ID   RT35_HUMAN              Reviewed;         323 AA.
AC   P82673; Q32LZ1; Q6P4C6; Q7L1M6; Q8NBP4; Q96AI0; Q9H044; Q9HC14; Q9P1R5;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Small ribosomal subunit protein mS35 {ECO:0000303|PubMed:25838379};
DE   AltName: Full=28S ribosomal protein S28, mitochondrial;
DE            Short=MRP-S28;
DE            Short=S28mt;
DE   AltName: Full=28S ribosomal protein S35, mitochondrial;
DE            Short=MRP-S35;
DE            Short=S35mt;
DE   Flags: Precursor;
GN   Name=MRPS35 {ECO:0000312|HGNC:HGNC:16635};
GN   Synonyms=MRPS28 {ECO:0000303|PubMed:11344316};
GN   ORFNames=HDCMD11P, MDS023, PSEC0213;
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] {ECO:0000305, ECO:0000312|EMBL:AAG14958.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hematopoietic stem cell;
RA   Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.;
RT   "Novel genes expressed in hematopoietic stem/progenitor cells from
RT   myelodysplastic syndrome patients.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Teratocarcinoma;
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 1).
RC   TISSUE=Embryo;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [4] {ECO:0000305, ECO:0000312|EMBL:AAI09373.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon {ECO:0000312|EMBL:AAH17086.1}, Lung
RC   {ECO:0000312|EMBL:AAH63515.1}, and Pancreas
RC   {ECO:0000312|EMBL:AAH28346.2};
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 [LARGE SCALE MRNA] OF 47-323 (ISOFORM 1).
RC   TISSUE=Melanoma;
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   [6] {ECO:0000305, ECO:0000312|EMBL:AAG14958.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 180-323 (ISOFORM 1).
RC   TISSUE=Dendritic cell {ECO:0000312|EMBL:AAF65185.1};
RA   Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT   "A novel gene from human dendritic cells.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000305}
RP   IDENTIFICATION.
RX   PubMed=11344316; DOI=10.1110/ps.35301;
RA   Koc E.C., Burkhart W., Blackburn K., Koc H., Moseley A., Spremulli L.L.;
RT   "Identification of four proteins from the small subunit of the mammalian
RT   mitochondrial ribosome using a proteomics approach.";
RL   Protein Sci. 10:471-481(2001).
RN   [8]
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   [9]
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   [10]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
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).
CC   -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt-
CC       SSU). Mature mammalian 55S mitochondrial ribosomes consist of a small
CC       (28S) and a large (39S) subunit. The 28S small subunit contains a 12S
CC       ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large
CC       subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial
CC       valine transfer RNA (mt-tRNA(Val)), which plays an integral structural
CC       role, and 52 different proteins. {ECO:0000269|PubMed:25838379}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000305};
CC         IsoId=P82673-1; Sequence=Displayed;
CC       Name=2 {ECO:0000305};
CC         IsoId=P82673-2; Sequence=VSP_054096, VSP_054097;
CC   -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC       mS35 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG14958.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF182422; AAG14958.1; ALT_FRAME; mRNA.
DR   EMBL; AK075378; BAC11579.1; -; mRNA.
DR   EMBL; AK075515; BAC11664.1; -; mRNA.
DR   EMBL; BC015862; AAH15862.2; -; mRNA.
DR   EMBL; BC017086; AAH17086.1; -; mRNA.
DR   EMBL; BC028346; AAH28346.2; -; mRNA.
DR   EMBL; BC063515; AAH63515.1; -; mRNA.
DR   EMBL; BC109372; AAI09373.1; -; mRNA.
DR   EMBL; AL512733; CAC21665.1; -; mRNA.
DR   EMBL; AF068296; AAF65185.1; -; mRNA.
DR   CCDS; CCDS53769.1; -. [P82673-2]
DR   CCDS; CCDS8714.1; -. [P82673-1]
DR   RefSeq; NP_001177793.1; NM_001190864.1. [P82673-2]
DR   RefSeq; NP_068593.2; NM_021821.3. [P82673-1]
DR   PDB; 3J9M; EM; 3.50 A; A1=1-323.
