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Ribonuclease inhibitor (Placental ribonuclease inhibitor) (Placental RNase inhibitor) (Ribonuclease/angiogenin inhibitor 1) (RAI)

 RINI_HUMAN              Reviewed;         461 AA.
P13489; Q8IZK8; Q96FD7; Q9BQ80; Q9UDK6;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-JUN-2018, entry version 201.
RecName: Full=Ribonuclease inhibitor;
AltName: Full=Placental ribonuclease inhibitor;
Short=Placental RNase inhibitor;
AltName: Full=Ribonuclease/angiogenin inhibitor 1;
Short=RAI;
Name=RNH1; Synonyms=PRI, RNH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-28; 35-44; 47-62;
65-72; 87-130; 147-181; 189-200; 206-226; 231-235; 239-268; 272-276;
288-295; 297-299; 303-316; 353-364; 374-394; 402-412; 424-449 AND
453-461, AND OXIDATION STATE OF THE CYSTEINES.
TISSUE=Placenta;
PubMed=3219362; DOI=10.1021/bi00423a007;
Lee F.S., Fox E.A., Zhou H.-M., Strydom D.J., Vallee B.L.;
"Primary structure of human placental ribonuclease inhibitor.";
Biochemistry 27:8545-8553(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 444-462.
PubMed=3243277;
Schneider R., Schneider-Scherzer E., Thurnher M., Auer B.,
Schweiger M.;
"The primary structure of human ribonuclease/angiogenin inhibitor
(RAI) discloses a novel highly diversified protein superfamily with a
common repetitive module.";
EMBO J. 7:4151-4156(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=14515218;
Huang G.H., Yang G.Z., Chen J.Y., Wu X.F.;
"Expression of a human ribonuclease inhibitor variant in Escherichia
coli and silkworm insect cell (Bombyx mori).";
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:960-963(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Colon, Lymph, and Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-14.
TISSUE=Brain;
PubMed=8037455; DOI=10.1006/abbi.1994.1328;
Nadano D., Yasuda T., Takeshita H., Uchide K., Kishi K.;
"Purification and characterization of human brain ribonuclease
inhibitor.";
Arch. Biochem. Biophys. 312:421-428(1994).
[7]
PROTEIN SEQUENCE OF 174-195 AND 288-302, AND INTERACTION WITH RNASE1.
PubMed=1633192; DOI=10.1016/0167-4838(92)90134-Y;
Crevel-Thieffry I., Cotterill S., Schuller E.;
"Characterisation of a tryptic peptide from human placental
ribonuclease inhibitor which inhibits ribonuclease activity.";
Biochim. Biophys. Acta 1122:107-112(1992).
[8]
MUTAGENESIS OF SER-461, AND INTERACTION WITH ANG AND RNASE1.
PubMed=9050852; DOI=10.1073/pnas.94.5.1761;
Chen C.Z., Shapiro R.;
"Site-specific mutagenesis reveals differences in the structural bases
for tight binding of RNase inhibitor to angiogenin and RNase A.";
Proc. Natl. Acad. Sci. U.S.A. 94:1761-1766(1997).
[9]
MUTAGENESIS OF 435-TYR-ASP-436, AND INTERACTION WITH ANG AND RNASE1.
PubMed=10413501; DOI=10.1021/bi990762a;
Chen C.Z., Shapiro R.;
"Superadditive and subadditive effects of 'hot spot' mutations within
the interfaces of placental ribonuclease inhibitor with angiogenin and
ribonuclease A.";
Biochemistry 38:9273-9285(1999).
[10]
FUNCTION, MUTAGENESIS OF TRP-262; TRP-264; TRP-319; 435-TYR-ASP-436
AND SER-461, AND INTERACTION WITH RNASE2.
