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P61823

- RNAS1_BOVIN

UniProt

P61823 - RNAS1_BOVIN

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Protein
Ribonuclease pancreatic
Gene
RNASE1, RNS1
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.1 Publication

Catalytic activityi

Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331Substrate
Binding sitei36 – 361Substrate
Active sitei38 – 381Proton acceptor2 Publications
Binding sitei92 – 921Substrate
Binding sitei111 – 1111Substrate
Active sitei145 – 1451Proton donor2 Publications

GO - Molecular functioni

  1. nucleic acid binding Source: InterPro
  2. pancreatic ribonuclease activity Source: UniProtKB-EC
  3. protein binding Source: IntAct
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

BRENDAi3.1.27.5. 908.
SABIO-RKP61823.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease pancreatic (EC:3.1.27.5)
Alternative name(s):
RNase 1
RNase A
Gene namesi
Name:RNASE1
Synonyms:RNS1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 10

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381H → A: Loss of activity.
Mutagenesisi145 – 1451H → A: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26262 Publications
Add
BLAST
Chaini27 – 150124Ribonuclease pancreatic
PRO_0000030915Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi27 – 271N-linked (Glc) (glycation); in vitro1 Publication
Glycosylationi33 – 331N-linked (Glc) (glycation); in vitro1 Publication
Disulfide bondi52 ↔ 1101 Publication
Glycosylationi60 – 601N-linked (GlcNAc...); partial1 Publication
CAR_000006
Glycosylationi63 – 631N-linked (Glc) (glycation); in vitro1 Publication
Disulfide bondi66 ↔ 1211 Publication
Glycosylationi67 – 671N-linked (Glc) (glycation); in vitro1 Publication
Disulfide bondi84 ↔ 1361 Publication
Disulfide bondi91 ↔ 981 Publication

Keywords - PTMi

Disulfide bond, Glycation, Glycoprotein

Proteomic databases

PaxDbiP61823.
PRIDEiP61823.

Miscellaneous databases

PMAP-CutDBP61823.

Expressioni

Tissue specificityi

Pancreas.

Interactioni

Subunit structurei

Interacts with and forms tight 1:1 complexes with RNH1. Dimerization of two such complexes may occur. Interaction with RNH1 inhibits this protein By similarity. Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
PDI1P179672EBI-908364,EBI-13012From a different organism.
RNH1P134893EBI-908364,EBI-1237106From a different organism.

Protein-protein interaction databases

BioGridi159601. 1 interaction.
IntActiP61823. 6 interactions.
MINTiMINT-1510416.
STRINGi9913.ENSBTAP00000011586.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 389
Beta strandi43 – 453
Helixi48 – 503
Helixi51 – 588
Beta strandi61 – 655
Beta strandi68 – 736
Helixi77 – 826
Helixi83 – 853
Beta strandi86 – 894
Beta strandi92 – 943
Beta strandi98 – 1003
Beta strandi102 – 11211
Beta strandi113 – 1153
Beta strandi118 – 1203
Beta strandi123 – 1308
Beta strandi132 – 1376
Turni138 – 1414
Beta strandi142 – 1498

