EXOS7_HUMAN
ID EXOS7_HUMAN Reviewed; 291 AA.
AC Q15024; Q96E72;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Exosome complex component RRP42;
DE AltName: Full=Exosome component 7;
DE AltName: Full=Ribosomal RNA-processing protein 42;
DE AltName: Full=p8;
GN Name=EXOSC7; Synonyms=KIAA0116, RRP42;
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 GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-274.
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-291, AND VARIANT LEU-274.
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [4]
RP PROTEIN SEQUENCE OF 2-23, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE RNA EXOSOME
RP CORE COMPLEX.
RX PubMed=11719186; DOI=10.1016/s0092-8674(01)00578-5;
RA Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R., Pruijn G.J.M.,
RA Stoecklin G., Moroni C., Mann M., Karin M.;
RT "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs.";
RL Cell 107:451-464(2001).
RN [6]
RP PROTEIN INTERACTION.
RX PubMed=12419256; DOI=10.1016/s0022-2836(02)00947-6;
RA Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.;
RT "Protein-protein interactions between human exosome components support the
RT assembly of RNase PH-type subunits into a six-membered PNPase-like ring.";
RL J. Mol. Biol. 323:653-663(2002).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EXOSC1.
RX PubMed=11812149; DOI=10.1006/jmbi.2001.5265;
RA Raijmakers R., Noordman Y.E., van Venrooij W.J., Pruijn G.J.M.;
RT "Protein-protein interactions of hCsl4p with other human exosome
RT subunits.";
RL J. Mol. Biol. 315:809-818(2002).
RN [8]
RP PROTEIN INTERACTION.
RX PubMed=15231747; DOI=10.1101/gr.2122004;
RA Lehner B., Sanderson C.M.;
RT "A protein interaction framework for human mRNA degradation.";
RL Genome Res. 14:1315-1323(2004).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION IN THE RNA EXOSOME COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=20531389; DOI=10.1038/emboj.2010.122;
RA Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G.,
RA Heck A.J., Raijmakers R., Pruijn G.J.;
RT "Dis3-like 1: a novel exoribonuclease associated with the human exosome.";
RL EMBO J. 29:2358-2367(2010).
RN [12]
RP INTERACTION WITH ZC3HAV1.
RX PubMed=21876179; DOI=10.1073/pnas.1101676108;
RA Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T.,
RA Gao G.;
RT "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively
RT targeting multiply spliced viral mRNAs for degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), LACK OF CATALYTIC ACTIVITY, AND
RP RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
RX PubMed=17174896; DOI=10.1016/j.cell.2006.10.037;
RA Liu Q., Greimann J.C., Lima C.D.;
RT "Reconstitution, activities, and structure of the eukaryotic RNA exosome.";
RL Cell 127:1223-1237(2006).
RN [16]
RP ERRATUM OF PUBMED:17174896.
RA Liu Q., Greimann J.C., Lima C.D.;
RL Cell 131:188-189(2007).
RN [17] {ECO:0007744|PDB:6D6Q, ECO:0007744|PDB:6D6R}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS), AND SUBUNIT.
RX PubMed=29906447; DOI=10.1016/j.cell.2018.05.041;
RA Weick E.M., Puno M.R., Januszyk K., Zinder J.C., DiMattia M.A., Lima C.D.;
RT "Helicase-Dependent RNA Decay Illuminated by a Cryo-EM Structure of a Human
RT Nuclear RNA Exosome-MTR4 Complex.";
RL Cell 173:1663-1677.e21(2018).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-274, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Non-catalytic component of the RNA exosome complex which has
CC 3'->5' exoribonuclease activity and participates in a multitude of
CC cellular RNA processing and degradation events. In the nucleus, the RNA
CC exosome complex is involved in proper maturation of stable RNA species
CC such as rRNA, snRNA and snoRNA, in the elimination of RNA processing
CC by-products and non-coding 'pervasive' transcripts, such as antisense
CC RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs
CC with processing defects, thereby limiting or excluding their export to
CC the cytoplasm. The RNA exosome may be involved in Ig class switch
CC recombination (CSR) and/or Ig variable region somatic hypermutation
CC (SHM) by targeting AICDA deamination activity to transcribed dsDNA
CC substrates. In the cytoplasm, the RNA exosome complex is involved in
CC general mRNA turnover and specifically degrades inherently unstable
CC mRNAs containing AU-rich elements (AREs) within their 3' untranslated
CC regions, and in RNA surveillance pathways, preventing translation of
CC aberrant mRNAs. It seems to be involved in degradation of histone mRNA.