PubMed=12578357; DOI=10.1021/bi026852o;
Teufel D.P., Kao R.Y., Acharya K.R., Shapiro R.;
"Mutational analysis of the complex of human RNase inhibitor and human
eosinophil-derived neurotoxin (RNase 2).";
Biochemistry 42:1451-1459(2003).
[11]
FUNCTION.
PubMed=17292889; DOI=10.1016/j.febslet.2007.01.072;
Monti D.M., Montesano Gesualdi N., Matousek J., Esposito F.,
D'Alessio G.;
"The cytosolic ribonuclease inhibitor contributes to intracellular
redox homeostasis.";
FEBS Lett. 581:930-934(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-461 IN COMPLEX WITH ANG,
INTERACTION WITH ANG, AND DOMAIN.
PubMed=9311977; DOI=10.1093/emboj/16.17.5162;
Papageorgiou A.C., Shapiro R., Acharya K.R.;
"Molecular recognition of human angiogenin by placental ribonuclease
inhibitor -- an X-ray crystallographic study at 2.0-A resolution.";
EMBO J. 16:5162-5177(1997).
[21]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-461 IN COMPLEX WITH RNASE2,
DOMAIN, INTERACTION WITH RNASE2, AND MUTAGENESIS OF TRP-376 AND
ARG-458.
PubMed=15755456; DOI=10.1016/j.jmb.2005.01.035;
Iyer S., Holloway D.E., Kumar K., Shapiro R., Acharya K.R.;
"Molecular recognition of human eosinophil-derived neurotoxin (RNase
2) by placental ribonuclease inhibitor.";
J. Mol. Biol. 347:637-655(2005).
[22]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RNASE1, DOMAIN,
AND INTERACTION WITH RNASE1.
PubMed=17350650; DOI=10.1016/j.jmb.2007.02.005;
Johnson R.J., McCoy J.G., Bingman C.A., Phillips G.N. Jr.,
Raines R.T.;
"Inhibition of human pancreatic ribonuclease by the human ribonuclease
inhibitor protein.";
J. Mol. Biol. 368:434-449(2007).
-!- FUNCTION: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and
ANG. May play a role in redox homeostasis.
{ECO:0000269|PubMed:12578357, ECO:0000269|PubMed:14515218,
ECO:0000269|PubMed:17292889}.
-!- SUBUNIT: Forms high-affinity heterodimers with RNASE1, ANG and
RNASE2. {ECO:0000269|PubMed:15755456, ECO:0000269|PubMed:17350650,
ECO:0000269|PubMed:9311977}.
-!- INTERACTION:
P03950:ANG; NbExp=2; IntAct=EBI-1237106, EBI-525291;
P07998:RNASE1; NbExp=2; IntAct=EBI-1237106, EBI-2823523;
P61823:RNASE1 (xeno); NbExp=3; IntAct=EBI-1237106, EBI-908364;
O00560:SDCBP; NbExp=5; IntAct=EBI-1237106, EBI-727004;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- DOMAIN: The LRR domain forms a horseshoe-shaped structure that
interacts tightly with target RNases via a large protein
interaction surface on its interior side.
{ECO:0000269|PubMed:15755456, ECO:0000269|PubMed:17350650,
ECO:0000269|PubMed:9311977}.
-!- PTM: The N-terminus is blocked.
-!- PTM: At least 30 of the 32 cysteine residues are in the reduced
form.
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EMBL; M22414; AAA59130.1; -; mRNA.
EMBL; M36717; AAA60249.1; -; mRNA.
EMBL; X13973; CAA32151.1; -; mRNA.
EMBL; AY071904; AAL60586.1; -; mRNA.
EMBL; AL161967; CAB82310.1; -; mRNA.
EMBL; BC000677; AAH00677.1; -; mRNA.
EMBL; BC003506; AAH03506.1; -; mRNA.
EMBL; BC011186; AAH11186.1; -; mRNA.
EMBL; BC011500; AAH11500.1; -; mRNA.
EMBL; BC014629; AAH14629.1; -; mRNA.