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2WX-ray2.10A/B27-150[»]
1A5PX-ray1.60A27-150[»]
1A5QX-ray2.30A27-150[»]
1AFKX-ray1.70A/B27-150[»]
1AFLX-ray1.70A/B27-150[»]
1AFUX-ray2.00A/B27-150[»]
1AQPX-ray2.00A27-150[»]
1B6VX-ray2.00A/B27-150[»]
1BELX-ray1.60A27-150[»]
1BZQX-ray2.80A/B/C/D27-150[»]
1C0BX-ray1.90A23-150[»]
1C0CX-ray2.00A23-150[»]
1C8WX-ray1.80A27-150[»]
1C9VX-ray1.70A27-150[»]
1C9XX-ray1.80A27-150[»]
1CJQX-ray3.00A27-41[»]
B50-150[»]
1CJRX-ray2.30A27-41[»]
B50-150[»]
1D5DX-ray2.25A27-41[»]
B50-150[»]
1D5EX-ray2.25A27-41[»]
B50-150[»]
1D5HX-ray2.25A27-41[»]
B50-150[»]
1DFJX-ray2.50E27-150[»]
1DY5X-ray0.87A/B27-150[»]
1EICX-ray1.40A27-150[»]
1EIDX-ray1.40A27-150[»]
1EIEX-ray1.40A27-150[»]
1EOSX-ray2.00A/B27-150[»]
1EOWX-ray2.00A27-150[»]
1F0VX-ray1.70A/B/C/D27-150[»]
1FEVX-ray2.25A27-41[»]
B50-150[»]
1FS3X-ray1.40A27-150[»]
1GV7X-ray2.10A84-111[»]
1IZPX-ray1.50A27-150[»]
1IZQX-ray1.80A27-150[»]
1IZRX-ray1.50A27-150[»]
1J7ZX-ray2.25A27-41[»]
B47-150[»]
1J80X-ray2.10A27-41[»]
B47-150[»]
1J81X-ray2.20A27-41[»]
B47-150[»]
1J82X-ray2.30A27-41[»]
B47-150[»]
1JN4X-ray1.80A/B27-150[»]
1JS0X-ray2.20A/B/C27-150[»]
1JVTX-ray2.05A/B27-150[»]
1JVUX-ray1.78A/B27-150[»]
1JVVX-ray2.20A/B27-150[»]
1KF2X-ray1.10A27-150[»]
1KF3X-ray1.05A27-150[»]
1KF4X-ray1.10A27-150[»]
1KF5X-ray1.15A27-150[»]
1KF7X-ray1.15A27-150[»]
1KF8X-ray1.15A27-150[»]
1KH8X-ray2.00A27-150[»]
1LSQX-ray1.90A/B27-150[»]
1O0FX-ray1.50A/B27-150[»]
1O0HX-ray1.20A/B27-150[»]
1O0MX-ray1.50A/B27-150[»]
1O0NX-ray1.50A/B27-150[»]
1O0OX-ray1.20A/B27-150[»]
1QHCX-ray1.70A/B27-150[»]
1RARX-ray1.90A28-150[»]
1RASX-ray1.70A28-150[»]
1RATX-ray1.50A27-150[»]
1RBBX-ray2.50A/B27-150[»]
1RBCX-ray2.00A47-150[»]
S27-41[»]
1RBDX-ray1.70A47-150[»]
S27-41[»]
1RBEX-ray1.75A47-150[»]
S27-41[»]
1RBFX-ray1.80A47-150[»]
S27-41[»]
1RBGX-ray1.80A47-150[»]
S27-41[»]
1RBHX-ray1.70A47-150[»]
S27-41[»]
1RBIX-ray1.80A47-150[»]
S27-41[»]
1RBJX-ray2.70A27-150[»]
1RBNX-ray2.10A27-150[»]
1RBWX-ray1.69A27-150[»]
1RBXX-ray1.69A27-150[»]
1RCAX-ray1.90A27-150[»]
1RCNX-ray2.32E27-150[»]
1RHAX-ray1.80A27-150[»]
1RHBX-ray1.50A27-150[»]
1RNCX-ray1.50A27-150[»]
1RNDX-ray1.50A27-150[»]
1RNMX-ray2.00E27-150[»]
1RNNX-ray1.80E27-150[»]
1RNOX-ray1.90A27-150[»]
1RNQX-ray2.00A27-150[»]
1RNUX-ray1.60A27-150[»]
1RNVX-ray1.60A27-150[»]
1RNWX-ray1.80A27-150[»]
1RNXX-ray1.90A27-150[»]
1RNYX-ray2.00A27-150[»]
1RNZX-ray1.90A27-150[»]
1ROBX-ray1.60A27-150[»]
1RPFX-ray2.20A27-150[»]
1RPGX-ray1.40A27-150[»]
1RPHX-ray2.20A27-150[»]
1RSMX-ray2.00A27-150[»]
1RTAX-ray2.50E27-150[»]
1RTBX-ray2.50A27-150[»]
1RUVX-ray1.25A27-150[»]
1SRNX-ray1.80A27-144[»]
B137-150[»]
1SSAX-ray2.00A27-144[»]
B137-150[»]
1SSBX-ray2.00A27-144[»]
B137-150[»]
1SSCX-ray2.00A27-138[»]
B140-150[»]
1U1BX-ray2.00A/B27-150[»]
1UN5X-ray2.60A-[»]
1W4OX-ray1.60A/B27-150[»]
1W4PX-ray1.69A/B27-150[»]
1W4QX-ray1.68A/B27-150[»]
1WBUX-ray1.90A/B27-150[»]
1XPSX-ray1.80A/B27-150[»]
1XPTX-ray1.90A/B27-150[»]
1YMNX-ray1.45A27-150[»]
1YMRX-ray1.50A27-150[»]
1YMWX-ray1.50A27-150[»]
1Z3LX-ray1.80E47-150[»]
S27-41[»]
1Z3MX-ray2.00E47-150[»]
S27-41[»]
1Z3PX-ray2.00E47-150[»]
S27-41[»]
1Z6DX-ray1.54A/B27-150[»]
1Z6SX-ray1.50A/B27-150[»]
2AASNMR-A27-150[»]
2APQX-ray1.80A27-150[»]
2APUmodel-0/1/2/3/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x/y/z27-150[»]
