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Ribonuclease pancreatic (EC 3.1.27.5) (HP-RNase) (RIB-1) (RNase UpI-1) (Ribonuclease 1) (RNase 1) (Ribonuclease A) (RNase A)

 RNAS1_HUMAN             Reviewed;         156 AA.
P07998; B2R589; D3DS06; Q16830; Q16869; Q1KHR2; Q6ICS5; Q9UCB4;
Q9UCB5;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 4.
05-DEC-2018, entry version 190.
RecName: Full=Ribonuclease pancreatic;
EC=3.1.27.5;
AltName: Full=HP-RNase;
AltName: Full=RIB-1;
AltName: Full=RNase UpI-1;
AltName: Full=Ribonuclease 1;
Short=RNase 1;
AltName: Full=Ribonuclease A;
Short=RNase A;
Flags: Precursor;
Name=RNASE1; Synonyms=RIB1, RNS1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
PubMed=8049276; DOI=10.1016/0167-4781(94)90208-9;
Seno M., Fatami J.I., Kosaka M., Seno S., Yamada H.;
"Nucleotide sequence encoding human pancreatic ribonuclease.";
Biochim. Biophys. Acta 1218:466-468(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16751256; DOI=10.1093/molbev/msl025;
Schienman J.E., Holt R.A., Auerbach M.R., Stewart C.B.;
"Duplication and divergence of two distinct pancreatic ribonuclease
genes in leaf-eating African and Asian colobine monkeys.";
Mol. Biol. Evol. 23:1465-1479(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas, and Prostate;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152.
TISSUE=Placenta;
PubMed=8588814;
Kochetov A.V., Lukasheva V.V., Filipenko M.L., Mertvetsov N.P.,
Rivkin M.I.;
"Primary structure of the coding part of the gene for human pancreatic
ribonuclease and its chromosomal location.";
Bioorg. Khim. 21:691-694(1995).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-155.
PubMed=7649283; DOI=10.1016/0014-5793(95)96890-G;
Russo N., de Nigris M., Ciardiello A., Di Donato A., D'Alessio G.;
"Expression in mammalian cells, purification and characterization of
recombinant human pancreatic ribonuclease.";
FEBS Lett. 369:352-352(1995).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-149.
TISSUE=Placenta;
PubMed=1741299; DOI=10.1093/nar/20.3.612;
Haugg M., Schein C.H.;
"The DNA sequences of the human and hamster secretory ribonucleases
determined with the polymerase chain reaction (PCR).";
Nucleic Acids Res. 20:612-612(1992).
[10]
PROTEIN SEQUENCE OF 29-156.
TISSUE=Pancreas;
PubMed=6201087; DOI=10.1016/0003-2697(84)90306-3;
Beintema J.J., Wietzes P., Weickmann J.L., Glitz D.G.;
"The amino acid sequence of human pancreatic ribonuclease.";
Anal. Biochem. 136:48-64(1984).
[11]
PROTEIN SEQUENCE OF 29-156, AND GLYCOSYLATION AT ASN-62; ASN-104 AND
ASN-116.
PubMed=3202829;
Beintema J.J., Blank A., Schieven G.L., Dekker C.A., Sorrentino S.,
Libonati M.;
"Differences in glycosylation pattern of human secretory
ribonucleases.";
Biochem. J. 255:501-505(1988).
[12]
PROTEIN SEQUENCE OF 29-47.
PubMed=2383019; DOI=10.1016/0003-9861(90)90424-W;
Mizuta K., Awazu S., Yasuda T., Kishi K.;
"Purification and characterization of three ribonucleases from human
kidney: comparison with urine ribonucleases.";
Arch. Biochem. Biophys. 281:144-151(1990).
[13]
PROTEIN SEQUENCE OF 29-43.
PubMed=2049798; DOI=10.1248/cpb.39.146;
Sakakibara R., Hashida K., Tominaga N., Sakai K., Ishiguro M.,
Imamura S., Ohmatsu F., Sato E.;
"A putative mouse oocyte maturation inhibitory protein from urine of
pregnant women: N-terminal sequence homology with human nonsecretory
ribonuclease.";
Chem. Pharm. Bull. 39:146-149(1991).
[14]
PROTEIN SEQUENCE OF 29-48.