EMBL; BC024037; AAH24037.1; -; mRNA.
EMBL; BC047730; AAH47730.1; -; mRNA.
CCDS; CCDS7697.1; -.
PIR; A31858; A31858.
RefSeq; NP_002930.2; NM_002939.3.
RefSeq; NP_976317.1; NM_203383.1.
RefSeq; NP_976318.1; NM_203384.1.
RefSeq; NP_976319.1; NM_203385.1.
RefSeq; NP_976320.1; NM_203386.2.
RefSeq; NP_976321.1; NM_203387.2.
RefSeq; NP_976322.1; NM_203388.2.
RefSeq; NP_976323.1; NM_203389.2.
RefSeq; XP_011518557.1; XM_011520255.1.
RefSeq; XP_011518559.1; XM_011520257.2.
RefSeq; XP_011518560.1; XM_011520258.2.
RefSeq; XP_011518561.1; XM_011520259.2.
RefSeq; XP_011518562.1; XM_011520260.2.
RefSeq; XP_011518563.1; XM_011520261.2.
RefSeq; XP_011518564.1; XM_011520262.2.
RefSeq; XP_011518565.1; XM_011520263.1.
RefSeq; XP_016873595.1; XM_017018106.1.
UniGene; Hs.530687; -.
PDB; 1A4Y; X-ray; 2.00 A; A/D=2-461.
PDB; 1Z7X; X-ray; 1.95 A; W/Y=1-461.
PDB; 2BEX; X-ray; 1.99 A; A/B=2-461.
PDB; 2Q4G; X-ray; 1.95 A; W/Y=1-461.
PDBsum; 1A4Y; -.
PDBsum; 1Z7X; -.
PDBsum; 2BEX; -.
PDBsum; 2Q4G; -.
ProteinModelPortal; P13489; -.
SMR; P13489; -.
BioGrid; 111977; 68.
CORUM; P13489; -.
IntAct; P13489; 34.
MINT; P13489; -.
STRING; 9606.ENSP00000346402; -.
iPTMnet; P13489; -.
PhosphoSitePlus; P13489; -.
SwissPalm; P13489; -.
BioMuta; RNH1; -.
DMDM; 132573; -.
REPRODUCTION-2DPAGE; IPI00550069; -.
EPD; P13489; -.
MaxQB; P13489; -.
PaxDb; P13489; -.
PeptideAtlas; P13489; -.
PRIDE; P13489; -.
ProteomicsDB; 52913; -.
Ensembl; ENST00000354420; ENSP00000346402; ENSG00000023191.
Ensembl; ENST00000356187; ENSP00000348515; ENSG00000023191.
Ensembl; ENST00000397604; ENSP00000380729; ENSG00000023191.
Ensembl; ENST00000397614; ENSP00000380738; ENSG00000023191.
Ensembl; ENST00000397615; ENSP00000380739; ENSG00000023191.
Ensembl; ENST00000438658; ENSP00000416589; ENSG00000023191.
Ensembl; ENST00000533410; ENSP00000435594; ENSG00000023191.
Ensembl; ENST00000534797; ENSP00000433999; ENSG00000023191.
Ensembl; ENST00000612988; ENSP00000479004; ENSG00000276230.
Ensembl; ENST00000617351; ENSP00000484572; ENSG00000276230.
Ensembl; ENST00000618184; ENSP00000478664; ENSG00000276230.
Ensembl; ENST00000619599; ENSP00000479966; ENSG00000276230.
Ensembl; ENST00000621211; ENSP00000480036; ENSG00000276230.
Ensembl; ENST00000632527; ENSP00000487940; ENSG00000276230.
Ensembl; ENST00000632954; ENSP00000487753; ENSG00000276230.
Ensembl; ENST00000633287; ENSP00000488734; ENSG00000276230.
GeneID; 6050; -.
KEGG; hsa:6050; -.