2BLPX-ray1.40A27-150[»]
2BLZX-ray1.40A27-150[»]
2E33X-ray2.70B27-150[»]
2E3WX-ray1.05A27-150[»]
2G4WX-ray1.84A/B27-150[»]
2G4XX-ray1.95A27-150[»]
2G8QX-ray1.50A/B27-150[»]
2G8RX-ray1.70A/B27-150[»]
2NUIX-ray1.10A27-150[»]
2OP2X-ray1.60A27-150[»]
2OQFX-ray2.30A/B/C/D27-150[»]
2P42X-ray1.80A/C27-150[»]
2P43X-ray1.65A27-150[»]
2P44X-ray1.80A27-150[»]
2P45X-ray1.10A27-150[»]
2P46X-ray2.50A/C27-150[»]
2P47X-ray2.50A27-150[»]
2P48X-ray2.30A27-150[»]
2P49X-ray1.38A27-150[»]
2P4AX-ray1.90A/C27-150[»]
2QCAX-ray1.33A27-150[»]
2RATX-ray1.50A27-150[»]
2RLNX-ray1.85E42-150[»]
S27-41[»]
2RNSX-ray1.60A27-150[»]
2W5GX-ray1.70A/B27-150[»]
2W5IX-ray2.40A/B27-150[»]
2W5KX-ray1.70A/B27-150[»]
2W5LX-ray1.70A/B27-150[»]
2W5MX-ray1.80A/B27-150[»]
2XOGX-ray1.72A/B27-150[»]
2XOIX-ray1.72A/B27-150[»]
3A1Rneutron diffraction1.70A27-150[»]
3D6OX-ray1.58A/B27-150[»]
3D6PX-ray1.60A/B27-150[»]
3D6QX-ray1.60A/B27-150[»]
3D7BX-ray1.60A/B27-150[»]
3D8YX-ray1.72A/B27-150[»]
3D8ZX-ray1.98A/B27-150[»]
3DH5X-ray1.60A27-150[»]
3DH6X-ray1.60A27-150[»]
3DI7X-ray1.60A27-150[»]
3DI8X-ray1.60A27-150[»]
3DI9X-ray2.00A27-150[»]
3DIBX-ray1.40A27-150[»]
3DICX-ray1.60A27-150[»]
3DXGX-ray1.39A/B27-150[»]
3DXHX-ray1.40A/B27-150[»]
3EUXX-ray1.65A/B27-150[»]
3EUYX-ray1.95A/B27-150[»]
3EUZX-ray1.84A/B27-150[»]
3EV0X-ray1.76A/B27-150[»]
3EV1X-ray2.00A/B27-150[»]
3EV2X-ray2.02A/B27-150[»]
3EV3X-ray1.68A/B27-150[»]
3EV4X-ray1.93A/B27-150[»]
3EV5X-ray1.68A/B27-150[»]
3EV6X-ray1.76A/B27-150[»]
3FKZX-ray1.99A/B27-150[»]
3FL0X-ray1.94A/B27-150[»]
3FL1X-ray1.90A/B27-150[»]
3FL3X-ray1.60A/B27-150[»]
3I67X-ray1.30A27-150[»]
3I6FX-ray1.30A27-150[»]
3I6HX-ray1.30A27-150[»]
3I6JX-ray1.30A27-150[»]
3I7WX-ray2.35A27-150[»]
3I7XX-ray2.60A27-150[»]
3I7YX-ray2.40A27-150[»]
3JW1X-ray1.60A/B27-150[»]
3LXOX-ray1.55A27-150[»]
3MWQX-ray1.68A26-150[»]
3MWRX-ray1.85A27-150[»]
3MX8X-ray2.10A26-150[»]
3MZQX-ray1.50A23-150[»]
3MZRX-ray1.50A23-150[»]
3OQYX-ray1.49A/B47-150[»]
a/b27-41[»]
3OQZX-ray2.50A/B47-150[»]
a/b27-41[»]
3OR0X-ray2.30A/B47-150[»]
a/b27-41[»]
3QL1X-ray1.29A27-150[»]
3QL2X-ray1.49A/B27-150[»]
3QSKX-ray1.75A27-150[»]
3RATX-ray1.50A27-150[»]
3RH1X-ray2.10A27-150[»]
3RIDX-ray2.18A/B/C/D27-150[»]
3RN3X-ray1.45A27-150[»]
3RSDX-ray1.60A27-150[»]
3RSKX-ray2.00A27-150[»]
3RSPX-ray1.70A27-150[»]
3SRNX-ray2.00A27-139[»]
B140-146[»]
4AO1X-ray1.58A27-150[»]
4G8VX-ray1.70A/B27-150[»]
4G8YX-ray1.80A/B27-150[»]
4G90X-ray1.90A/B27-150[»]
4J5ZX-ray1.80A27-150[»]
4J60X-ray1.69A27-150[»]
4J61X-ray1.69A27-150[»]
4J62X-ray2.04A27-150[»]
4J63X-ray2.04A27-150[»]
4J64X-ray1.78A27-150[»]
4J65X-ray1.96A27-150[»]
4J66X-ray2.04A27-150[»]
4J67X-ray1.86A27-150[»]
4J68X-ray1.78A27-150[»]
4J69X-ray1.89A27-150[»]
4J6AX-ray2.04A27-150[»]
4K7LX-ray1.38A27-41[»]
B47-150[»]
4K7MX-ray1.80A27-150[»]
4L55X-ray1.65A/B27-150[»]
4MXFX-ray2.25A/B27-150[»]
4O36X-ray1.22A27-41[»]
B47-150[»]
4O37X-ray1.40A27-41[»]
B47-150[»]
4RATX-ray1.50A27-150[»]
4RSDX-ray1.60A27-150[»]
4RSKX-ray2.10A27-150[»]
4SRNX-ray2.00A27-139[»]
B140-150[»]
5RATX-ray1.50A27-150[»]
5RSAX-ray2.00A27-150[»]
6RATX-ray1.50A27-150[»]
6RSAX-ray2.00A27-150[»]
7RATX-ray1.50A27-150[»]
7RSAX-ray1.26A27-150[»]
8RATX-ray1.50A27-150[»]
8RSAX-ray1.80A/B27-150[»]
9RATX-ray1.50A27-150[»]
9RSAX-ray1.80A/B27-150[»]
ProteinModelPortaliP61823.
SMRiP61823. Positions 27-150.

