RNAS1_HUMAN
ID RNAS1_HUMAN Reviewed; 156 AA.
AC P07998; B2R589; D3DS06; Q16830; Q16869; Q1KHR2; Q6ICS5; Q9UCB4; Q9UCB5;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 4.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Ribonuclease pancreatic;
DE EC=4.6.1.18;
DE AltName: Full=HP-RNase;
DE AltName: Full=RIB-1;
DE AltName: Full=RNase UpI-1;
DE AltName: Full=Ribonuclease 1;
DE Short=RNase 1;
DE AltName: Full=Ribonuclease A;
DE Short=RNase A;
DE Flags: Precursor;
GN Name=RNASE1; Synonyms=RIB1, RNS1;
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].
RC TISSUE=Pancreas;
RX PubMed=8049276; DOI=10.1016/0167-4781(94)90208-9;
RA Seno M., Fatami J.I., Kosaka M., Seno S., Yamada H.;
RT "Nucleotide sequence encoding human pancreatic ribonuclease.";
RL Biochim. Biophys. Acta 1218:466-468(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16751256; DOI=10.1093/molbev/msl025;
RA Schienman J.E., Holt R.A., Auerbach M.R., Stewart C.B.;
RT "Duplication and divergence of two distinct pancreatic ribonuclease genes
RT in leaf-eating African and Asian colobine monkeys.";
RL Mol. Biol. Evol. 23:1465-1479(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Prostate;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152.
RC TISSUE=Placenta;
RX PubMed=8588814;
RA Kochetov A.V., Lukasheva V.V., Filipenko M.L., Mertvetsov N.P.,
RA Rivkin M.I.;
RT "Primary structure of the coding part of the gene for human pancreatic
RT ribonuclease and its chromosomal location.";
RL Bioorg. Khim. 21:691-694(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-155.
RX PubMed=7649283; DOI=10.1016/0014-5793(95)96890-g;
RA Russo N., de Nigris M., Ciardiello A., Di Donato A., D'Alessio G.;
RT "Expression in mammalian cells, purification and characterization of
RT recombinant human pancreatic ribonuclease.";
RL FEBS Lett. 369:352-352(1995).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-149.
RC TISSUE=Placenta;
RX PubMed=1741299; DOI=10.1093/nar/20.3.612;
RA Haugg M., Schein C.H.;
RT "The DNA sequences of the human and hamster secretory ribonucleases
RT determined with the polymerase chain reaction (PCR).";
RL Nucleic Acids Res. 20:612-612(1992).
RN [10]
RP PROTEIN SEQUENCE OF 29-156.
RC TISSUE=Pancreas;
RX PubMed=6201087; DOI=10.1016/0003-2697(84)90306-3;
RA Beintema J.J., Wietzes P., Weickmann J.L., Glitz D.G.;
RT "The amino acid sequence of human pancreatic ribonuclease.";
RL Anal. Biochem. 136:48-64(1984).
RN [11]
RP PROTEIN SEQUENCE OF 29-156, AND GLYCOSYLATION AT ASN-62; ASN-104 AND
RP ASN-116.
RX PubMed=3202829;
RA Beintema J.J., Blank A., Schieven G.L., Dekker C.A., Sorrentino S.,
RA Libonati M.;
RT "Differences in glycosylation pattern of human secretory ribonucleases.";
RL Biochem. J. 255:501-505(1988).
RN [12]
RP PROTEIN SEQUENCE OF 29-47.
RX PubMed=2383019; DOI=10.1016/0003-9861(90)90424-w;
RA Mizuta K., Awazu S., Yasuda T., Kishi K.;
RT "Purification and characterization of three ribonucleases from human
RT kidney: comparison with urine ribonucleases.";
RL Arch. Biochem. Biophys. 281:144-151(1990).
RN [13]
RP PROTEIN SEQUENCE OF 29-43.