DR   PDB; 6NU2; EM; 3.90 A; A1=52-323.
DR   PDB; 6NU3; EM; 4.40 A; A1=1-323.
DR   PDB; 6RW4; EM; 2.97 A; 1=1-323.
DR   PDB; 6RW5; EM; 3.14 A; 1=1-323.
DR   PDB; 6VLZ; EM; 2.97 A; A1=1-323.
DR   PDB; 6VMI; EM; 2.96 A; A1=1-323.
DR   PDB; 6ZM5; EM; 2.89 A; A1=1-323.
DR   PDB; 6ZM6; EM; 2.59 A; A1=1-323.
DR   PDB; 6ZS9; EM; 4.00 A; A1=1-323.
DR   PDB; 6ZSA; EM; 4.00 A; A1=1-323.
DR   PDB; 6ZSB; EM; 4.50 A; A1=1-323.
DR   PDB; 6ZSC; EM; 3.50 A; A1=1-323.
DR   PDB; 6ZSD; EM; 3.70 A; A1=1-323.
DR   PDB; 6ZSE; EM; 5.00 A; A1=1-323.
DR   PDB; 6ZSG; EM; 4.00 A; A1=1-323.
DR   PDB; 7A5F; EM; 4.40 A; b6=1-323.
DR   PDB; 7A5G; EM; 4.33 A; b6=1-323.
DR   PDB; 7A5I; EM; 3.70 A; b6=1-323.
DR   PDB; 7A5K; EM; 3.70 A; b6=1-323.
DR   PDB; 7L08; EM; 3.49 A; A1=1-323.
DR   PDB; 7OG4; EM; 3.80 A; A1=1-323.
DR   PDB; 7P2E; EM; 2.40 A; 1=1-323.
DR   PDB; 7PNX; EM; 2.76 A; 1=1-323.
DR   PDB; 7PNY; EM; 3.06 A; 1=1-323.
DR   PDB; 7PNZ; EM; 3.09 A; 1=1-323.
DR   PDB; 7PO0; EM; 2.90 A; 1=1-323.
DR   PDB; 7PO1; EM; 2.92 A; 1=1-323.
DR   PDB; 7PO2; EM; 3.09 A; 1=1-323.
DR   PDB; 7PO3; EM; 2.92 A; 1=1-323.
DR   PDB; 7QI4; EM; 2.21 A; A1=1-323.
DR   PDB; 7QI5; EM; 2.63 A; A1=1-323.
DR   PDB; 7QI6; EM; 2.98 A; A1=1-323.
DR   PDB; 8ANY; EM; 2.85 A; A1=1-323.
DR   PDB; 8CSP; EM; 2.66 A; 1=1-323.
DR   PDB; 8CSQ; EM; 2.54 A; 1=1-323.
DR   PDB; 8CSR; EM; 2.54 A; 1=1-323.
DR   PDB; 8CSS; EM; 2.36 A; 1=1-323.
DR   PDB; 8CST; EM; 2.85 A; 1=1-323.
DR   PDB; 8CSU; EM; 3.03 A; 1=1-323.
DR   PDB; 8OIR; EM; 3.10 A; AB=1-323.
DR   PDB; 8OIS; EM; 3.00 A; AB=1-323.
DR   PDBsum; 3J9M; -.
DR   PDBsum; 6NU2; -.
DR   PDBsum; 6NU3; -.
DR   PDBsum; 6RW4; -.
DR   PDBsum; 6RW5; -.
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; 7A5I; -.
DR   PDBsum; 7A5K; -.
DR   PDBsum; 7L08; -.
DR   PDBsum; 7OG4; -.
DR   PDBsum; 7P2E; -.
DR   PDBsum; 7PNX; -.
DR   PDBsum; 7PNY; -.
DR   PDBsum; 7PNZ; -.
DR   PDBsum; 7PO0; -.
DR   PDBsum; 7PO1; -.
DR   PDBsum; 7PO2; -.