Miscellaneous databases

EvolutionaryTraceiP61823.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 715Substrate binding

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40319.
GeneTreeiENSGT00390000007840.
HOGENOMiHOG000276883.
HOVERGENiHBG008396.
InParanoidiP61823.
KOiK01168.
OMAiANKHIIV.
OrthoDBiEOG7J1826.
TreeFamiTF333393.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61823-1 [UniParc]FASTAAdd to Basket

« Hide

MALKSLVLLS LLVLVLLLVR VQPSLGKETA AAKFERQHMD SSTSAASSSN    50
YCNQMMKSRN LTKDRCKPVN TFVHESLADV QAVCSQKNVA CKNGQTNCYQ 100
SYSTMSITDC RETGSSKYPN CAYKTTQANK HIIVACEGNP YVPVHFDASV 150
Length:150
Mass (Da):16,461
Last modified:June 7, 2004 - v1
Checksum:i74E5DC61E679187D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07283 Genomic DNA. Translation: CAA30263.1.
BC149529 mRNA. Translation: AAI49530.1.
BC149636 mRNA. Translation: AAI49637.1.
S80747 mRNA. Translation: AAB35594.1.
S81740 Genomic DNA. Translation: AAB36134.1.
PIRiS00897. NRBO.
RefSeqiNP_001014408.2. NM_001014386.4.
XP_005211519.1. XM_005211462.1.
UniGeneiBt.4630.

Genome annotation databases

EnsembliENSBTAT00000011586; ENSBTAP00000011586; ENSBTAG00000008793.
GeneIDi282340.
KEGGibta:282340.

