RINI_HUMAN
ID RINI_HUMAN Reviewed; 461 AA.
AC P13489; Q8IZK8; Q96FD7; Q9BQ80; Q9UDK6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Ribonuclease inhibitor;
DE AltName: Full=Placental ribonuclease inhibitor;
DE Short=Placental RNase inhibitor;
DE AltName: Full=Ribonuclease/angiogenin inhibitor 1;
DE Short=RAI;
GN Name=RNH1; Synonyms=PRI, RNH;
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], PROTEIN SEQUENCE OF 20-28; 35-44; 47-62; 65-72;
RP 87-130; 147-181; 189-200; 206-226; 231-235; 239-268; 272-276; 288-295;
RP 297-299; 303-316; 353-364; 374-394; 402-412; 424-449 AND 453-461, AND
RP OXIDATION STATE OF THE CYSTEINES.
RC TISSUE=Placenta;
RX PubMed=3219362; DOI=10.1021/bi00423a007;
RA Lee F.S., Fox E.A., Zhou H.-M., Strydom D.J., Vallee B.L.;
RT "Primary structure of human placental ribonuclease inhibitor.";
RL Biochemistry 27:8545-8553(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 444-462.
RX PubMed=3243277; DOI=10.1002/j.1460-2075.1988.tb03310.x;
RA Schneider R., Schneider-Scherzer E., Thurnher M., Auer B., Schweiger M.;
RT "The primary structure of human ribonuclease/angiogenin inhibitor (RAI)
RT discloses a novel highly diversified protein superfamily with a common
RT repetitive module.";
RL EMBO J. 7:4151-4156(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=14515218;
RA Huang G.H., Yang G.Z., Chen J.Y., Wu X.F.;
RT "Expression of a human ribonuclease inhibitor variant in Escherichia coli
RT and silkworm insect cell (Bombyx mori).";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:960-963(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Colon, Lymph, and Ovary;
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 [6]
RP PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Brain;
RX PubMed=8037455; DOI=10.1006/abbi.1994.1328;
RA Nadano D., Yasuda T., Takeshita H., Uchide K., Kishi K.;
RT "Purification and characterization of human brain ribonuclease inhibitor.";
RL Arch. Biochem. Biophys. 312:421-428(1994).
RN [7]
RP PROTEIN SEQUENCE OF 174-195 AND 288-302, AND INTERACTION WITH RNASE1.
RX PubMed=1633192; DOI=10.1016/0167-4838(92)90134-y;
RA Crevel-Thieffry I., Cotterill S., Schuller E.;
RT "Characterisation of a tryptic peptide from human placental ribonuclease
RT inhibitor which inhibits ribonuclease activity.";
RL Biochim. Biophys. Acta 1122:107-112(1992).
RN [8]
RP MUTAGENESIS OF SER-461, AND INTERACTION WITH ANG AND RNASE1.
RX PubMed=9050852; DOI=10.1073/pnas.94.5.1761;
RA Chen C.Z., Shapiro R.;
RT "Site-specific mutagenesis reveals differences in the structural bases for
RT tight binding of RNase inhibitor to angiogenin and RNase A.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1761-1766(1997).
RN [9]
RP MUTAGENESIS OF 435-TYR-ASP-436, AND INTERACTION WITH ANG AND RNASE1.
RX PubMed=10413501; DOI=10.1021/bi990762a;
RA Chen C.Z., Shapiro R.;
RT "Superadditive and subadditive effects of 'hot spot' mutations within the
RT interfaces of placental ribonuclease inhibitor with angiogenin and
RT ribonuclease A.";
RL Biochemistry 38:9273-9285(1999).
RN [10]
RP FUNCTION, MUTAGENESIS OF TRP-262; TRP-264; TRP-319; 435-TYR-ASP-436 AND
RP SER-461, AND INTERACTION WITH RNASE2.
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 [11]
RP FUNCTION.
RX PubMed=17292889; DOI=10.1016/j.febslet.2007.01.072;
RA Monti D.M., Montesano Gesualdi N., Matousek J., Esposito F., D'Alessio G.;
RT "The cytosolic ribonuclease inhibitor contributes to intracellular redox
RT homeostasis.";
RL FEBS Lett. 581:930-934(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
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 [19]
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 [20]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-461 IN COMPLEX WITH ANG,
RP INTERACTION WITH ANG, AND DOMAIN.
RX PubMed=9311977; DOI=10.1093/emboj/16.17.5162;
RA Papageorgiou A.C., Shapiro R., Acharya K.R.;
RT "Molecular recognition of human angiogenin by placental ribonuclease
RT inhibitor -- an X-ray crystallographic study at 2.0-A resolution.";
RL EMBO J. 16:5162-5177(1997).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-461 IN COMPLEX WITH RNASE2,
RP DOMAIN, INTERACTION WITH RNASE2, AND MUTAGENESIS OF TRP-376 AND ARG-458.
