RNAS2_HUMAN
ID RNAS2_HUMAN Reviewed; 161 AA.
AC P10153; Q52M39; Q9H2B7; Q9UCG7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Non-secretory ribonuclease;
DE EC=4.6.1.18 {ECO:0000250|UniProtKB:P47784};
DE AltName: Full=Eosinophil-derived neurotoxin;
DE AltName: Full=RNase UpI-2;
DE AltName: Full=Ribonuclease 2;
DE Short=RNase 2;
DE AltName: Full=Ribonuclease US;
DE Flags: Precursor;
GN Name=RNASE2; Synonyms=EDN, RNS2;
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].
RX PubMed=2591744; DOI=10.1016/0378-1119(89)90414-9;
RA Hamann K.J., Barker R.L., Loegering D.A., Pease L.R., Gleich G.J.;
RT "Sequence of human eosinophil-derived neurotoxin cDNA: identity of deduced
RT amino acid sequence with human nonsecretory ribonucleases.";
RL Gene 83:161-167(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2745977;
RA Barker R.L., Loegering D.A., Ten R.M., Hamann K.J., Pease L.R.,
RA Gleich G.J.;
RT "Eosinophil cationic protein cDNA. Comparison with other toxic cationic
RT proteins and ribonucleases.";
RL J. Immunol. 143:952-955(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2734298; DOI=10.1073/pnas.86.12.4460;
RA Rosenberg H.F., Tenen D.G., Ackerman S.J.;
RT "Molecular cloning of the human eosinophil-derived neurotoxin: a member of
RT the ribonuclease gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4460-4464(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2387583; DOI=10.1016/0888-7543(90)90197-3;
RA Hamann K.J., Ten R.M., Loegering D.A., Jenkins R.B., Heise M.T.,
RA Schad C.R., Pease L.R., Gleich G.J., Barker R.L.;
RT "Structure and chromosome localization of the human eosinophil-derived
RT neurotoxin and eosinophil cationic protein genes: evidence for intronless
RT coding sequences in the ribonuclease gene superfamily.";
RL Genomics 7:535-546(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-156.
RX PubMed=11102386; DOI=10.1093/genetics/156.4.1949;
RA Zhang J., Rosenberg H.F.;
RT "Sequence variation at two eosinophil-associated ribonuclease loci in
RT humans.";
RL Genetics 156:1949-1958(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Colon, and Leukemia;
RA Simonsen C.C., Kennedy J., Comstock L., Ashton N., McGrogan M.;
RL Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP PROTEIN SEQUENCE OF 28-161.
RX PubMed=3166997; DOI=10.1021/bi00412a046;
RA Beintema J.J., Hofsteenge J., Iwama M., Morita T., Ohgi K., Irie M.,
RA Sugiyama R.H., Schieven G.L., Dekker C.A., Glitz D.G.;
RT "Amino acid sequence of the nonsecretory ribonuclease of human urine.";
RL Biochemistry 27:4530-4538(1988).
RN [9]
RP PROTEIN SEQUENCE OF 28-82, AND FUNCTION.
RX PubMed=3458170; DOI=10.1073/pnas.83.10.3146;
RA Gleich G.J., Loegering D.A., Bell M.P., Checkel J.L., Ackerman S.J.,
RA McKean D.J.;
RT "Biochemical and functional similarities between human eosinophil-derived
RT neurotoxin and eosinophil cationic protein: homology with ribonuclease.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3146-3150(1986).
RN [10]
RP PROTEIN SEQUENCE OF 28-55.
RX PubMed=3926759; DOI=10.1093/oxfordjournals.jbchem.a135134;
RA Niwata Y., Ohgi K., Sanda A., Takizawa Y., Irie M.;
RT "Purification and properties of bovine kidney ribonucleases.";
RL J. Biochem. 97:923-934(1985).
RN [11]
RP PROTEIN SEQUENCE OF 28-53.