Cross-referencesi

Web resourcesi

Worthington enzyme manual
Functional Glycomics Gateway - Glycan Binding

RNase A

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07283 Genomic DNA. Translation: CAA30263.1 .
BC149529 mRNA. Translation: AAI49530.1 .
BC149636 mRNA. Translation: AAI49637.1 .
S80747 mRNA. Translation: AAB35594.1 .
S81740 Genomic DNA. Translation: AAB36134.1 .
PIRi S00897. NRBO.
RefSeqi NP_001014408.2. NM_001014386.4.
XP_005211519.1. XM_005211462.1.
UniGenei Bt.4630.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A2W X-ray 2.10 A/B 27-150 [» ]
1A5P X-ray 1.60 A 27-150 [» ]
1A5Q X-ray 2.30 A 27-150 [» ]
1AFK X-ray 1.70 A/B 27-150 [» ]
1AFL X-ray 1.70 A/B 27-150 [» ]
1AFU X-ray 2.00 A/B 27-150 [» ]
1AQP X-ray 2.00 A 27-150 [» ]
1B6V X-ray 2.00 A/B 27-150 [» ]
1BEL X-ray 1.60 A 27-150 [» ]
1BZQ X-ray 2.80 A/B/C/D 27-150 [» ]
1C0B X-ray 1.90 A 23-150 [» ]
1C0C X-ray 2.00 A 23-150 [» ]
1C8W X-ray 1.80 A 27-150 [» ]
1C9V X-ray 1.70 A 27-150 [» ]
1C9X X-ray 1.80 A 27-150 [» ]
1CJQ X-ray 3.00 A 27-41 [» ]
B 50-150 [» ]
1CJR X-ray 2.30 A 27-41 [» ]
B 50-150 [» ]
1D5D X-ray 2.25 A 27-41 [» ]
B 50-150 [» ]
1D5E X-ray 2.25 A 27-41 [» ]
B 50-150 [» ]
1D5H X-ray 2.25 A 27-41 [» ]
B 50-150 [» ]
1DFJ X-ray 2.50 E 27-150 [» ]
1DY5 X-ray 0.87 A/B 27-150 [» ]
1EIC X-ray 1.40 A 27-150 [» ]
1EID X-ray 1.40 A 27-150 [» ]
1EIE X-ray 1.40 A 27-150 [» ]
1EOS X-ray 2.00 A/B 27-150 [» ]
1EOW X-ray 2.00 A 27-150 [» ]
1F0V X-ray 1.70 A/B/C/D 27-150 [» ]
1FEV X-ray 2.25 A 27-41 [» ]
B 50-150 [» ]
1FS3 X-ray 1.40 A 27-150 [» ]
1GV7 X-ray 2.10 A 84-111 [» ]
1IZP X-ray 1.50 A 27-150 [» ]
1IZQ X-ray 1.80 A 27-150 [» ]
1IZR X-ray 1.50 A 27-150 [» ]
1J7Z X-ray 2.25 A 27-41 [» ]
B 47-150 [» ]
1J80 X-ray 2.10 A 27-41 [» ]
B 47-150 [» ]
1J81 X-ray 2.20 A 27-41 [» ]
B 47-150 [» ]
1J82 X-ray 2.30 A 27-41 [» ]
B 47-150 [» ]
1JN4 X-ray 1.80 A/B 27-150 [» ]
1JS0 X-ray 2.20 A/B/C 27-150 [» ]
1JVT X-ray 2.05 A/B 27-150 [» ]
1JVU X-ray 1.78 A/B 27-150 [» ]
1JVV X-ray 2.20 A/B 27-150 [» ]
1KF2 X-ray 1.10 A 27-150 [» ]
1KF3 X-ray 1.05 A 27-150 [» ]
1KF4 X-ray 1.10 A 27-150 [» ]
1KF5 X-ray 1.15 A 27-150 [» ]
1KF7 X-ray 1.15 A 27-150 [» ]
1KF8 X-ray 1.15 A 27-150 [» ]
1KH8 X-ray 2.00 A 27-150 [» ]
1LSQ X-ray 1.90 A/B 27-150 [» ]
1O0F X-ray 1.50 A/B 27-150 [» ]
1O0H X-ray 1.20 A/B 27-150 [» ]
1O0M X-ray 1.50 A/B 27-150 [» ]
1O0N X-ray 1.50 A/B 27-150 [» ]
1O0O X-ray 1.20 A/B 27-150 [» ]
1QHC X-ray 1.70 A/B 27-150 [» ]
1RAR X-ray 1.90 A 28-150 [» ]
1RAS X-ray 1.70 A 28-150 [» ]
1RAT X-ray 1.50 A 27-150 [» ]
1RBB X-ray 2.50 A/B 27-150 [» ]
1RBC X-ray 2.00 A 47-150 [» ]
S 27-41 [» ]
1RBD X-ray 1.70 A 47-150 [» ]
S 27-41 [» ]
1RBE X-ray 1.75 A 47-150 [» ]
S 27-41 [» ]
1RBF X-ray 1.80 A 47-150 [» ]
S 27-41 [» ]
1RBG X-ray 1.80 A 47-150 [» ]
S 27-41 [» ]
1RBH X-ray 1.70 A 47-150 [» ]
S 27-41 [» ]
1RBI X-ray 1.80 A 47-150 [» ]
S 27-41 [» ]
1RBJ X-ray 2.70 A 27-150 [» ]
1RBN X-ray 2.10 A 27-150 [» ]