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 [22]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RNASE1, DOMAIN, AND
RP INTERACTION WITH RNASE1.
RX PubMed=17350650; DOI=10.1016/j.jmb.2007.02.005;
RA Johnson R.J., McCoy J.G., Bingman C.A., Phillips G.N. Jr., Raines R.T.;
RT "Inhibition of human pancreatic ribonuclease by the human ribonuclease
RT inhibitor protein.";
RL J. Mol. Biol. 368:434-449(2007).
CC -!- FUNCTION: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG.
CC May play a role in redox homeostasis. {ECO:0000269|PubMed:12578357,
CC ECO:0000269|PubMed:14515218, ECO:0000269|PubMed:17292889}.
CC -!- SUBUNIT: Forms high-affinity heterodimers with RNASE1, ANG and RNASE2.
CC {ECO:0000269|PubMed:15755456, ECO:0000269|PubMed:17350650,
CC ECO:0000269|PubMed:9311977}.
CC -!- INTERACTION:
CC P13489; P03950: ANG; NbExp=3; IntAct=EBI-1237106, EBI-525291;
CC P13489; P07998: RNASE1; NbExp=8; IntAct=EBI-1237106, EBI-2823523;
CC P13489; O00560: SDCBP; NbExp=8; IntAct=EBI-1237106, EBI-727004;
CC P13489; O76024: WFS1; NbExp=3; IntAct=EBI-1237106, EBI-720609;
CC P13489; P61823: RNASE1; Xeno; NbExp=3; IntAct=EBI-1237106, EBI-908364;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: The LRR domain forms a horseshoe-shaped structure that
CC interacts tightly with target RNases via a large protein interaction
CC surface on its interior side. {ECO:0000269|PubMed:15755456,
CC ECO:0000269|PubMed:17350650, ECO:0000269|PubMed:9311977}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: At least 30 of the 32 cysteine residues are in the reduced form.
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DR EMBL; M22414; AAA59130.1; -; mRNA.
DR EMBL; M36717; AAA60249.1; -; mRNA.
DR EMBL; X13973; CAA32151.1; -; mRNA.
DR EMBL; AY071904; AAL60586.1; -; mRNA.
DR EMBL; AL161967; CAB82310.1; -; mRNA.
DR EMBL; BC000677; AAH00677.1; -; mRNA.
DR EMBL; BC003506; AAH03506.1; -; mRNA.
DR EMBL; BC011186; AAH11186.1; -; mRNA.
DR EMBL; BC011500; AAH11500.1; -; mRNA.
DR EMBL; BC014629; AAH14629.1; -; mRNA.
DR EMBL; BC024037; AAH24037.1; -; mRNA.
DR EMBL; BC047730; AAH47730.1; -; mRNA.
DR CCDS; CCDS7697.1; -.
DR PIR; A31858; A31858.
DR RefSeq; NP_002930.2; NM_002939.3.
DR RefSeq; NP_976317.1; NM_203383.1.
DR RefSeq; NP_976318.1; NM_203384.1.
DR RefSeq; NP_976319.1; NM_203385.1.
DR RefSeq; NP_976320.1; NM_203386.2.
DR RefSeq; NP_976321.1; NM_203387.2.
DR RefSeq; NP_976322.1; NM_203388.2.
DR RefSeq; NP_976323.1; NM_203389.2.
DR RefSeq; XP_011518557.1; XM_011520255.1.
DR RefSeq; XP_011518559.1; XM_011520257.2.
DR RefSeq; XP_011518560.1; XM_011520258.2.
DR RefSeq; XP_011518561.1; XM_011520259.2.
DR RefSeq; XP_011518562.1; XM_011520260.2.
DR RefSeq; XP_011518563.1; XM_011520261.2.
DR RefSeq; XP_011518564.1; XM_011520262.2.
DR RefSeq; XP_011518565.1; XM_011520263.1.
DR RefSeq; XP_016873595.1; XM_017018106.1.
DR PDB; 1A4Y; X-ray; 2.00 A; A/D=2-461.
DR PDB; 1Z7X; X-ray; 1.95 A; W/Y=1-461.
DR PDB; 2BEX; X-ray; 1.99 A; A/B=2-461.
DR PDB; 2Q4G; X-ray; 1.95 A; W/Y=1-461.
DR PDBsum; 1A4Y; -.
DR PDBsum; 1Z7X; -.
DR PDBsum; 2BEX; -.
DR PDBsum; 2Q4G; -.
DR AlphaFoldDB; P13489; -.