CC The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9)
CC is proposed to play a pivotal role in the binding and presentation of
CC RNA for ribonucleolysis, and to serve as a scaffold for the association
CC with catalytic subunits and accessory proteins or complexes.
CC -!- SUBUNIT: Component of the RNA exosome complex (PubMed:29906447).
CC Specifically part of the catalytically inactive RNA exosome core (Exo-
CC 9) complex which is believed to associate with catalytic subunits
CC EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA
CC exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH
CC domain-containing subunits specifically containing the heterodimers
CC EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1
CC domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the
CC top of the ring structure. Interacts with EXOSC1. Interacts with
CC ZC3HAV1. {ECO:0000269|PubMed:11719186, ECO:0000269|PubMed:11812149,
CC ECO:0000269|PubMed:20531389, ECO:0000269|PubMed:21876179,
CC ECO:0000269|PubMed:29906447}.
CC -!- INTERACTION:
CC Q15024; P62508-3: ESRRG; NbExp=3; IntAct=EBI-371841, EBI-12001340;
CC Q15024; Q9Y3B2: EXOSC1; NbExp=9; IntAct=EBI-371841, EBI-371892;
CC Q15024; Q13868: EXOSC2; NbExp=7; IntAct=EBI-371841, EBI-301735;
CC Q15024; Q9NPD3: EXOSC4; NbExp=6; IntAct=EBI-371841, EBI-371823;
CC Q15024; Q92551: IP6K1; NbExp=6; IntAct=EBI-371841, EBI-751911;
CC Q15024; P61086: UBE2K; NbExp=3; IntAct=EBI-371841, EBI-473850;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11812149}.
CC Cytoplasm {ECO:0000305|PubMed:11812149}. Nucleus
CC {ECO:0000305|PubMed:11812149}.
CC -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
CC -!- CAUTION: The six exosome core subunits containing a RNase PH-domain are
CC not phosphorolytically active. {ECO:0000305}.
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DR EMBL; AC104165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012831; AAH12831.1; -; mRNA.
DR EMBL; D29958; BAA06226.1; -; mRNA.
DR CCDS; CCDS2725.1; -.
DR RefSeq; NP_055819.2; NM_015004.3.
DR PDB; 2NN6; X-ray; 3.35 A; E=1-291.
DR PDB; 6D6Q; EM; 3.45 A; E=1-291.
DR PDB; 6D6R; EM; 3.45 A; E=1-291.
DR PDB; 6H25; EM; 3.80 A; E=1-291.
DR PDBsum; 2NN6; -.
DR PDBsum; 6D6Q; -.
DR PDBsum; 6D6R; -.
DR PDBsum; 6H25; -.
DR AlphaFoldDB; Q15024; -.
DR SMR; Q15024; -.
DR BioGRID; 116658; 121.
DR ComplexPortal; CPX-476; Nuclear exosome complex, DIS3-EXOSC10 variant.
DR ComplexPortal; CPX-591; Nucleolar exosome complex, EXOSC10 variant.
DR ComplexPortal; CPX-592; Cytoplasmic exosome complex, DIS3L variant.
DR ComplexPortal; CPX-593; Exosome complex, DIS3 variant.
DR ComplexPortal; CPX-600; Cytoplasmic exosome complex, DIS3L-EXOSC10 variant.
DR CORUM; Q15024; -.
DR DIP; DIP-31266N; -.
DR IntAct; Q15024; 47.
DR MINT; Q15024; -.
DR STRING; 9606.ENSP00000265564; -.
DR MoonDB; Q15024; Predicted.
DR GlyGen; Q15024; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15024; -.
DR PhosphoSitePlus; Q15024; -.
DR SwissPalm; Q15024; -.
DR BioMuta; EXOSC7; -.
DR DMDM; 322510129; -.
DR SWISS-2DPAGE; Q15024; -.
DR EPD; Q15024; -.
DR jPOST; Q15024; -.
DR MassIVE; Q15024; -.
DR MaxQB; Q15024; -.
DR PaxDb; Q15024; -.
DR PeptideAtlas; Q15024; -.