RX PubMed=2049798; DOI=10.1248/cpb.39.146;
RA Sakakibara R., Hashida K., Tominaga N., Sakai K., Ishiguro M., Imamura S.,
RA Ohmatsu F., Sato E.;
RT "A putative mouse oocyte maturation inhibitory protein from urine of
RT pregnant women: N-terminal sequence homology with human nonsecretory
RT ribonuclease.";
RL Chem. Pharm. Bull. 39:146-149(1991).
RN [14]
RP PROTEIN SEQUENCE OF 29-48.
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 [15]
RP PROTEIN SEQUENCE OF 29-49.
RX PubMed=8280059; DOI=10.1042/bj2960617;
RA Yasuda T., Nadano D., Takeshita H., Kishi K.;
RT "Two distinct secretory ribonucleases from human cerebrum: purification,
RT characterization and relationships to other ribonucleases.";
RL Biochem. J. 296:617-625(1993).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 29-156, AND MUTAGENESIS OF
RP 116-ASN-GLY-117.
RX PubMed=11021969; DOI=10.1006/jmbi.2000.4506;
RA Pous J., Canals A., Terzyan S.S., Guasch A., Benito A., Ribo M.,
RA Vilanova M., Coll M.;
RT "Three-dimensional structure of a human pancreatic ribonuclease variant, a
RT step forward in the design of cytotoxic ribonucleases.";
RL J. Mol. Biol. 303:49-60(2000).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-156.
RX PubMed=11264578; DOI=10.1107/s0907444901001147;
RA Pous J., Mallorqui-Fernandez G., Peracaula R., Terzyan S.S., Futami J.,
RA Tada H., Yamada H., Seno M., de Llorens R., Gomis-Rueth F.-X., Coll M.;
RT "Three-dimensional structure of human RNase 1 delta N7 at 1.9 A
RT resolution.";
RL Acta Crystallogr. D 57:498-505(2001).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-156, AND DISULFIDE BONDS.
RX PubMed=11591351; DOI=10.1016/s0969-2126(01)00659-1;
RA Canals A., Pous J., Guasch A., Benito A., Ribo M., Vilanova M., Coll M.;
RT "The structure of an engineered domain-swapped ribonuclease dimer and its
RT implications for the evolution of proteins toward oligomerization.";
RL Structure 9:967-976(2001).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 29-156 IN COMPLEX WITH RNH1,
RP FUNCTION, SUBUNIT, INTERACTION WITH RNH1, DISULFIDE BONDS, AND MUTAGENESIS
RP OF ARG-67; ASN-95; ASN-116; GLY-117 AND ARG-119.
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).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 29-156, AND DISULFIDE BONDS.
RX PubMed=17586772; DOI=10.1110/ps.072851407;
RA Yamada H., Tamada T., Kosaka M., Miyata K., Fujiki S., Tano M., Moriya M.,
RA Yamanishi M., Honjo E., Tada H., Ino T., Yamaguchi H., Futami J., Seno M.,
RA Nomoto T., Hirata T., Yoshimura M., Kuroki R.;
RT "'Crystal lattice engineering,' an approach to engineer protein crystal
RT contacts by creating intermolecular symmetry: crystallization and structure
RT determination of a mutant human RNase 1 with a hydrophobic interface of
RT leucines.";
RL Protein Sci. 16:1389-1397(2007).
CC -!- FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3'
CC side of pyrimidine nucleotides. Acts on single-stranded and double-
CC stranded RNA. {ECO:0000269|PubMed:17350650}.
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 -!- 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 -!- SUBUNIT: Monomer. Interacts with and forms tight 1:1 complexes with
CC RNH1. Dimerization of two such complexes may occur. Interaction with
CC RNH1 inhibits this protein. {ECO:0000269|PubMed:17350650}.
CC -!- INTERACTION:
CC P07998; P13489: RNH1; NbExp=8; IntAct=EBI-2823523, EBI-1237106;
CC P07998; Q9C029: TRIM7; NbExp=3; IntAct=EBI-2823523, EBI-2813981;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Pancreas and other tissues and body fluids
CC (indicating it may have other physiological functions besides its role
CC in digestion).