1RBW X-ray 1.69 A 27-150 [» ]
1RBX X-ray 1.69 A 27-150 [» ]
1RCA X-ray 1.90 A 27-150 [» ]
1RCN X-ray 2.32 E 27-150 [» ]
1RHA X-ray 1.80 A 27-150 [» ]
1RHB X-ray 1.50 A 27-150 [» ]
1RNC X-ray 1.50 A 27-150 [» ]
1RND X-ray 1.50 A 27-150 [» ]
1RNM X-ray 2.00 E 27-150 [» ]
1RNN X-ray 1.80 E 27-150 [» ]
1RNO X-ray 1.90 A 27-150 [» ]
1RNQ X-ray 2.00 A 27-150 [» ]
1RNU X-ray 1.60 A 27-150 [» ]
1RNV X-ray 1.60 A 27-150 [» ]
1RNW X-ray 1.80 A 27-150 [» ]
1RNX X-ray 1.90 A 27-150 [» ]
1RNY X-ray 2.00 A 27-150 [» ]
1RNZ X-ray 1.90 A 27-150 [» ]
1ROB X-ray 1.60 A 27-150 [» ]
1RPF X-ray 2.20 A 27-150 [» ]
1RPG X-ray 1.40 A 27-150 [» ]
1RPH X-ray 2.20 A 27-150 [» ]
1RSM X-ray 2.00 A 27-150 [» ]
1RTA X-ray 2.50 E 27-150 [» ]
1RTB X-ray 2.50 A 27-150 [» ]
1RUV X-ray 1.25 A 27-150 [» ]
1SRN X-ray 1.80 A 27-144 [» ]
B 137-150 [» ]
1SSA X-ray 2.00 A 27-144 [» ]
B 137-150 [» ]
1SSB X-ray 2.00 A 27-144 [» ]
B 137-150 [» ]
1SSC X-ray 2.00 A 27-138 [» ]
B 140-150 [» ]
1U1B X-ray 2.00 A/B 27-150 [» ]
1UN5 X-ray 2.60 A - [» ]
1W4O X-ray 1.60 A/B 27-150 [» ]
1W4P X-ray 1.69 A/B 27-150 [» ]
1W4Q X-ray 1.68 A/B 27-150 [» ]
1WBU X-ray 1.90 A/B 27-150 [» ]
1XPS X-ray 1.80 A/B 27-150 [» ]
1XPT X-ray 1.90 A/B 27-150 [» ]
1YMN X-ray 1.45 A 27-150 [» ]
1YMR X-ray 1.50 A 27-150 [» ]
1YMW X-ray 1.50 A 27-150 [» ]
1Z3L X-ray 1.80 E 47-150 [» ]
S 27-41 [» ]
1Z3M X-ray 2.00 E 47-150 [» ]
S 27-41 [» ]
1Z3P X-ray 2.00 E 47-150 [» ]
S 27-41 [» ]
1Z6D X-ray 1.54 A/B 27-150 [» ]
1Z6S X-ray 1.50 A/B 27-150 [» ]
2AAS NMR - A 27-150 [» ]
2APQ X-ray 1.80 A 27-150 [» ]
2APU model - 0/1/2/3/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x/y/z 27-150 [» ]
2BLP X-ray 1.40 A 27-150 [» ]
2BLZ X-ray 1.40 A 27-150 [» ]
2E33 X-ray 2.70 B 27-150 [» ]
2E3W X-ray 1.05 A 27-150 [» ]
2G4W X-ray 1.84 A/B 27-150 [» ]
2G4X X-ray 1.95 A 27-150 [» ]
2G8Q X-ray 1.50 A/B 27-150 [» ]
2G8R X-ray 1.70 A/B 27-150 [» ]
2NUI X-ray 1.10 A 27-150 [» ]
2OP2 X-ray 1.60 A 27-150 [» ]
2OQF X-ray 2.30 A/B/C/D 27-150 [» ]
2P42 X-ray 1.80 A/C 27-150 [» ]
2P43 X-ray 1.65 A 27-150 [» ]
2P44 X-ray 1.80 A 27-150 [» ]
2P45 X-ray 1.10 A 27-150 [» ]
2P46 X-ray 2.50 A/C 27-150 [» ]
2P47 X-ray 2.50 A 27-150 [» ]
2P48 X-ray 2.30 A 27-150 [» ]
2P49 X-ray 1.38 A 27-150 [» ]
2P4A X-ray 1.90 A/C 27-150 [» ]
2QCA X-ray 1.33 A 27-150 [» ]
2RAT X-ray 1.50 A 27-150 [» ]
2RLN X-ray 1.85 E 42-150 [» ]
S 27-41 [» ]
2RNS X-ray 1.60 A 27-150 [» ]
2W5G X-ray 1.70 A/B 27-150 [» ]
2W5I X-ray 2.40 A/B 27-150 [» ]
2W5K X-ray 1.70 A/B 27-150 [» ]
2W5L X-ray 1.70 A/B 27-150 [» ]
2W5M X-ray 1.80 A/B 27-150 [» ]
2XOG X-ray 1.72 A/B 27-150 [» ]
2XOI X-ray 1.72 A/B 27-150 [» ]
3A1R neutron diffraction 1.70 A 27-150 [» ]
3D6O X-ray 1.58 A/B 27-150 [» ]
3D6P X-ray 1.60 A/B 27-150 [» ]
3D6Q X-ray 1.60 A/B 27-150 [» ]
3D7B X-ray 1.60 A/B 27-150 [» ]
3D8Y X-ray 1.72 A/B 27-150 [» ]
3D8Z X-ray 1.98 A/B 27-150 [» ]
3DH5 X-ray 1.60 A 27-150 [» ]
3DH6 X-ray 1.60 A 27-150 [» ]
3DI7 X-ray 1.60 A 27-150 [» ]