TISSUE=Urine;
PubMed=1587793;
Sakakibara R., Hashida K., Kitahara T., Ishiguro M.;
"Characterization of a unique nonsecretory ribonuclease from urine of
pregnant women.";
J. Biochem. 111:325-330(1992).
[15]
PROTEIN SEQUENCE OF 29-49.
PubMed=8280059; DOI=10.1042/bj2960617;
Yasuda T., Nadano D., Takeshita H., Kishi K.;
"Two distinct secretory ribonucleases from human cerebrum:
purification, characterization and relationships to other
ribonucleases.";
Biochem. J. 296:617-625(1993).
[16]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 29-156, AND MUTAGENESIS OF
116-ASN-GLY-117.
PubMed=11021969; DOI=10.1006/jmbi.2000.4506;
Pous J., Canals A., Terzyan S.S., Guasch A., Benito A., Ribo M.,
Vilanova M., Coll M.;
"Three-dimensional structure of a human pancreatic ribonuclease
variant, a step forward in the design of cytotoxic ribonucleases.";
J. Mol. Biol. 303:49-60(2000).
[17]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-156.
PubMed=11264578; DOI=10.1107/S0907444901001147;
Pous J., Mallorqui-Fernandez G., Peracaula R., Terzyan S.S.,
Futami J., Tada H., Yamada H., Seno M., de Llorens R.,
Gomis-Rueth F.-X., Coll M.;
"Three-dimensional structure of human RNase 1 delta N7 at 1.9 A
resolution.";
Acta Crystallogr. D 57:498-505(2001).
[18]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-156, AND DISULFIDE BONDS.
PubMed=11591351; DOI=10.1016/S0969-2126(01)00659-1;
Canals A., Pous J., Guasch A., Benito A., Ribo M., Vilanova M.,
Coll M.;
"The structure of an engineered domain-swapped ribonuclease dimer and
its implications for the evolution of proteins toward
oligomerization.";
Structure 9:967-976(2001).
[19]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 29-156 IN COMPLEX WITH RNH1,
FUNCTION, SUBUNIT, INTERACTION WITH RNH1, DISULFIDE BONDS, AND
MUTAGENESIS OF ARG-67; ASN-95; ASN-116; GLY-117 AND ARG-119.
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).
[20]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 29-156, AND DISULFIDE BONDS.
PubMed=17586772; DOI=10.1110/ps.072851407;
Yamada H., Tamada T., Kosaka M., Miyata K., Fujiki S., Tano M.,
Moriya M., Yamanishi M., Honjo E., Tada H., Ino T., Yamaguchi H.,
Futami J., Seno M., Nomoto T., Hirata T., Yoshimura M., Kuroki R.;
"'Crystal lattice engineering,' an approach to engineer protein
crystal contacts by creating intermolecular symmetry: crystallization
and structure determination of a mutant human RNase 1 with a
hydrophobic interface of leucines.";
Protein Sci. 16:1389-1397(2007).
-!- FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the
3' side of pyrimidine nucleotides. Acts on single-stranded and
double-stranded RNA. {ECO:0000269|PubMed:17350650}.
-!- CATALYTIC ACTIVITY:
Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and
3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic
phosphate intermediates.; EC=3.1.27.5;
-!- SUBUNIT: Monomer. Interacts with and forms tight 1:1 complexes
with RNH1. Dimerization of two such complexes may occur.
Interaction with RNH1 inhibits this protein.
{ECO:0000269|PubMed:17350650}.
-!- INTERACTION:
P13489:RNH1; NbExp=6; IntAct=EBI-2823523, EBI-1237106;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Pancreas and other tissues and body fluids
(indicating it may have other physiological functions besides its
role in digestion).
-!- PTM: N-linked glycans are of complex type.
{ECO:0000269|PubMed:3202829}.
-!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
{ECO:0000305}.
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EMBL; D26129; BAA05124.1; -; mRNA.
EMBL; DQ494867; ABF00144.1; -; Genomic_DNA.
EMBL; AK312100; BAG35036.1; -; mRNA.
EMBL; CR450318; CAG29314.1; -; mRNA.
EMBL; CH471078; EAW66437.1; -; Genomic_DNA.
EMBL; CH471078; EAW66438.1; -; Genomic_DNA.
EMBL; BC005324; AAH05324.1; -; mRNA.