UCSC; uc001lpk.1; human.
CTD; 6050; -.
DisGeNET; 6050; -.
EuPathDB; HostDB:ENSG00000023191.16; -.
GeneCards; RNH1; -.
HGNC; HGNC:10074; RNH1.
HPA; HPA039223; -.
HPA; HPA040781; -.
MIM; 173320; gene.
neXtProt; NX_P13489; -.
OpenTargets; ENSG00000023191; -.
PharmGKB; PA34447; -.
eggNOG; KOG4308; Eukaryota.
eggNOG; ENOG410ZBX3; LUCA.
GeneTree; ENSGT00900000140813; -.
HOGENOM; HOG000140402; -.
HOVERGEN; HBG001059; -.
InParanoid; P13489; -.
KO; K16634; -.
OMA; LWLWECD; -.
OrthoDB; EOG091G01CG; -.
PhylomeDB; P13489; -.
ChiTaRS; RNH1; human.
EvolutionaryTrace; P13489; -.
GeneWiki; RNH1; -.
GenomeRNAi; 6050; -.
PRO; PR:P13489; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000023191; -.
CleanEx; HS_RNH1; -.
ExpressionAtlas; P13489; baseline and differential.
Genevisible; P13489; HS.
GO; GO:0032311; C:angiogenin-PRI complex; IPI:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0008428; F:ribonuclease inhibitor activity; IDA:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; NAS:UniProtKB.
GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
InterPro; IPR032675; LRR_dom_sf.
Pfam; PF13516; LRR_6; 6.
SMART; SM00367; LRR_CC; 5.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Leucine-rich repeat; Phosphoprotein;
Polymorphism; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:8037455}.
CHAIN 2 461 Ribonuclease inhibitor.
/FTId=PRO_0000097343.
REPEAT 20 48 LRR 1.
REPEAT 49 76 LRR 2.
REPEAT 77 105 LRR 3.
REPEAT 106 133 LRR 4.
REPEAT 134 162 LRR 5.
REPEAT 163 190 LRR 6.
REPEAT 191 219 LRR 7.
REPEAT 220 247 LRR 8.
REPEAT 248 276 LRR 9.
REPEAT 277 304 LRR 10.
REPEAT 305 333 LRR 11.
REPEAT 334 361 LRR 12.
REPEAT 362 390 LRR 13.
REPEAT 391 418 LRR 14.
REPEAT 419 447 LRR 15.
REGION 2 11 2 X 5 AA tandem repeats of S-L-D-I-Q.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 82 82 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
VARIANT 170 170 P -> L (in dbSNP:rs17585).
/FTId=VAR_014726.
MUTAGEN 262 262 W->A: Binding affinity decreased 5000-
fold over the wild type for RNASE2; when
associated with A-264 and A-319.
{ECO:0000269|PubMed:12578357}.
MUTAGEN 264 264 W->A: Substantially decreased binding
affinity for RNASE2. Binding affinity
decreased 5000-fold over the wild type
for RNASE2; when associated with A-262
and A-319. {ECO:0000269|PubMed:12578357}.
MUTAGEN 319 319 W->A: Substantially decreased binding
affinity for RNASE2. Binding affinity
decreased 5000-fold over the wild type
for RNASE2; when associated with A-262
and A-264. {ECO:0000269|PubMed:12578357}.
MUTAGEN 376 376 W->A: 40-fold reduction in binding
affinity for RNASE2.
{ECO:0000269|PubMed:15755456}.
MUTAGEN 435 436 YD->AA: Substantially decreases binding
affinity for RNASE1, ANG and RNASE2.
{ECO:0000269|PubMed:10413501,
ECO:0000269|PubMed:12578357}.
MUTAGEN 458 458 R->A: 25-fold reduction in binding
affinity for RNASE2.
{ECO:0000269|PubMed:15755456}.