3DI8 X-ray 1.60 A 27-150 [» ]
3DI9 X-ray 2.00 A 27-150 [» ]
3DIB X-ray 1.40 A 27-150 [» ]
3DIC X-ray 1.60 A 27-150 [» ]
3DXG X-ray 1.39 A/B 27-150 [» ]
3DXH X-ray 1.40 A/B 27-150 [» ]
3EUX X-ray 1.65 A/B 27-150 [» ]
3EUY X-ray 1.95 A/B 27-150 [» ]
3EUZ X-ray 1.84 A/B 27-150 [» ]
3EV0 X-ray 1.76 A/B 27-150 [» ]
3EV1 X-ray 2.00 A/B 27-150 [» ]
3EV2 X-ray 2.02 A/B 27-150 [» ]
3EV3 X-ray 1.68 A/B 27-150 [» ]
3EV4 X-ray 1.93 A/B 27-150 [» ]
3EV5 X-ray 1.68 A/B 27-150 [» ]
3EV6 X-ray 1.76 A/B 27-150 [» ]
3FKZ X-ray 1.99 A/B 27-150 [» ]
3FL0 X-ray 1.94 A/B 27-150 [» ]
3FL1 X-ray 1.90 A/B 27-150 [» ]
3FL3 X-ray 1.60 A/B 27-150 [» ]
3I67 X-ray 1.30 A 27-150 [» ]
3I6F X-ray 1.30 A 27-150 [» ]
3I6H X-ray 1.30 A 27-150 [» ]
3I6J X-ray 1.30 A 27-150 [» ]
3I7W X-ray 2.35 A 27-150 [» ]
3I7X X-ray 2.60 A 27-150 [» ]
3I7Y X-ray 2.40 A 27-150 [» ]
3JW1 X-ray 1.60 A/B 27-150 [» ]
3LXO X-ray 1.55 A 27-150 [» ]
3MWQ X-ray 1.68 A 26-150 [» ]
3MWR X-ray 1.85 A 27-150 [» ]
3MX8 X-ray 2.10 A 26-150 [» ]
3MZQ X-ray 1.50 A 23-150 [» ]
3MZR X-ray 1.50 A 23-150 [» ]
3OQY X-ray 1.49 A/B 47-150 [» ]
a/b 27-41 [» ]
3OQZ X-ray 2.50 A/B 47-150 [» ]
a/b 27-41 [» ]
3OR0 X-ray 2.30 A/B 47-150 [» ]
a/b 27-41 [» ]
3QL1 X-ray 1.29 A 27-150 [» ]
3QL2 X-ray 1.49 A/B 27-150 [» ]
3QSK X-ray 1.75 A 27-150 [» ]
3RAT X-ray 1.50 A 27-150 [» ]
3RH1 X-ray 2.10 A 27-150 [» ]
3RID X-ray 2.18 A/B/C/D 27-150 [» ]
3RN3 X-ray 1.45 A 27-150 [» ]
3RSD X-ray 1.60 A 27-150 [» ]
3RSK X-ray 2.00 A 27-150 [» ]
3RSP X-ray 1.70 A 27-150 [» ]
3SRN X-ray 2.00 A 27-139 [» ]
B 140-146 [» ]
4AO1 X-ray 1.58 A 27-150 [» ]
4G8V X-ray 1.70 A/B 27-150 [» ]
4G8Y X-ray 1.80 A/B 27-150 [» ]
4G90 X-ray 1.90 A/B 27-150 [» ]
4J5Z X-ray 1.80 A 27-150 [» ]
4J60 X-ray 1.69 A 27-150 [» ]
4J61 X-ray 1.69 A 27-150 [» ]
4J62 X-ray 2.04 A 27-150 [» ]
4J63 X-ray 2.04 A 27-150 [» ]
4J64 X-ray 1.78 A 27-150 [» ]
4J65 X-ray 1.96 A 27-150 [» ]
4J66 X-ray 2.04 A 27-150 [» ]
4J67 X-ray 1.86 A 27-150 [» ]
4J68 X-ray 1.78 A 27-150 [» ]
4J69 X-ray 1.89 A 27-150 [» ]
4J6A X-ray 2.04 A 27-150 [» ]
4K7L X-ray 1.38 A 27-41 [» ]
B 47-150 [» ]
4K7M X-ray 1.80 A 27-150 [» ]
4L55 X-ray 1.65 A/B 27-150 [» ]
4MXF X-ray 2.25 A/B 27-150 [» ]
4O36 X-ray 1.22 A 27-41 [» ]
B 47-150 [» ]
4O37 X-ray 1.40 A 27-41 [» ]
B 47-150 [» ]
4RAT X-ray 1.50 A 27-150 [» ]
4RSD X-ray 1.60 A 27-150 [» ]
4RSK X-ray 2.10 A 27-150 [» ]
4SRN X-ray 2.00 A 27-139 [» ]
B 140-150 [» ]
5RAT X-ray 1.50 A 27-150 [» ]
5RSA X-ray 2.00 A 27-150 [» ]
6RAT X-ray 1.50 A 27-150 [» ]
6RSA X-ray 2.00 A 27-150 [» ]
7RAT X-ray 1.50 A 27-150 [» ]
7RSA X-ray 1.26 A 27-150 [» ]
8RAT X-ray 1.50 A 27-150 [» ]
8RSA X-ray 1.80 A/B 27-150 [» ]
9RAT X-ray 1.50 A 27-150 [» ]
9RSA X-ray 1.80 A/B 27-150 [» ]
ProteinModelPortali P61823.
SMRi P61823. Positions 27-150.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 159601. 1 interaction.
IntActi P61823. 6 interactions.
MINTi MINT-1510416.
STRINGi 9913.ENSBTAP00000011586.