CC -!- PTM: N-linked glycans are of complex type.
CC {ECO:0000269|PubMed:3202829}.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; D26129; BAA05124.1; -; mRNA.
DR EMBL; DQ494867; ABF00144.1; -; Genomic_DNA.
DR EMBL; AK312100; BAG35036.1; -; mRNA.
DR EMBL; CR450318; CAG29314.1; -; mRNA.
DR EMBL; CH471078; EAW66437.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66438.1; -; Genomic_DNA.
DR EMBL; BC005324; AAH05324.1; -; mRNA.
DR EMBL; BC022882; AAH22882.1; -; mRNA.
DR EMBL; X79235; CAA55817.1; -; Genomic_DNA.
DR EMBL; S79281; AAB35096.1; -; mRNA.
DR EMBL; X62946; CAA44718.1; -; Genomic_DNA.
DR CCDS; CCDS9559.1; -.
DR PIR; I53530; I53530.
DR PIR; S45003; NRHU1.
DR RefSeq; NP_002924.1; NM_002933.4.
DR RefSeq; NP_937875.1; NM_198232.2.
DR RefSeq; NP_937877.1; NM_198234.2.
DR RefSeq; NP_937878.1; NM_198235.2.
DR PDB; 1DZA; X-ray; 1.65 A; A/B=28-156.
DR PDB; 1E21; X-ray; 1.90 A; A=29-156.
DR PDB; 1H8X; X-ray; 2.00 A; A/B=29-156.
DR PDB; 1Z7X; X-ray; 1.95 A; X/Z=29-156.
DR PDB; 2E0J; X-ray; 1.60 A; A/B=29-156.
DR PDB; 2E0L; X-ray; 1.60 A; A/B=29-156.
DR PDB; 2E0M; X-ray; 1.70 A; A/B=29-156.
DR PDB; 2E0O; X-ray; 2.00 A; A/B=29-156.
DR PDB; 2K11; NMR; -; A=29-155.
DR PDB; 2Q4G; X-ray; 1.95 A; X/Z=29-156.
DR PDB; 3F8G; X-ray; 2.60 A; A/B=29-153.
DR PDB; 4KXH; X-ray; 2.70 A; A/B/C/D=29-156.
DR PDBsum; 1DZA; -.
DR PDBsum; 1E21; -.
DR PDBsum; 1H8X; -.
DR PDBsum; 1Z7X; -.
DR PDBsum; 2E0J; -.
DR PDBsum; 2E0L; -.
DR PDBsum; 2E0M; -.
DR PDBsum; 2E0O; -.
DR PDBsum; 2K11; -.
DR PDBsum; 2Q4G; -.
DR PDBsum; 3F8G; -.
DR PDBsum; 4KXH; -.
DR AlphaFoldDB; P07998; -.
DR BMRB; P07998; -.
DR SMR; P07998; -.
DR BioGRID; 111964; 11.
DR IntAct; P07998; 10.
DR MINT; P07998; -.
DR STRING; 9606.ENSP00000381057; -.
DR BindingDB; P07998; -.
DR ChEMBL; CHEMBL5425; -.
DR DrugBank; DB08661; 1-(2,5-dideoxy-5-pyrrolidin-1-yl-beta-L-erythro-pentofuranosyl)-5-methylpyrimidine-2,4(1H,3H)-dione.
DR DrugBank; DB03765; 2'-cytidylic acid.
DR DrugBank; DB02573; 2'-deoxycytidine-2'-deoxyadenosine-3',5'-monophosphate.
DR DrugBank; DB03448; 2'-Deoxyuridine 3'-Monophosphate.
DR DrugBank; DB03155; 2'-fluoro-2'-deoxyuridine 3'-monophosphate.
DR DrugBank; DB02363; 2'-Monophosphoadenosine-5'-Diphosphate.
DR DrugBank; DB01842; 3'-Phosphate-Adenosine-5'-Diphosphate.
DR DrugBank; DB02714; 3'-Uridinemonophosphate.