MUTAGEN 461 461 Missing: A significant decrease in
binding affinity with RNASE1, slight
decrease for the ANG ligand, no real
change in binding affinity for RNASE2.
{ECO:0000269|PubMed:12578357,
ECO:0000269|PubMed:9050852}.
CONFLICT 188 188 R -> H (in Ref. 5; AAH03506).
{ECO:0000305}.
CONFLICT 359 359 R -> A (in Ref. 3; AAL60586).
{ECO:0000305}.
CONFLICT 365 365 L -> P (in Ref. 3; AAL60586).
{ECO:0000305}.
CONFLICT 423 424 RQ -> SE (in Ref. 2; CAA32151/AAA60249).
{ECO:0000305}.
STRAND 3 12 {ECO:0000244|PDB:1Z7X}.
HELIX 17 27 {ECO:0000244|PDB:1Z7X}.
STRAND 31 38 {ECO:0000244|PDB:1Z7X}.
HELIX 42 53 {ECO:0000244|PDB:1Z7X}.
STRAND 60 62 {ECO:0000244|PDB:1Z7X}.
HELIX 69 78 {ECO:0000244|PDB:1Z7X}.
STRAND 89 91 {ECO:0000244|PDB:1Z7X}.
HELIX 99 101 {ECO:0000244|PDB:1Z7X}.
HELIX 102 108 {ECO:0000244|PDB:1Z7X}.
STRAND 117 119 {ECO:0000244|PDB:1Z7X}.
STRAND 122 124 {ECO:0000244|PDB:1Z7X}.
HELIX 126 137 {ECO:0000244|PDB:1Z7X}.
STRAND 146 148 {ECO:0000244|PDB:1Z7X}.
HELIX 156 158 {ECO:0000244|PDB:1Z7X}.
HELIX 159 168 {ECO:0000244|PDB:1Z7X}.
STRAND 174 176 {ECO:0000244|PDB:1Z7X}.
STRAND 179 181 {ECO:0000244|PDB:1Z7X}.
HELIX 183 196 {ECO:0000244|PDB:1Z7X}.
STRAND 203 205 {ECO:0000244|PDB:1Z7X}.
HELIX 215 225 {ECO:0000244|PDB:1Z7X}.
STRAND 231 233 {ECO:0000244|PDB:1Z7X}.
STRAND 236 238 {ECO:0000244|PDB:1Z7X}.
HELIX 240 251 {ECO:0000244|PDB:1Z7X}.
STRAND 260 262 {ECO:0000244|PDB:1Z7X}.
HELIX 270 282 {ECO:0000244|PDB:1Z7X}.
STRAND 288 290 {ECO:0000244|PDB:1Z7X}.
HELIX 297 308 {ECO:0000244|PDB:1Z7X}.
STRAND 310 312 {ECO:0000244|PDB:2Q4G}.
STRAND 317 319 {ECO:0000244|PDB:1Z7X}.
HELIX 327 329 {ECO:0000244|PDB:1Z7X}.
HELIX 330 339 {ECO:0000244|PDB:1Z7X}.
STRAND 345 347 {ECO:0000244|PDB:1Z7X}.
STRAND 350 352 {ECO:0000244|PDB:1Z7X}.
HELIX 354 365 {ECO:0000244|PDB:1Z7X}.
STRAND 374 376 {ECO:0000244|PDB:1Z7X}.
HELIX 384 396 {ECO:0000244|PDB:1Z7X}.
STRAND 402 404 {ECO:0000244|PDB:1Z7X}.
STRAND 407 409 {ECO:0000244|PDB:1Z7X}.
HELIX 412 422 {ECO:0000244|PDB:1Z7X}.
STRAND 431 433 {ECO:0000244|PDB:1Z7X}.
HELIX 441 453 {ECO:0000244|PDB:1Z7X}.
STRAND 457 460 {ECO:0000244|PDB:1Z7X}.
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


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