DR PRIDE; Q15024; -.
DR ProteomicsDB; 60375; -.
DR Antibodypedia; 12600; 297 antibodies from 27 providers.
DR DNASU; 23016; -.
DR Ensembl; ENST00000265564.8; ENSP00000265564.7; ENSG00000075914.13.
DR GeneID; 23016; -.
DR KEGG; hsa:23016; -.
DR MANE-Select; ENST00000265564.8; ENSP00000265564.7; NM_015004.4; NP_055819.2.
DR UCSC; uc003coi.3; human.
DR CTD; 23016; -.
DR DisGeNET; 23016; -.
DR GeneCards; EXOSC7; -.
DR HGNC; HGNC:28112; EXOSC7.
DR HPA; ENSG00000075914; Low tissue specificity.
DR MIM; 606488; gene.
DR neXtProt; NX_Q15024; -.
DR OpenTargets; ENSG00000075914; -.
DR PharmGKB; PA134880567; -.
DR VEuPathDB; HostDB:ENSG00000075914; -.
DR eggNOG; KOG1612; Eukaryota.
DR GeneTree; ENSGT00950000183130; -.
DR HOGENOM; CLU_038194_4_0_1; -.
DR InParanoid; Q15024; -.
DR OMA; PESVFEM; -.
DR OrthoDB; 965225at2759; -.
DR PhylomeDB; Q15024; -.
DR TreeFam; TF320641; -.
DR PathwayCommons; Q15024; -.
DR Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress.
DR Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease.
DR Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q15024; -.
DR SIGNOR; Q15024; -.
DR BioGRID-ORCS; 23016; 737 hits in 1082 CRISPR screens.
DR ChiTaRS; EXOSC7; human.
DR EvolutionaryTrace; Q15024; -.
DR GenomeRNAi; 23016; -.
DR Pharos; Q15024; Tbio.
DR PRO; PR:Q15024; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q15024; protein.
DR Bgee; ENSG00000075914; Expressed in oocyte and 211 other tissues.
DR ExpressionAtlas; Q15024; baseline and differential.
DR Genevisible; Q15024; HS.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:0000178; C:exosome (RNase complex); IDA:UniProtKB.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0101019; C:nucleolar exosome (RNase complex); IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; TAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:UniProtKB.
DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IBA:GO_Central.
DR GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
DR GO; GO:0006401; P:RNA catabolic process; IDA:ComplexPortal.
DR GO; GO:0006396; P:RNA processing; IDA:ComplexPortal.
DR GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; TAS:UniProtKB.
DR GO; GO:0034473; P:U1 snRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0034476; P:U5 snRNA 3'-end processing; IBA:GO_Central.
DR Gene3D; 3.30.230.70; -; 1.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR Pfam; PF01138; RNase_PH; 1.
DR Pfam; PF03725; RNase_PH_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55666; SSF55666; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Exosome;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..291
FT /note="Exosome complex component RRP42"
FT /id="PRO_0000139963"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 169
FT /note="R -> Q (in dbSNP:rs34512144)"
FT /id="VAR_032765"
FT VARIANT 274
FT /note="V -> L (in dbSNP:rs6794)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7788527, ECO:0007744|PubMed:21269460"
FT /id="VAR_014923"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:2NN6"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:2NN6"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:6D6Q"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6D6Q"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:2NN6"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:2NN6"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6D6Q"
FT STRAND 201..213
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2NN6"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 249..278
FT /evidence="ECO:0007829|PDB:2NN6"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:6D6Q"
SQ SEQUENCE 291 AA; 31821 MW; A674F745CEC61BBB CRC64;
MASVTLSEAE KVYIVHGVQE DLRVDGRGCE DYRCVEVETD VVSNTSGSAR VKLGHTDILV
GVKAEMGTPK LEKPNEGYLE FFVDCSASAT PEFEGRGGDD LGTEIANTLY RIFNNKSSVD
LKTLCISPRE HCWVLYVDVL LLECGGNLFD AISIAVKAAL FNTRIPRVRV LEDEEGSKDI
ELSDDPYDCI RLSVENVPCI VTLCKIGYRH VVDATLQEEA CSLASLLVSV TSKGVVTCMR
KVGKGSLDPE SIFEMMETGK RVGKVLHASL QSVVHKEESL GPKRQKVGFL G