DR DrugBank; DB08596; 5'-deoxy-5'-piperidin-1-ylthymidine.
DR DrugBank; DB03792; 5-Aminouracil.
DR DrugBank; DB01812; Adenosine 3',5'-diphosphate.
DR DrugBank; DB02098; Adenosine-2'-5'-Diphosphate.
DR DrugBank; DB03186; Adenylate-3'-phosphate-[[2'-deoxy-uridine-5'-phosphate]-3'-phosphate].
DR DrugBank; DB02805; Arabinouridine 3'-phosphate.
DR DrugBank; DB00128; Aspartic acid.
DR DrugBank; DB04272; Citric acid.
DR DrugBank; DB02987; Cysteine-S-acetamide.
DR DrugBank; DB01961; Cytidine 3'-monophosphate.
DR DrugBank; DB03326; Deoxycytidylyl-3',5'-guanosine.
DR DrugBank; DB01942; Formic acid.
DR DrugBank; DB00536; Guanidine.
DR DrugBank; DB04464; N-Formylmethionine.
DR DrugBank; DB03726; Purine Riboside-5'-Monophosphate.
DR DrugBank; DB03900; tert-butanol.
DR DrugBank; DB03512; Uridine-2',3'-vanadate.
DR DrugBank; DB03447; Uridylyl-2'-5'-phospho-adenosine.
DR DrugBank; DB04514; Uridylyl-2'-5'-phospho-guanosine.
DR GlyConnect; 1973; 3 N-Linked glycans (2 sites).
DR GlyGen; P07998; 3 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; P07998; -.
DR PhosphoSitePlus; P07998; -.
DR BioMuta; RNASE1; -.
DR DMDM; 1350818; -.
DR jPOST; P07998; -.
DR MassIVE; P07998; -.
DR PaxDb; P07998; -.
DR PeptideAtlas; P07998; -.
DR PRIDE; P07998; -.
DR ProteomicsDB; 52059; -.
DR Antibodypedia; 18; 285 antibodies from 25 providers.
DR DNASU; 6035; -.
DR Ensembl; ENST00000340900.3; ENSP00000344193.3; ENSG00000129538.14.
DR Ensembl; ENST00000397967.5; ENSP00000381057.4; ENSG00000129538.14.
DR Ensembl; ENST00000397970.4; ENSP00000381060.4; ENSG00000129538.14.
DR Ensembl; ENST00000412779.2; ENSP00000399493.2; ENSG00000129538.14.
DR GeneID; 6035; -.
DR KEGG; hsa:6035; -.
DR MANE-Select; ENST00000397967.5; ENSP00000381057.4; NM_002933.5; NP_002924.1.
DR CTD; 6035; -.
DR DisGeNET; 6035; -.
DR GeneCards; RNASE1; -.
DR HGNC; HGNC:10044; RNASE1.
DR HPA; ENSG00000129538; Tissue enriched (pancreas).
DR MIM; 180440; gene.
DR neXtProt; NX_P07998; -.
DR OpenTargets; ENSG00000129538; -.
DR PharmGKB; PA34412; -.
DR VEuPathDB; HostDB:ENSG00000129538; -.
DR eggNOG; ENOG502SQ4K; Eukaryota.
DR GeneTree; ENSGT00940000160869; -.
DR HOGENOM; CLU_117006_0_0_1; -.
DR InParanoid; P07998; -.
DR OMA; SNSTYCN; -.
DR OrthoDB; 1549558at2759; -.
DR PhylomeDB; P07998; -.
DR TreeFam; TF333393; -.
DR BRENDA; 4.6.1.18; 2681.
DR PathwayCommons; P07998; -.
DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR SignaLink; P07998; -.
DR BioGRID-ORCS; 6035; 17 hits in 1074 CRISPR screens.
DR ChiTaRS; RNASE1; human.
DR EvolutionaryTrace; P07998; -.
DR GeneWiki; RNASE1; -.
DR GenomeRNAi; 6035; -.
DR Pharos; P07998; Tchem.