DR   PDBsum; 7PO3; -.
DR   PDBsum; 7QI4; -.
DR   PDBsum; 7QI5; -.
DR   PDBsum; 7QI6; -.
DR   PDBsum; 8ANY; -.
DR   PDBsum; 8CSP; -.
DR   PDBsum; 8CSQ; -.
DR   PDBsum; 8CSR; -.
DR   PDBsum; 8CSS; -.
DR   PDBsum; 8CST; -.
DR   PDBsum; 8CSU; -.
DR   PDBsum; 8OIR; -.
DR   PDBsum; 8OIS; -.
DR   AlphaFoldDB; P82673; -.
DR   EMDB; EMD-0514; -.
DR   EMDB; EMD-0515; -.
DR   EMDB; EMD-10021; -.
DR   EMDB; EMD-10022; -.
DR   EMDB; EMD-11278; -.
DR   EMDB; EMD-11279; -.
DR   EMDB; EMD-11390; -.
DR   EMDB; EMD-11391; -.
DR   EMDB; EMD-11392; -.
DR   EMDB; EMD-11393; -.
DR   EMDB; EMD-11394; -.
DR   EMDB; EMD-11395; -.
DR   EMDB; EMD-11397; -.
DR   EMDB; EMD-11641; -.
DR   EMDB; EMD-11642; -.
DR   EMDB; EMD-11644; -.
DR   EMDB; EMD-11646; -.
DR   EMDB; EMD-12877; -.
DR   EMDB; EMD-13170; -.
DR   EMDB; EMD-13555; -.
DR   EMDB; EMD-13556; -.
DR   EMDB; EMD-13557; -.
DR   EMDB; EMD-13558; -.
DR   EMDB; EMD-13559; -.
DR   EMDB; EMD-13560; -.
DR   EMDB; EMD-13561; -.
DR   EMDB; EMD-13980; -.
DR   EMDB; EMD-13981; -.
DR   EMDB; EMD-13982; -.
DR   EMDB; EMD-15544; -.
DR   EMDB; EMD-16897; -.
DR   EMDB; EMD-16898; -.
DR   EMDB; EMD-21233; -.
DR   EMDB; EMD-21242; -.
DR   EMDB; EMD-23096; -.
DR   EMDB; EMD-26966; -.
DR   EMDB; EMD-26967; -.
DR   EMDB; EMD-26968; -.
DR   EMDB; EMD-26969; -.
DR   EMDB; EMD-26970; -.
DR   EMDB; EMD-26971; -.
DR   SMR; P82673; -.
DR   BioGRID; 121919; 315.
DR   ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR   CORUM; P82673; -.
DR   IntAct; P82673; 108.
DR   MINT; P82673; -.
DR   STRING; 9606.ENSP00000081029; -.
DR   GlyGen; P82673; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P82673; -.
DR   MetOSite; P82673; -.
DR   PhosphoSitePlus; P82673; -.
DR   BioMuta; MRPS35; -.
DR   DMDM; 74708095; -.
DR   EPD; P82673; -.
DR   jPOST; P82673; -.
DR   MassIVE; P82673; -.
DR   MaxQB; P82673; -.
DR   PaxDb; 9606-ENSP00000081029; -.
DR   PeptideAtlas; P82673; -.
DR   ProteomicsDB; 57712; -. [P82673-1]
DR   ProteomicsDB; 57713; -. [P82673-2]
DR   Pumba; P82673; -.
DR   Antibodypedia; 24450; 148 antibodies from 25 providers.
DR   DNASU; 60488; -.
DR   Ensembl; ENST00000081029.8; ENSP00000081029.3; ENSG00000061794.13. [P82673-1]
DR   Ensembl; ENST00000538315.5; ENSP00000445390.1; ENSG00000061794.13. [P82673-2]
DR   GeneID; 60488; -.
DR   KEGG; hsa:60488; -.
DR   MANE-Select; ENST00000081029.8; ENSP00000081029.3; NM_021821.4; NP_068593.2.
DR   UCSC; uc001rih.4; human. [P82673-1]
DR   AGR; HGNC:16635; -.