Chemistry

BindingDBi P61823.
ChEMBLi CHEMBL6091.
DrugBanki DB00536. Guanidine.
DB00128. L-Aspartic Acid.

Proteomic databases

PaxDbi P61823.
PRIDEi P61823.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000011586 ; ENSBTAP00000011586 ; ENSBTAG00000008793 .
GeneIDi 282340.
KEGGi bta:282340.

Organism-specific databases

CTDi 6035.

Phylogenomic databases

eggNOGi NOG40319.
GeneTreei ENSGT00390000007840.
HOGENOMi HOG000276883.
HOVERGENi HBG008396.
InParanoidi P61823.
KOi K01168.
OMAi ANKHIIV.
OrthoDBi EOG7J1826.
TreeFami TF333393.

Enzyme and pathway databases

BRENDAi 3.1.27.5. 908.
SABIO-RK P61823.

Miscellaneous databases

EvolutionaryTracei P61823.
NextBioi 20806135.
PMAP-CutDB P61823.

Family and domain databases

Gene3Di 3.10.130.10. 1 hit.
InterProi IPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view ]
PANTHERi PTHR11437. PTHR11437. 1 hit.
Pfami PF00074. RnaseA. 1 hit.
[Graphical view ]
PRINTSi PR00794. RIBONUCLEASE.
ProDomi PD000535. RNaseA. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00092. RNAse_Pc. 1 hit.
[Graphical view ]
SUPFAMi SSF54076. SSF54076. 1 hit.
PROSITEi PS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the bovine pancreatic ribonuclease gene: the unique intervening sequence in the 5' untranslated region contains a promoter-like element."
    Carsana A., Confalone E., Palmieri M., Libonati M., Furia A.
    Nucleic Acids Res. 16:5491-5502(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal pancreas.
  3. "Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11."
    Delcardayre S.B., Ribo M., Yokel E.M., Quirk D.J., Rutter W.J., Raines R.T.
    Protein Eng. 8:261-273(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-150, FUNCTION.
  4. "The sequence of amino acid residues in bovine pancreatic ribonuclease: revisions and confirmations."
    Smyth D.G., Stein W.H., Moore S.
    J. Biol. Chem. 238:227-234(1963) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-150, DISULFIDE BONDS.
    Tissue: Pancreas.
  5. "On the structure of bovine pancreatic ribonuclease B. Isolation of a glycopeptide."
    Plummer T.H. Jr., Hirs C.H.W.
    J. Biol. Chem. 239:2530-2538(1964) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-150.
    Tissue: Pancreas.
  6. "Molecular evolution of genes encoding ribonucleases in ruminant species."
    Confalone E., Beintema J.J., Sasso M.P., Carsana A., Palmieri M., Vento M.T., Furia A.
    J. Mol. Evol. 41:850-858(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-150.
  7. "The reactivities of the histidine residues at the active site of ribonuclease toward halo acids of different structures."
    Heinrikson R.L., Stein W.H., Crestfield A.M., Moore S.
    J. Biol. Chem. 240:2921-2934(1965) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  8. "Heavy atom-labelled derivatives of bovine pancreatic ribonuclease. I. Specific reactions of ribonuclease with N-acetylhomocysteine thiolactone and silver ion."
    Shall S., Barnard E.A.
    J. Mol. Biol. 41:237-251(1969) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  9. "Glycation of amino groups in protein. Studies on the specificity of modification of RNase by glucose."
    Watkins N.G., Thorpe S.R., Baynes J.W.
    J. Biol. Chem. 260:10629-10636(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCATION AT LYS-27; LYS-33; LYS-63 AND LYS-67.
  10. "The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease."
    McPherson A., Brayer G., Cascio D., Williams R.
    Science 232:765-768(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  11. "Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS: strong correlation between signal strength and glycoform quantities."
    Thaysen-Andersen M., Mysling S., Hojrup P.
    Anal. Chem. 81:3933-3943(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-60.
  12. "The three-dimensional structure of ribonuclease-S. Interpretation of an electron density map at a nominal resolution of 2 A."
    Wyckoff H.W., Tsernoglou D., Hanson A.W., Knox J.R., Lee B., Richards F.M.
    J. Biol. Chem. 245:305-328(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  13. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  14. "The refined crystal structure of ribonuclease A at 2.0-A resolution."
    Wlodawer A., Bott R., Sjoelin L.
    J. Biol. Chem. 257:1325-1332(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  15. "Structure of phosphate-free ribonuclease A refined at 1.26 A."
    Wlodawer A., Svensson L.A., Sjoelin L., Gilliland G.L.
    Biochemistry 27:2705-2717(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS).
  16. "Crystal structures of ribonuclease A complexes with 5'-diphosphoadenosine 3'-phosphate and 5'-diphosphoadenosine 2'-phosphate at 1.7-A resolution."
    Leonidas D.D., Shapiro R., Irons L.I., Russo N., Acharya K.R.
    Biochemistry 36:5578-5588(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  17. "Excavating an active site: the nucleobase specificity of ribonuclease A."
    Kelemen B.R., Schultz L.W., Sweeney R.Y., Raines R.T.
    Biochemistry 39:14487-14494(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-125 OF MUTANT GLY-67.
  18. "Contribution of the active site histidine residues of ribonuclease A to nucleic acid binding."
    Park C., Schultz L.W., Raines R.T.
    Biochemistry 40:4949-4956(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS ALA-38 AND ALA-145.
  19. "Cleavage of 3',5'-pyrophosphate-linked dinucleotides by ribonuclease A and angiogenin."
    Jardine A.M., Leonidas D.D., Jenkins J.L., Park C., Raines R.T., Acharya K.R., Shapiro R.
    Biochemistry 40:10262-10272(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
  20. "Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease A as revealed by crystallographic study of three Phe120 mutants at 1.4 A resolution."
    Chatani E., Hayashi R., Moriyama H., Ueki T.
    Protein Sci. 11:72-81(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF MUTANTS ALA-120; PHE-120 AND TRP-120.
  21. "Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution."
    Robertson A.D., Purisima E.O., Eastman M.A., Scheraga H.A.
    Biochemistry 28:5930-5938(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  22. "Sequential 1H-NMR assignment and solution structure of bovine pancreatic ribonuclease A."
    Rico M., Bruix M., Santoro J., Gonzalez C., Neira J.L., Nieto J.L., Herranz J.
    Eur. J. Biochem. 183:623-638(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  23. "3D structure of bovine pancreatic ribonuclease A in aqueous solution: an approach to tertiary structure determination from a small basis of 1H NMR NOE correlations."
    Rico M., Santoro J., Gonzalez C., Bruix M., Neira J.L., Nieto J.L., Herranz J.
    J. Biomol. NMR 1:283-298(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiRNAS1_BOVIN
AccessioniPrimary (citable) accession number: P61823
Secondary accession number(s): A6QPW8, P00656, Q9TSF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2004
Last modified: September 3, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Ribonuclease can destabilize or unwind the DNA helix by complexing with single-stranded DNA; this complex arises by an extended multisite cation-anion interaction between the lysine and arginine residues of the enzyme and the phosphate groups of the nucleotides.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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