSB; EM; 4.50 A; 6=1-380.
DR PDB; 6ZSC; EM; 3.50 A; 6=1-380.
DR PDB; 6ZSD; EM; 3.70 A; 6=1-380.
DR PDB; 6ZSE; EM; 5.00 A; 6=1-380.
DR PDB; 6ZSG; EM; 4.00 A; 6=1-380.
DR PDB; 7A5F; EM; 4.40 A; 63=1-380.
DR PDB; 7A5G; EM; 4.33 A; 63=1-380.
DR PDB; 7A5H; EM; 3.30 A; 6=1-380.
DR PDB; 7A5I; EM; 3.70 A; 63=1-380.
DR PDB; 7A5J; EM; 3.10 A; 6=1-380.
DR PDB; 7A5K; EM; 3.70 A; 63=1-380.
DR PDB; 7L08; EM; 3.49 A; 6=1-380.
DR PDB; 7L20; EM; 3.15 A; 6=1-380.
DR PDB; 7O9K; EM; 3.10 A; 6=1-380.
DR PDB; 7O9M; EM; 2.50 A; 6=1-380.
DR PDB; 7ODR; EM; 2.90 A; 6=1-380.
DR PDB; 7ODS; EM; 3.10 A; 6=1-380.
DR PDB; 7ODT; EM; 3.10 A; 6=1-380.
DR PDB; 7OF0; EM; 2.20 A; 6=1-380.
DR PDB; 7OF2; EM; 2.70 A; 6=1-380.
DR PDB; 7OF3; EM; 2.70 A; 6=1-380.
DR PDB; 7OF4; EM; 2.70 A; 6=1-380.
DR PDB; 7OF5; EM; 2.90 A; 6=1-380.
DR PDB; 7OF6; EM; 2.60 A; 6=1-380.
DR PDB; 7OF7; EM; 2.50 A; 6=1-380.
DR PDB; 7OG4; EM; 3.80 A; 6=1-380.
DR PDB; 7OI6; EM; 5.70 A; 6=1-380.
DR PDB; 7OI7; EM; 3.50 A; 6=1-380.
DR PDB; 7OI8; EM; 3.50 A; 6=1-380.
DR PDB; 7OI9; EM; 3.30 A; 6=1-380.
DR PDB; 7OIA; EM; 3.20 A; 6=1-380.
DR PDB; 7OIB; EM; 3.30 A; 6=1-380.
DR PDB; 7OIC; EM; 3.10 A; 6=1-380.
DR PDB; 7OID; EM; 3.70 A; 6=1-380.
DR PDB; 7OIE; EM; 3.50 A; 6=1-380.
DR PDB; 7PD3; EM; 3.40 A; 6=1-380.
DR PDB; 7QH6; EM; 3.08 A; 6=1-380.
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; Q96DV4; -.
DR SMR; Q96DV4; -.
DR BioGRID; 122365; 246.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q96DV4; -.
DR IntAct; Q96DV4; 116.
DR MINT; Q96DV4; -.
DR STRING; 9606.ENSP00000308275; -.
DR GlyGen; Q96DV4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96DV4; -.
DR PhosphoSitePlus; Q96DV4; -.
DR SwissPalm; Q96DV4; -.
DR BioMuta; MRPL38; -.
DR DMDM; 118573679; -.
DR EPD; Q96DV4; -.
DR jPOST; Q96DV4; -.
DR MassIVE; Q96DV4; -.
DR MaxQB; Q96DV4; -.
DR PaxDb; Q96DV4; -.
DR PeptideAtlas; Q96DV4; -.
DR PRIDE; Q96DV4; -.
DR ProteomicsDB; 3499; -.
DR ProteomicsDB; 76330; -. [Q96DV4-1]
DR Antibodypedia; 19644; 110 antibodies from 24 providers.
DR DNASU; 64978; -.
DR Ensembl; ENST00000309352.4; ENSP00000308275.4; ENSG00000204316.13. [Q96DV4-1]
DR GeneID; 64978; -.
DR KEGG; hsa:64978; -.
DR MANE-Select; ENST00000309352.4; ENSP00000308275.4; NM_032478.4; NP_115867.2.
DR UCSC; uc010wso.2; human. [Q96DV4-1]
DR CTD; 64978; -.
DR DisGeNET; 64978; -.
DR GeneCards; MRPL38; -.
DR HGNC; HGNC:14033; MRPL38.
DR HPA; ENSG00000204316; Low tissue specificity.
DR MIM; 611844; gene.
DR neXtProt; NX_Q96DV4; -.
DR OpenTargets; ENSG00000204316; -.
DR PharmGKB; PA30969; -.
DR VEuPathDB; HostDB:ENSG00000204316; -.
DR eggNOG; KOG3346; Eukaryota.
DR GeneTree; ENSGT00900000141125; -.
DR HOGENOM; CLU_043994_0_0_1; -.
DR InParanoid; Q96DV4; -.
DR OMA; EMCHYLP; -.
DR OrthoDB; 1557122at2759; -.
DR PhylomeDB; Q96DV4; -.
DR TreeFam; TF315074; -.
DR PathwayCommons; Q96DV4; -.
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; Q96DV4; -.
DR SIGNOR; Q96DV4; -.
DR BioGRID-ORCS; 64978; 489 hits in 1084 CRISPR screens.
DR ChiTaRS; MRPL38; human.
DR GenomeRNAi; 64978; -.
DR Pharos; Q96DV4; Tdark.
DR PRO; PR:Q96DV4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96DV4; protein.
DR Bgee; ENSG00000204316; Expressed in right hemisphere of cerebellum and 95 other tissues.
DR Genevisible; Q96DV4; 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:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR CDD; cd00866; PEBP_euk; 1.
DR Gene3D; 3.90.280.10; -; 1.
DR InterPro; IPR008914; PEBP.
DR InterPro; IPR036610; PEBP-like_sf.
DR InterPro; IPR035810; PEBP_euk.
DR PANTHER; PTHR11362; PTHR11362; 1.
DR Pfam; PF01161; PBP; 1.
DR SUPFAM; SSF49777; SSF49777; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Mitochondrion;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..380
FT /note="39S ribosomal protein L38, mitochondrial"
FT /id="PRO_0000261652"
FT COILED 99..127
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056090"
FT VARIANT 99
FT /note="R -> W (in dbSNP:rs34136221)"
FT /id="VAR_059808"
FT VARIANT 371
FT /note="D -> H (in dbSNP:rs9191)"
FT /id="VAR_029472"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:5OOL"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5OOL"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3J7Y"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:7OI7"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 231..241
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:3J7Y"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 266..277
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 306..310
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 311..321
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 380 AA; 44597 MW; 7BC527A7E1C06A6C CRC64;
MAAPWWRAAL CECRRWRGFS TSAVLGRRTP PLGPMPNSDI DLSNLERLEK YRSFDRYRRR
AEQEAQAPHW WRTYREYFGE KTDPKEKIDI GLPPPKVSRT QQLLERKQAI QELRANVEEE
RAARLRTASV PLDAVRAEWE RTCGPYHKQR LAEYYGLYRD LFHGATFVPR VPLHVAYAVG
EDDLMPVYCG NEVTPTEAAQ APEVTYEAEE GSLWTLLLTS LDGHLLEPDA EYLHWLLTNI
PGNRVAEGQV TCPYLPPFPA RGSGIHRLAF LLFKQDQPID FSEDARPSPC YQLAQRTFRT
FDFYKKHQET MTPAGLSFFQ CRWDDSVTYI FHQLLDMREP VFEFVRPPPY HPKQKRFPHR
QPLRYLDRYR DSHEPTYGIY