RC TISSUE=Liver;
RX PubMed=3182786; DOI=10.1016/s0021-9258(18)37567-7;
RA Sorrentino S., Tucker G.K., Glitz D.G.;
RT "Purification and characterization of a ribonuclease from human liver.";
RL J. Biol. Chem. 263:16125-16131(1988).
RN [12]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Urine;
RX PubMed=1587793; DOI=10.1093/oxfordjournals.jbchem.a123757;
RA Sakakibara R., Hashida K., Kitahara T., Ishiguro M.;
RT "Characterization of a unique nonsecretory ribonuclease from urine of
RT pregnant women.";
RL J. Biochem. 111:325-330(1992).
RN [13]
RP PROTEIN SEQUENCE OF 28-45.
RC TISSUE=Urine;
RX PubMed=8471426; DOI=10.1038/bjc.1993.127;
RA Kardana A., Bagshawe K.D., Coles B., Read D., Taylor M.;
RT "Characterisation of UGP and its relationship with beta-core fragment.";
RL Br. J. Cancer 67:686-692(1993).
RN [14]
RP GLYCOSYLATION AT TRP-34.
RX PubMed=7947762; DOI=10.1021/bi00250a003;
RA Hofsteenge J., Mueller D.R., de Beer T., Loeffler A., Richter W.J.,
RA Vliegenthart J.F.G.;
RT "New type of linkage between a carbohydrate and a protein: C-glycosylation
RT of a specific tryptophan residue in human RNase Us.";
RL Biochemistry 33:13524-13530(1994).
RN [15]
RP STRUCTURE OF C-GLYCOSYLATED GROUP.
RX PubMed=7547911; DOI=10.1021/bi00037a016;
RA de Beer T., Vliegenthart J.F.G., Loeffler A., Hofsteenge J.;
RT "The hexopyranosyl residue that is C-glycosidically linked to the side
RT chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.";
RL Biochemistry 34:11785-11789(1995).
RN [16]
RP GLYCOSYLATION AT TRP-34.
RX PubMed=9450956; DOI=10.1091/mbc.9.2.301;
RA Krieg J., Hartmann S., Vicentini A., Glasner W., Hess D., Hofsteenge J.;
RT "Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of
RT sequence Trp-x-x-Trp.";
RL Mol. Biol. Cell 9:301-309(1998).
RN [17]
RP FUNCTION, AND INTERACTION WITH RNH1.
RX PubMed=12578357; DOI=10.1021/bi026852o;
RA Teufel D.P., Kao R.Y., Acharya K.R., Shapiro R.;
RT "Mutational analysis of the complex of human RNase inhibitor and human
RT eosinophil-derived neurotoxin (RNase 2).";
RL Biochemistry 42:1451-1459(2003).
RN [18]
RP INVOLVEMENT IN CHEMOTAXIS.
RX PubMed=12855582; DOI=10.1182/blood-2003-01-0151;
RA Yang D., Rosenberg H.F., Chen Q., Dyer K.D., Kurosaka K., Oppenheim J.J.;
RT "Eosinophil-derived neurotoxin (EDN), an antimicrobial protein with
RT chemotactic activities for dendritic cells.";
RL Blood 102:3396-3403(2003).
RN [19]
RP NITRATION AT TYR-60.
RX PubMed=18694936; DOI=10.1074/jbc.m801196200;
RA Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M.,
RA Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N., Acharya K.R.,
RA Schmid-Grendelmeier P., Simon H.-U., Schwarz H., Tsutsui M., Shimokawa H.,
RA Bellon G., Lee J.J., Przybylski M., Doering G.;
RT "Post-translational tyrosine nitration of eosinophil granule toxins
RT mediated by eosinophil peroxidase.";
RL J. Biol. Chem. 283:28629-28640(2008).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
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 [22]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
RX PubMed=8759319; DOI=10.1006/jmbi.1996.0420;
RA Mosimann S.C., Newton D.L., Youle R.J., James M.N.G.;
RT "X-ray crystallographic structure of recombinant eosinophil-derived
RT neurotoxin at 1.83-A resolution.";
RL J. Mol. Biol. 260:540-552(1996).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=11154698; DOI=10.1074/jbc.m010585200;
RA Leonidas D.D., Boix E., Prill R., Suzuki M., Turton R., Minson K.,
RA Swaminathan G.J., Youle R.J., Acharya K.R.;
RT "Mapping the ribonucleolytic active site of eosinophil-derived neurotoxin
RT (EDN). High resolution crystal structures of EDN complexes with adenylic
RT nucleotide inhibitors.";
RL J. Biol. Chem. 276:15009-15017(2001).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 28-161 IN COMPLEX WITH RNH1, AND
RP SUBUNIT.