EMBL; BC022882; AAH22882.1; -; mRNA.
EMBL; X79235; CAA55817.1; -; Genomic_DNA.
EMBL; S79281; AAB35096.1; -; mRNA.
EMBL; X62946; CAA44718.1; -; Genomic_DNA.
CCDS; CCDS9559.1; -.
PIR; I53530; I53530.
PIR; S45003; NRHU1.
RefSeq; NP_002924.1; NM_002933.4.
RefSeq; NP_937875.1; NM_198232.2.
RefSeq; NP_937877.1; NM_198234.2.
RefSeq; NP_937878.1; NM_198235.2.
UniGene; Hs.78224; -.
PDB; 1DZA; X-ray; 1.65 A; A/B=28-156.
PDB; 1E21; X-ray; 1.90 A; A=29-156.
PDB; 1H8X; X-ray; 2.00 A; A/B=29-156.
PDB; 1Z7X; X-ray; 1.95 A; X/Z=29-156.
PDB; 2E0J; X-ray; 1.60 A; A/B=29-156.
PDB; 2E0L; X-ray; 1.60 A; A/B=29-156.
PDB; 2E0M; X-ray; 1.70 A; A/B=29-156.
PDB; 2E0O; X-ray; 2.00 A; A/B=29-156.
PDB; 2K11; NMR; -; A=29-155.
PDB; 2Q4G; X-ray; 1.95 A; X/Z=29-156.
PDB; 3F8G; X-ray; 2.60 A; A/B=29-153.
PDB; 4KXH; X-ray; 2.70 A; A/B/C/D=29-156.
PDBsum; 1DZA; -.
PDBsum; 1E21; -.
PDBsum; 1H8X; -.
PDBsum; 1Z7X; -.
PDBsum; 2E0J; -.
PDBsum; 2E0L; -.
PDBsum; 2E0M; -.
PDBsum; 2E0O; -.
PDBsum; 2K11; -.
PDBsum; 2Q4G; -.
PDBsum; 3F8G; -.
PDBsum; 4KXH; -.
ProteinModelPortal; P07998; -.
SMR; P07998; -.
BioGrid; 111964; 5.
IntAct; P07998; 7.
MINT; P07998; -.
STRING; 9606.ENSP00000344193; -.
BindingDB; P07998; -.
ChEMBL; CHEMBL5425; -.
DrugBank; DB03765; 2'-cytidylic acid.
DrugBank; DB03448; 2'-Deoxyuridine 3'-Monophosphate.
DrugBank; DB02363; 2'-Monophosphoadenosine-5'-Diphosphate.
DrugBank; DB03900; 2-Methyl-2-Propanol.
DrugBank; DB01842; 3'-Phosphate-Adenosine-5'-Diphosphate.
DrugBank; DB02714; 3'-Uridinemonophosphate.
DrugBank; DB08596; 5'-deoxy-5'-piperidin-1-ylthymidine.
DrugBank; DB02098; Adenosine-2'-5'-Diphosphate.
DrugBank; DB01812; Adenosine-3'-5'-Diphosphate.
DrugBank; DB04272; Citric Acid.
DrugBank; DB02987; Cysteine-S-Acetamide.
DrugBank; DB01961; Cytidine-3'-Monophosphate.
DrugBank; DB01942; Formic Acid.
DrugBank; DB00536; Guanidine.
DrugBank; DB02325; Isopropyl Alcohol.
DrugBank; DB00128; L-Aspartic Acid.
DrugBank; DB04464; N-Formylmethionine.
DrugBank; DB04514; Phosphoric Acid-2'-[2'-Deoxy-Uridine]Ester-5'-Guanosine Ester.
DrugBank; DB03726; Purine Riboside-5'-Monophosphate.
DrugBank; DB03186; U-Pi-a-Pi.
DrugBank; DB02805; Uracil arabinose-3'-phosphate.
DrugBank; DB03447; Uridylyl-2'-5'-Phospho-Adenosine.
iPTMnet; P07998; -.
PhosphoSitePlus; P07998; -.
BioMuta; RNASE1; -.
DMDM; 1350818; -.
PaxDb; P07998; -.
PeptideAtlas; P07998; -.
PRIDE; P07998; -.
ProteomicsDB; 52059; -.
Ensembl; ENST00000340900; ENSP00000344193; ENSG00000129538.