DR   CTD; 60488; -.
DR   DisGeNET; 60488; -.
DR   GeneCards; MRPS35; -.
DR   HGNC; HGNC:16635; MRPS35.
DR   HPA; ENSG00000061794; Low tissue specificity.
DR   MIM; 611995; gene.
DR   neXtProt; NX_P82673; -.
DR   OpenTargets; ENSG00000061794; -.
DR   PharmGKB; PA31022; -.
DR   VEuPathDB; HostDB:ENSG00000061794; -.
DR   eggNOG; KOG3933; Eukaryota.
DR   GeneTree; ENSGT00390000003443; -.
DR   HOGENOM; CLU_060973_0_1_1; -.
DR   InParanoid; P82673; -.
DR   OMA; TTDYCQS; -.
DR   OrthoDB; 2913023at2759; -.
DR   PhylomeDB; P82673; -.
DR   TreeFam; TF318686; -.
DR   PathwayCommons; P82673; -.
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; P82673; -.
DR   SIGNOR; P82673; -.
DR   BioGRID-ORCS; 60488; 436 hits in 1172 CRISPR screens.
DR   ChiTaRS; MRPS35; human.
DR   GeneWiki; MRPS35; -.
DR   GenomeRNAi; 60488; -.
DR   Pharos; P82673; Tdark.
DR   PRO; PR:P82673; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P82673; Protein.
DR   Bgee; ENSG00000061794; Expressed in rectum and 204 other cell types or tissues.
DR   ExpressionAtlas; P82673; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005763; C:mitochondrial small ribosomal subunit; ISS: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:0032543; P:mitochondrial translation; NAS:ComplexPortal.
DR   InterPro; IPR019349; Ribosomal_mS35_mit.
DR   InterPro; IPR039848; Ribosomal_mS35_mt.
DR   PANTHER; PTHR13490:SF0; 28S RIBOSOMAL PROTEIN S35, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13490; MITOCHONDRIAL 28S RIBOSOMAL PROTEIN S28; 1.
DR   Pfam; PF10213; MRP-S28; 1.
DR   Genevisible; P82673; HS.
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..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..323
FT                   /note="Small ribosomal subunit protein mS35"
FT                   /id="PRO_0000046055"
FT   REGION          31..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          257..321
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        43..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         176..194
FT                   /note="KLSSLNLDDHAKKKLIKLV -> PFKEAELRLCSVSTNSVIP (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054096"
FT   VAR_SEQ         195..323
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054097"
FT   VARIANT         6
FT                   /note="L -> I (in dbSNP:rs35475802)"
FT                   /id="VAR_052051"
FT   HELIX           56..59
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           116..125
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           126..129
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           140..146
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          149..157
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           166..169
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          171..176
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           177..179
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           184..194
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   TURN            200..203
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          204..209
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           215..233
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           239..242
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   TURN            245..247
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:8CST"
FT   HELIX           257..272
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   TURN            280..285
FT                   /evidence="ECO:0007829|PDB:8CSP"
FT   HELIX           287..301
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           306..320
FT                   /evidence="ECO:0007829|PDB:8CSS"
SQ   SEQUENCE   323 AA;  36844 MW;  B29F819E914F2B49 CRC64;
     MAAAALPAWL SLQSRARTLR AFSTAVYSAT PVPTPSLPER TPGNERPPRR KALPPRTEKM
     AVDQDWPSVY PVAAPFKPSA VPLPVRMGYP VKKGVPMAKE GNLELLKIPN FLHLTPVAIK
     KHCEALKDFC TEWPAALDSD EKCEKHFPIE IDSTDYVSSG PSVRNPRARV VVLRVKLSSL
     NLDDHAKKKL IKLVGERYCK TTDVLTIKTD RCPLRRQNYD YAVYLLTVLY HESWNTEEWE
     KSKTEADMEE YIWENSSSER NILETLLQMK AAEKNMEINK EELLGTKEIE EYKKSVVSLK
     NEEENENSIS QYKESVKRLL NVT
//