RX PubMed=15755456; DOI=10.1016/j.jmb.2005.01.035;
RA Iyer S., Holloway D.E., Kumar K., Shapiro R., Acharya K.R.;
RT "Molecular recognition of human eosinophil-derived neurotoxin (RNase 2) by
RT placental ribonuclease inhibitor.";
RL J. Mol. Biol. 347:637-655(2005).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) OF 28-161 IN COMPLEX WITH ADP AND
RP ATP.
RX PubMed=16401072; DOI=10.1021/bi0518592;
RA Baker M.D., Holloway D.E., Swaminathan G.J., Acharya K.R.;
RT "Crystal structures of eosinophil-derived neurotoxin (EDN) in complex with
RT the inhibitors 5'-ATP, Ap3A, Ap4A, and Ap5A.";
RL Biochemistry 45:416-426(2006).
CC -!- FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine
CC specific nuclease with a slight preference for U. Cytotoxin and
CC helminthotoxin. Selectively chemotactic for dendritic cells. Possesses
CC a wide variety of biological activities. {ECO:0000269|PubMed:12578357,
CC ECO:0000269|PubMed:3458170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-
CC phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
CC Evidence={ECO:0000250|UniProtKB:P47784};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-
CC phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
CC Evidence={ECO:0000250|UniProtKB:P47784};
CC -!- SUBUNIT: Interacts with and forms a tight 1:1 complex with RNH1.
CC Dimerization of two such complexes may occur.
CC {ECO:0000269|PubMed:12578357, ECO:0000269|PubMed:15755456,
CC ECO:0000269|PubMed:16401072}.
CC -!- INTERACTION:
CC P10153; Q15700: DLG2; NbExp=3; IntAct=EBI-12286629, EBI-80426;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. Cytoplasmic granule.
CC Note=Matrix of eosinophil's large specific granule.
CC -!- TISSUE SPECIFICITY: Liver, lung, spleen, leukocytes and body fluids.
CC -!- DOMAIN: The N-terminal region is necessary for mediating chemotactic
CC activity.
CC -!- PTM: A particular signal processing and glycosylation pattern may
CC differentiate the UpI2 RNase, found specifically in pregnant women
CC urine, from other nonsecretory RNases. {ECO:0000269|PubMed:7947762,
CC ECO:0000269|PubMed:9450956}.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M30510; AAC82505.1; -; mRNA.
DR EMBL; M28129; AAA50284.1; -; mRNA.
DR EMBL; M24157; AAA52337.1; -; mRNA.
DR EMBL; X16546; CAA34546.1; -; Genomic_DNA.
DR EMBL; AF294007; AAG31577.1; -; Genomic_DNA.
DR EMBL; AF294008; AAG31578.1; -; Genomic_DNA.
DR EMBL; AF294009; AAG31579.1; -; Genomic_DNA.
DR EMBL; AF294010; AAG31580.1; -; Genomic_DNA.
DR EMBL; AF294011; AAG31581.1; -; Genomic_DNA.
DR EMBL; AF294012; AAG31582.1; -; Genomic_DNA.
DR EMBL; AF294013; AAG31583.1; -; Genomic_DNA.
DR EMBL; AF294014; AAG31584.1; -; Genomic_DNA.
DR EMBL; AF294015; AAG31585.1; -; Genomic_DNA.
DR EMBL; X55987; CAA39459.1; -; Genomic_DNA.
DR EMBL; X55988; CAA39460.1; -; mRNA.
DR EMBL; BC093678; AAH93678.1; -; mRNA.