Ensembl; ENST00000397967; ENSP00000381057; ENSG00000129538.
Ensembl; ENST00000397970; ENSP00000381060; ENSG00000129538.
Ensembl; ENST00000412779; ENSP00000399493; ENSG00000129538.
GeneID; 6035; -.
KEGG; hsa:6035; -.
CTD; 6035; -.
DisGeNET; 6035; -.
EuPathDB; HostDB:ENSG00000129538.13; -.
GeneCards; RNASE1; -.
HGNC; HGNC:10044; RNASE1.
HPA; HPA001140; -.
MIM; 180440; gene.
neXtProt; NX_P07998; -.
OpenTargets; ENSG00000129538; -.
PharmGKB; PA34412; -.
eggNOG; ENOG410IYEN; Eukaryota.
eggNOG; ENOG41113F1; LUCA.
GeneTree; ENSGT00940000160869; -.
HOVERGEN; HBG008396; -.
InParanoid; P07998; -.
KO; K01168; -.
OMA; SNSTYCN; -.
OrthoDB; EOG091G15X3; -.
PhylomeDB; P07998; -.
TreeFam; TF333393; -.
BRENDA; 3.1.27.5; 2681.
ChiTaRS; RNASE1; human.
EvolutionaryTrace; P07998; -.
GeneWiki; RNASE1; -.
GenomeRNAi; 6035; -.
PRO; PR:P07998; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000129538; Expressed in 226 organ(s), highest expression level in right testis.
CleanEx; HS_RNASE1; -.
ExpressionAtlas; P07998; baseline and differential.
Genevisible; P07998; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0004522; F:ribonuclease A activity; TAS:ProtInc.
GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:UniProtKB.
Gene3D; 3.10.130.10; -; 1.
InterPro; IPR001427; RNaseA.
InterPro; IPR036816; RNaseA-like_dom_sf.
InterPro; IPR023411; RNaseA_AS.
InterPro; IPR023412; RNaseA_domain.
PANTHER; PTHR11437; PTHR11437; 1.
Pfam; PF00074; RnaseA; 1.
PRINTS; PR00794; RIBONUCLEASE.
ProDom; PD000535; RNaseA; 1.
SMART; SM00092; RNAse_Pc; 1.
SUPFAM; SSF54076; SSF54076; 1.
PROSITE; PS00127; RNASE_PANCREATIC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Nuclease;
Reference proteome; Secreted; Signal.
SIGNAL 1 28 {ECO:0000269|PubMed:1587793,
ECO:0000269|PubMed:2049798,
ECO:0000269|PubMed:2383019,
ECO:0000269|PubMed:3202829,
ECO:0000269|PubMed:6201087,
ECO:0000269|PubMed:8280059}.
CHAIN 29 156 Ribonuclease pancreatic.
/FTId=PRO_0000030921.
REGION 69 73 Substrate binding. {ECO:0000250}.
ACT_SITE 40 40 Proton acceptor.
ACT_SITE 147 147 Proton donor.
BINDING 35 35 Substrate. {ECO:0000250}.
BINDING 38 38 Substrate. {ECO:0000250}.
BINDING 94 94 Substrate. {ECO:0000250}.
BINDING 113 113 Substrate. {ECO:0000250}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:3202829}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3202829}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3202829}.
DISULFID 54 112
DISULFID 68 123
DISULFID 86 138
DISULFID 93 100
MUTAGEN 67 67 R->D: Substantially decreases binding
affinity for RNH1 but maintains high
conformational stability; when associated
with D-95, A-116, D-117 and D-119.
{ECO:0000269|PubMed:17350650}.
MUTAGEN 95 95 N->D: Substantially decreases binding
affinity for RNH1 but maintains high
conformational stability; when associated
with D-67, A-116, D-117 and D-119.
{ECO:0000269|PubMed:17350650}.
MUTAGEN 116 117 NG->RS: No effect on inhibition by RNH1.
{ECO:0000269|PubMed:11021969}.
MUTAGEN 116 116 N->A: Substantially decreases binding
affinity for RNH1 but maintains high
conformational stability; when associated
with D-67, D-95, D-117 and D-119.
{ECO:0000269|PubMed:17350650}.