DR SMR; P13489; -.
DR BioGRID; 111977; 118.
DR CORUM; P13489; -.
DR IntAct; P13489; 54.
DR MINT; P13489; -.
DR STRING; 9606.ENSP00000433999; -.
DR GlyGen; P13489; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P13489; -.
DR PhosphoSitePlus; P13489; -.
DR SwissPalm; P13489; -.
DR BioMuta; RNH1; -.
DR DMDM; 132573; -.
DR REPRODUCTION-2DPAGE; IPI00550069; -.
DR EPD; P13489; -.
DR jPOST; P13489; -.
DR MassIVE; P13489; -.
DR MaxQB; P13489; -.
DR PaxDb; P13489; -.
DR PeptideAtlas; P13489; -.
DR PRIDE; P13489; -.
DR ProteomicsDB; 52913; -.
DR Antibodypedia; 22490; 474 antibodies from 31 providers.
DR DNASU; 6050; -.
DR Ensembl; ENST00000354420.7; ENSP00000346402.2; ENSG00000023191.17.
DR Ensembl; ENST00000356187.9; ENSP00000348515.5; ENSG00000023191.17.
DR Ensembl; ENST00000397604.7; ENSP00000380729.3; ENSG00000023191.17.
DR Ensembl; ENST00000397614.5; ENSP00000380738.1; ENSG00000023191.17.
DR Ensembl; ENST00000397615.6; ENSP00000380739.2; ENSG00000023191.17.
DR Ensembl; ENST00000438658.6; ENSP00000416589.2; ENSG00000023191.17.
DR Ensembl; ENST00000533410.5; ENSP00000435594.1; ENSG00000023191.17.
DR Ensembl; ENST00000534797.5; ENSP00000433999.1; ENSG00000023191.17.
DR Ensembl; ENST00000612988.4; ENSP00000479004.1; ENSG00000276230.4.
DR Ensembl; ENST00000617351.4; ENSP00000484572.1; ENSG00000276230.4.
DR Ensembl; ENST00000618184.3; ENSP00000478664.1; ENSG00000276230.4.
DR Ensembl; ENST00000619599.4; ENSP00000479966.1; ENSG00000276230.4.
DR Ensembl; ENST00000621211.2; ENSP00000480036.1; ENSG00000276230.4.
DR Ensembl; ENST00000632527.1; ENSP00000487940.1; ENSG00000276230.4.
DR Ensembl; ENST00000632954.1; ENSP00000487753.1; ENSG00000276230.4.
DR Ensembl; ENST00000633287.1; ENSP00000488734.1; ENSG00000276230.4.
DR GeneID; 6050; -.
DR KEGG; hsa:6050; -.
DR MANE-Select; ENST00000354420.7; ENSP00000346402.2; NM_203387.3; NP_976321.1.
DR UCSC; uc001lpk.1; human.
DR CTD; 6050; -.
DR DisGeNET; 6050; -.
DR GeneCards; RNH1; -.
DR HGNC; HGNC:10074; RNH1.
DR HPA; ENSG00000023191; Low tissue specificity.
DR MIM; 173320; gene.
DR neXtProt; NX_P13489; -.
DR OpenTargets; ENSG00000023191; -.
DR PharmGKB; PA34447; -.
DR VEuPathDB; HostDB:ENSG00000023191; -.
DR eggNOG; KOG4308; Eukaryota.
DR GeneTree; ENSGT00940000161492; -.
DR HOGENOM; CLU_002274_4_6_1; -.
DR InParanoid; P13489; -.
DR OMA; GGNDIHA; -.
DR OrthoDB; 710473at2759; -.
DR PhylomeDB; P13489; -.
DR PathwayCommons; P13489; -.
DR SignaLink; P13489; -.
DR BioGRID-ORCS; 6050; 64 hits in 1072 CRISPR screens.
DR ChiTaRS; RNH1; human.
DR EvolutionaryTrace; P13489; -.
DR GeneWiki; RNH1; -.
DR GenomeRNAi; 6050; -.
DR Pharos; P13489; Tbio.
DR PRO; PR:P13489; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P13489; protein.
DR Bgee; ENSG00000023191; Expressed in skin of leg and 98 other tissues.
DR ExpressionAtlas; P13489; baseline and differential.
DR Genevisible; P13489; HS.
DR GO; GO:0032311; C:angiogenin-PRI complex; IPI:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; NAS:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR041302; LRR_RI_cap.
DR Pfam; PF13516; LRR_6; 6.
DR Pfam; PF18779; LRR_RI_capping; 1.