DR PRO; PR:P07998; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P07998; protein.
DR Bgee; ENSG00000129538; Expressed in right testis and 201 other tissues.
DR ExpressionAtlas; P07998; baseline and differential.
DR Genevisible; P07998; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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; TAS:ProtInc.
DR GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
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; Direct protein sequencing; Disulfide bond; Endonuclease;
KW Glycoprotein; Hydrolase; Lyase; Nuclease; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:1587793,
FT ECO:0000269|PubMed:2049798, ECO:0000269|PubMed:2383019,
FT ECO:0000269|PubMed:3202829, ECO:0000269|PubMed:6201087,
FT ECO:0000269|PubMed:8280059"
FT CHAIN 29..156
FT /note="Ribonuclease pancreatic"
FT /id="PRO_0000030921"
FT REGION 33..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT ACT_SITE 147
FT /note="Proton donor"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 69..73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:3202829"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3202829"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3202829"
FT DISULFID 54..112
FT DISULFID 68..123
FT DISULFID 86..138
FT DISULFID 93..100
FT MUTAGEN 67
FT /note="R->D: Substantially decreases binding affinity for
FT RNH1 but maintains high conformational stability; when
FT associated with D-95, A-116, D-117 and D-119."
FT /evidence="ECO:0000269|PubMed:17350650"
FT MUTAGEN 95
FT /note="N->D: Substantially decreases binding affinity for
FT RNH1 but maintains high conformational stability; when
FT associated with D-67, A-116, D-117 and D-119."
FT /evidence="ECO:0000269|PubMed:17350650"
FT MUTAGEN 116..117
FT /note="NG->RS: No effect on inhibition by RNH1."
FT /evidence="ECO:0000269|PubMed:11021969"
FT MUTAGEN 116
FT /note="N->A: Substantially decreases binding affinity for
FT RNH1 but maintains high conformational stability; when
FT associated with D-67, D-95, D-117 and D-119."
FT /evidence="ECO:0000269|PubMed:17350650"
FT MUTAGEN 117
FT /note="G->D: Substantially decreases binding affinity for
FT RNH1 but maintains high conformational stability; when
FT associated with D-67, D-95, A-116 and D-119."
FT /evidence="ECO:0000269|PubMed:17350650"
FT MUTAGEN 119
FT /note="R->D: Substantially decreases binding affinity for
FT RNH1 but maintains high conformational stability; when
FT associated with D-67, D-95, A-116 and D-117."
FT /evidence="ECO:0000269|PubMed:17350650"
FT CONFLICT 2
FT /note="A -> G (in Ref. 7; CAA55817)"
FT /evidence="ECO:0000305"
FT CONFLICT 4
FT /note="Missing (in Ref. 8; AAB35096)"
FT /evidence="ECO:0000305"
FT CONFLICT 9..11
FT /note="RLL -> VLP (in Ref. 8; AAB35096)"
FT /evidence="ECO:0000305"
FT CONFLICT 16..22
FT /note="ILLVLGW -> VLLLVR (in Ref. 8; AAB35096)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="R -> L (in Ref. 4; CAG29314)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="S -> T (in Ref. 7; CAA55817)"
FT /evidence="ECO:0000305"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:2E0J"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:1H8X"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:2E0J"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:2E0L"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2E0J"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:2E0J"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:2E0J"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:2E0J"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2E0J"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:2E0J"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:2E0J"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:3F8G"
FT STRAND 125..139
FT /evidence="ECO:0007829|PDB:2E0J"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:2E0J"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:2E0J"
SQ SEQUENCE 156 AA; 17644 MW; F63B17B8B55115F9 CRC64;
MALEKSLVRL LLLVLILLVL GWVQPSLGKE SRAKKFQRQH MDSDSSPSSS STYCNQMMRR
RNMTQGRCKP VNTFVHEPLV DVQNVCFQEK VTCKNGQGNC YKSNSSMHIT DCRLTNGSRY
PNCAYRTSPK ERHIIVACEG SPYVPVHFDA SVEDST