MUTAGEN 117 117 G->D: Substantially decreases binding
affinity for RNH1 but maintains high
conformational stability; when associated
with D-67, D-95, A-116 and D-119.
{ECO:0000269|PubMed:17350650}.
MUTAGEN 119 119 R->D: Substantially decreases binding
affinity for RNH1 but maintains high
conformational stability; when associated
with D-67, D-95, A-116 and D-117.
{ECO:0000269|PubMed:17350650}.
CONFLICT 2 2 A -> G (in Ref. 7; CAA55817).
{ECO:0000305}.
CONFLICT 4 4 Missing (in Ref. 8; AAB35096).
{ECO:0000305}.
CONFLICT 9 11 RLL -> VLP (in Ref. 8; AAB35096).
{ECO:0000305}.
CONFLICT 16 22 ILLVLGW -> VLLLVR (in Ref. 8; AAB35096).
{ECO:0000305}.
CONFLICT 67 67 R -> L (in Ref. 4; CAG29314).
{ECO:0000305}.
CONFLICT 151 151 S -> T (in Ref. 7; CAA55817).
{ECO:0000305}.
HELIX 32 40 {ECO:0000244|PDB:2E0J}.
TURN 47 50 {ECO:0000244|PDB:1H8X}.
HELIX 53 60 {ECO:0000244|PDB:2E0J}.
TURN 61 64 {ECO:0000244|PDB:2E0L}.
STRAND 65 67 {ECO:0000244|PDB:2E0J}.
STRAND 70 75 {ECO:0000244|PDB:2E0J}.
HELIX 79 83 {ECO:0000244|PDB:2E0J}.
HELIX 84 87 {ECO:0000244|PDB:2E0J}.
STRAND 88 92 {ECO:0000244|PDB:2E0J}.
STRAND 96 102 {ECO:0000244|PDB:2E0J}.
STRAND 107 114 {ECO:0000244|PDB:2E0J}.
STRAND 120 122 {ECO:0000244|PDB:3F8G}.
STRAND 125 139 {ECO:0000244|PDB:2E0J}.
TURN 140 143 {ECO:0000244|PDB:2E0J}.
STRAND 144 152 {ECO:0000244|PDB:2E0J}.
SEQUENCE 156 AA; 17644 MW; F63B17B8B55115F9 CRC64;
MALEKSLVRL LLLVLILLVL GWVQPSLGKE SRAKKFQRQH MDSDSSPSSS STYCNQMMRR
RNMTQGRCKP VNTFVHEPLV DVQNVCFQEK VTCKNGQGNC YKSNSSMHIT DCRLTNGSRY
PNCAYRTSPK ERHIIVACEG SPYVPVHFDA SVEDST


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E0765h ELISA kit EDN,Eosinophil-derived neurotoxin,Homo sapiens,Human,Non-secretory ribonuclease,Ribonuclease 2,Ribonuclease US,RNase 2,RNase UpI-2,RNASE2,RNS2 96T
E0765h ELISA EDN,Eosinophil-derived neurotoxin,Homo sapiens,Human,Non-secretory ribonuclease,Ribonuclease 2,Ribonuclease US,RNase 2,RNase UpI-2,RNASE2,RNS2 96T
EIAAB35609 AGS4,Aicardi-Goutieres syndrome 4 protein,Homo sapiens,Human,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H(35),RNase H2 subunit A,RNase HI large subunit,RNA
EIAAB35523 Bos taurus,Bovine,K6b,Ribonuclease K2,Ribonuclease K6,RK6B,RNase K2,RNase K6,RNASE6,RNS6
EIAAB35510 2-5A-dependent ribonuclease,2-5A-dependent RNase,Homo sapiens,Human,Ribonuclease 4,Ribonuclease L,RNase L,RNASEL,RNS4
EIAAB35515 Bos taurus,Bovine,Ribonuclease pancreatic,RNase 1,RNase A,RNASE1,RNS1
EIAAB35514 Pig,Ribonuclease pancreatic,RNase 1,RNase A,RNASE1,RNS1,Sus scrofa
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EIAAB35628 Bos taurus,Bovine,Ribonuclease BS-1,Seminal ribonuclease,Seminal RNase,SRN,S-RNase
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EIAAB35607 Mouse,Mus musculus,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H2 subunit A,RNase HI large subunit,Rnaseh2a,Rnasehi


 

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