DR SMART; SM00367; LRR_CC; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Leucine-rich repeat; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8037455,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..461
FT /note="Ribonuclease inhibitor"
FT /id="PRO_0000097343"
FT REPEAT 20..48
FT /note="LRR 1"
FT REPEAT 49..76
FT /note="LRR 2"
FT REPEAT 77..105
FT /note="LRR 3"
FT REPEAT 106..133
FT /note="LRR 4"
FT REPEAT 134..162
FT /note="LRR 5"
FT REPEAT 163..190
FT /note="LRR 6"
FT REPEAT 191..219
FT /note="LRR 7"
FT REPEAT 220..247
FT /note="LRR 8"
FT REPEAT 248..276
FT /note="LRR 9"
FT REPEAT 277..304
FT /note="LRR 10"
FT REPEAT 305..333
FT /note="LRR 11"
FT REPEAT 334..361
FT /note="LRR 12"
FT REPEAT 362..390
FT /note="LRR 13"
FT REPEAT 391..418
FT /note="LRR 14"
FT REPEAT 419..447
FT /note="LRR 15"
FT REGION 2..11
FT /note="2 X 5 AA tandem repeats of S-L-D-I-Q"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 82
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VARIANT 170
FT /note="P -> L (in dbSNP:rs17585)"
FT /id="VAR_014726"
FT MUTAGEN 262
FT /note="W->A: Binding affinity decreased 5000-fold over the
FT wild type for RNASE2; when associated with A-264 and A-
FT 319."
FT /evidence="ECO:0000269|PubMed:12578357"
FT MUTAGEN 264
FT /note="W->A: Substantially decreased binding affinity for
FT RNASE2. Binding affinity decreased 5000-fold over the wild
FT type for RNASE2; when associated with A-262 and A-319."
FT /evidence="ECO:0000269|PubMed:12578357"
FT MUTAGEN 319
FT /note="W->A: Substantially decreased binding affinity for
FT RNASE2. Binding affinity decreased 5000-fold over the wild
FT type for RNASE2; when associated with A-262 and A-264."
FT /evidence="ECO:0000269|PubMed:12578357"
FT MUTAGEN 376
FT /note="W->A: 40-fold reduction in binding affinity for
FT RNASE2."
FT /evidence="ECO:0000269|PubMed:15755456"
FT MUTAGEN 435..436
FT /note="YD->AA: Substantially decreases binding affinity for
FT RNASE1, ANG and RNASE2."
FT /evidence="ECO:0000269|PubMed:10413501,
FT ECO:0000269|PubMed:12578357"
FT MUTAGEN 458
FT /note="R->A: 25-fold reduction in binding affinity for
FT RNASE2."
FT /evidence="ECO:0000269|PubMed:15755456"
FT MUTAGEN 461
FT /note="Missing: A significant decrease in binding affinity
FT with RNASE1, slight decrease for the ANG ligand, no real
FT change in binding affinity for RNASE2."
FT /evidence="ECO:0000269|PubMed:12578357,
FT ECO:0000269|PubMed:9050852"
FT CONFLICT 188
FT /note="R -> H (in Ref. 5; AAH03506)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="R -> A (in Ref. 3; AAL60586)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="L -> P (in Ref. 3; AAL60586)"
FT /evidence="ECO:0000305"
FT CONFLICT 423..424
FT /note="RQ -> SE (in Ref. 2; CAA32151/AAA60249)"
FT /evidence="ECO:0000305"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:2Q4G"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 384..396
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 412..422
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:1Z7X"
FT HELIX 441..453
FT /evidence="ECO:0007829|PDB:1Z7X"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:1Z7X"
SQ SEQUENCE 461 AA; 49973 MW; 5E88CDAC95BAE5B3 CRC64;
MSLDIQSLDI QCEELSDARW AELLPLLQQC QVVRLDDCGL TEARCKDISS ALRVNPALAE
LNLRSNELGD VGVHCVLQGL QTPSCKIQKL SLQNCCLTGA GCGVLSSTLR TLPTLQELHL
SDNLLGDAGL QLLCEGLLDP QCRLEKLQLE YCSLSAASCE PLASVLRAKP DFKELTVSNN
DINEAGVRVL CQGLKDSPCQ LEALKLESCG VTSDNCRDLC GIVASKASLR ELALGSNKLG
DVGMAELCPG LLHPSSRLRT LWIWECGITA KGCGDLCRVL RAKESLKELS LAGNELGDEG
ARLLCETLLE PGCQLESLWV KSCSFTAACC SHFSSVLAQN RFLLELQISN NRLEDAGVRE
LCQGLGQPGS VLRVLWLADC DVSDSSCSSL AATLLANHSL RELDLSNNCL GDAGILQLVE
SVRQPGCLLE QLVLYDIYWS EEMEDRLQAL EKDKPSLRVI S