DR EMBL; BC093680; AAH93680.1; -; mRNA.
DR EMBL; BC096059; AAH96059.1; -; mRNA.
DR CCDS; CCDS9561.1; -.
DR PIR; A35328; A33922.
DR RefSeq; NP_002925.1; NM_002934.2.
DR PDB; 1GQV; X-ray; 0.98 A; A=28-161.
DR PDB; 1HI2; X-ray; 1.60 A; A=28-161.
DR PDB; 1HI3; X-ray; 1.80 A; A=28-161.
DR PDB; 1HI4; X-ray; 1.80 A; A=28-161.
DR PDB; 1HI5; X-ray; 1.80 A; A=28-161.
DR PDB; 1K2A; X-ray; 1.00 A; A=26-160.
DR PDB; 2BEX; X-ray; 1.99 A; C/D=28-161.
DR PDB; 2BZZ; X-ray; 0.98 A; A=28-161.
DR PDB; 2C01; X-ray; 1.24 A; X=28-161.
DR PDB; 2C02; X-ray; 2.00 A; A=28-161.
DR PDB; 2C05; X-ray; 1.86 A; A=28-161.
DR PDB; 5E13; X-ray; 1.34 A; A=1-161.
DR PDB; 6SSO; X-ray; 1.21 A; A=27-161.
DR PDBsum; 1GQV; -.
DR PDBsum; 1HI2; -.
DR PDBsum; 1HI3; -.
DR PDBsum; 1HI4; -.
DR PDBsum; 1HI5; -.
DR PDBsum; 1K2A; -.
DR PDBsum; 2BEX; -.
DR PDBsum; 2BZZ; -.
DR PDBsum; 2C01; -.
DR PDBsum; 2C02; -.
DR PDBsum; 2C05; -.
DR PDBsum; 5E13; -.
DR PDBsum; 6SSO; -.
DR AlphaFoldDB; P10153; -.
DR SMR; P10153; -.
DR BioGRID; 111965; 11.
DR ELM; P10153; -.
DR IntAct; P10153; 3.
DR STRING; 9606.ENSP00000303276; -.
DR BindingDB; P10153; -.
DR ChEMBL; CHEMBL5120; -.
DR DrugBank; DB01812; Adenosine 3',5'-diphosphate.
DR DrugBank; DB02098; Adenosine-2'-5'-Diphosphate.
DR GlyConnect; 436; 3 N-Linked glycans.
DR GlyGen; P10153; 7 sites, 1 C-linked glycan (2 sites), 4 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P10153; -.
DR PhosphoSitePlus; P10153; -.
DR BioMuta; RNASE2; -.
DR DMDM; 133168; -.
DR EPD; P10153; -.
DR jPOST; P10153; -.
DR MassIVE; P10153; -.
DR PaxDb; P10153; -.
DR PeptideAtlas; P10153; -.
DR PRIDE; P10153; -.
DR ProteomicsDB; 52573; -.
DR Antibodypedia; 22074; 169 antibodies from 21 providers.
DR DNASU; 6036; -.
DR Ensembl; ENST00000304625.3; ENSP00000303276.2; ENSG00000169385.3.
DR GeneID; 6036; -.
DR KEGG; hsa:6036; -.
DR MANE-Select; ENST00000304625.3; ENSP00000303276.2; NM_002934.3; NP_002925.1.
DR CTD; 6036; -.
DR DisGeNET; 6036; -.
DR GeneCards; RNASE2; -.
DR HGNC; HGNC:10045; RNASE2.
DR HPA; ENSG00000169385; Tissue enriched (bone).
DR MIM; 131410; gene.
DR neXtProt; NX_P10153; -.
DR OpenTargets; ENSG00000169385; -.
DR PharmGKB; PA34413; -.
DR VEuPathDB; HostDB:ENSG00000169385; -.
DR eggNOG; ENOG502TF52; Eukaryota.
DR GeneTree; ENSGT00940000162253; -.
DR HOGENOM; CLU_117006_0_1_1; -.
DR InParanoid; P10153; -.
DR OMA; MFYIVAC; -.
DR OrthoDB; 1482425at2759; -.
DR PhylomeDB; P10153; -.
DR TreeFam; TF333393; -.
DR PathwayCommons; P10153; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P10153; -.
DR SIGNOR; P10153; -.
DR BioGRID-ORCS; 6036; 6 hits in 1037 CRISPR screens.
DR ChiTaRS; RNASE2; human.
DR EvolutionaryTrace; P10153; -.
DR GeneWiki; Eosinophil-derived_neurotoxin; -.
DR GenomeRNAi; 6036; -.
DR Pharos; P10153; Tchem.
DR PRO; PR:P10153; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P10153; protein.
DR Bgee; ENSG00000169385; Expressed in trabecular bone tissue and 127 other tissues.
DR ExpressionAtlas; P10153; baseline and differential.
DR Genevisible; P10153; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004522; F:ribonuclease A activity; IEA:UniProtKB-EC.
DR GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; IBA:GO_Central.
DR GO; GO:0006401; P:RNA catabolic process; TAS:ProtInc.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:UniProtKB.
DR Gene3D; 3.10.130.10; -; 1.
DR InterPro; IPR001427; RNaseA.
DR InterPro; IPR036816; RNaseA-like_dom_sf.
DR InterPro; IPR023411; RNaseA_AS.
DR InterPro; IPR023412; RNaseA_domain.
DR PANTHER; PTHR11437; PTHR11437; 1.
DR Pfam; PF00074; RnaseA; 1.
DR PRINTS; PR00794; RIBONUCLEASE.
DR SMART; SM00092; RNAse_Pc; 1.
DR SUPFAM; SSF54076; SSF54076; 1.
DR PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Direct protein sequencing; Disulfide bond;
KW Endonuclease; Glycoprotein; Hydrolase; Lyase; Lysosome; Nitration;
KW Nuclease; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:3166997,
FT ECO:0000269|PubMed:3182786, ECO:0000269|PubMed:3458170,
FT ECO:0000269|PubMed:3926759, ECO:0000269|PubMed:8471426"
FT CHAIN 28..161
FT /note="Non-secretory ribonuclease"
FT /id="PRO_0000030874"
FT ACT_SITE 42
FT /note="Proton acceptor"
FT ACT_SITE 156
FT /note="Proton donor"
FT BINDING 65..69
FT /ligand="substrate"
FT MOD_RES 60
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000269|PubMed:18694936"
FT CARBOHYD 34
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:7947762,
FT ECO:0000269|PubMed:9450956"
FT /id="CAR_000004"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 50..110
FT DISULFID 64..123
FT DISULFID 82..138
FT DISULFID 89..98
FT VARIANT 100
FT /note="H -> Q (in dbSNP:rs8012891)"
FT /id="VAR_059820"
FT VARIANT 156
FT /note="H -> N (in dbSNP:rs146887874)"
FT /evidence="ECO:0000269|PubMed:11102386"
FT /id="VAR_013150"
FT CONFLICT 37
FT /note="W -> R (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 39..40
FT /note="ET -> QE (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="T -> V (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="S -> T (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:1GQV"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1GQV"
FT HELIX 50..61
FT /evidence="ECO:0007829|PDB:1GQV"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:1GQV"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:1GQV"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1GQV"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:1GQV"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1GQV"
FT STRAND 124..140
FT /evidence="ECO:0007829|PDB:1GQV"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1GQV"
FT STRAND 151..161
FT /evidence="ECO:0007829|PDB:1GQV"
SQ SEQUENCE 161 AA; 18354 MW; 9406C4596CA69038 CRC64;
MVPKLFTSQI CLLLLLGLLA VEGSLHVKPP QFTWAQWFET QHINMTSQQC TNAMQVINNY
QRRCKNQNTF LLTTFANVVN VCGNPNMTCP SNKTRKNCHH SGSQVPLIHC NLTTPSPQNI
SNCRYAQTPA NMFYIVACDN RDQRRDPPQY PVVPVHLDRI I
