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Protein

Ribonuclease 7

Gene

RNASE7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits a potent RNase activity. Has broad-spectrum antimicrobial activity against many pathogenic microorganisms and remarkably potent activity (lethal dose of 90% < 30 nM) against a vancomycin resistant Enterococcus faecium.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei43 – 431Proton acceptorBy similarity
Binding sitei91 – 911SubstrateBy similarity
Active sitei151 – 1511Proton donorBy similarity

GO - Molecular functioni

  • endonuclease activity Source: GO_Central
  • lipopolysaccharide binding Source: UniProtKB
  • nucleic acid binding Source: InterPro
  • peptidoglycan binding Source: UniProtKB
  • ribonuclease activity Source: UniProtKB

GO - Biological processi

  • antibacterial humoral response Source: UniProtKB
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • innate immune response Source: UniProtKB
  • membrane disruption in other organism Source: UniProtKB
  • nucleic acid phosphodiester bond hydrolysis Source: GOC
  • response to bacterium Source: UniProtKB
  • RNA phosphodiester bond hydrolysis Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Endonuclease, Hydrolase, Nuclease

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease 7 (EC:3.1.27.-)
Short name:
RNase 7
Alternative name(s):
Skin-derived antimicrobial protein 2
Short name:
SAP-2
Gene namesi
Name:RNASE7
ORF Names:UNQ2516/PRO6006
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:19278. RNASE7.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134939592.

Polymorphism and mutation databases

BioMutaiRNASE7.
DMDMi296452879.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 156128Ribonuclease 7PRO_0000030901Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 1091 Publication
Disulfide bondi65 ↔ 1191 Publication
Disulfide bondi83 ↔ 1341 Publication
Disulfide bondi90 ↔ 971 Publication
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9H1E1.
PaxDbiQ9H1E1.
PRIDEiQ9H1E1.

PTM databases

iPTMnetiQ9H1E1.
PhosphoSiteiQ9H1E1.

Expressioni

Tissue specificityi

Expressed in various epithelial tissues including skin, respiratory tract, genito-urinary tract and, at a low level, in the gut. Expressed in liver, kidney, skeletal muscle and heart.2 Publications

Gene expression databases

BgeeiQ9H1E1.
CleanExiHS_RNASE7.
GenevisibleiQ9H1E1. HS.

Organism-specific databases

HPAiCAB062560.
CAB068225.
HPA005690.

Interactioni

Protein-protein interaction databases

BioGridi124179. 21 interactions.
STRINGi9606.ENSP00000298690.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 439Combined sources
Helixi50 – 6213Combined sources
Beta strandi67 – 726Combined sources
Helixi76 – 827Combined sources
Beta strandi90 – 934Combined sources
Beta strandi97 – 993Combined sources
Beta strandi104 – 11411Combined sources
Beta strandi120 – 1289Combined sources
Beta strandi130 – 1356Combined sources
Beta strandi146 – 15510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HKYNMR-A29-156[»]
ProteinModelPortaliQ9H1E1.
SMRiQ9H1E1. Positions 29-156.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H1E1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 705Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IXRT. Eukaryota.
ENOG4111AZ3. LUCA.
GeneTreeiENSGT00840000129759.
HOGENOMiHOG000276882.
HOVERGENiHBG008396.
InParanoidiQ9H1E1.
KOiK01172.
OMAiIVACKPP.
OrthoDBiEOG7J1826.
PhylomeDBiQ9H1E1.
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.

Q9H1E1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPARAGFCP LLLLLLLGLW VAEIPVSAKP KGMTSSQWFK IQHMQPSPQA
60 70 80 90 100
CNSAMKNINK HTKRCKDLNT FLHEPFSSVA ATCQTPKIAC KNGDKNCHQS
110 120 130 140 150
HGAVSLTMCK LTSGKHPNCR YKEKRQNKSY VVACKPPQKK DSQQFHLVPV

HLDRVL
Length:156
Mass (Da):17,419
Last modified:May 18, 2010 - v2
Checksum:iA8659D3EECEF4054
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031A → P.4 Publications
Corresponds to variant rs1263872 [ dbSNP | Ensembl ].
VAR_024619
Natural varianti116 – 1161H → Y.4 Publications
Corresponds to variant rs1243469 [ dbSNP | Ensembl ].
VAR_024620

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131212 mRNA. Translation: CAC20410.1.
AJ306608 mRNA. Translation: CAC84462.1.
AJ306609 mRNA. Translation: CAC84457.1.
AJ306610 mRNA. Translation: CAC84458.1.
AY170392 mRNA. Translation: AAO12510.1.
AY359097 mRNA. Translation: AAQ89455.1.
AL161668 Genomic DNA. No translation available.
BC074960 mRNA. Translation: AAH74960.1.
BC112334 mRNA. Translation: AAI12335.1.
CCDSiCCDS41914.1.
RefSeqiNP_115961.2. NM_032572.3.
UniGeneiHs.525206.

Genome annotation databases

EnsembliENST00000298690; ENSP00000298690; ENSG00000165799.
ENST00000481538; ENSP00000431382; ENSG00000165799.
GeneIDi84659.
KEGGihsa:84659.
UCSCiuc001vzk.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131212 mRNA. Translation: CAC20410.1.
AJ306608 mRNA. Translation: CAC84462.1.
AJ306609 mRNA. Translation: CAC84457.1.
AJ306610 mRNA. Translation: CAC84458.1.
AY170392 mRNA. Translation: AAO12510.1.
AY359097 mRNA. Translation: AAQ89455.1.
AL161668 Genomic DNA. No translation available.
BC074960 mRNA. Translation: AAH74960.1.
BC112334 mRNA. Translation: AAI12335.1.
CCDSiCCDS41914.1.
RefSeqiNP_115961.2. NM_032572.3.
UniGeneiHs.525206.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HKYNMR-A29-156[»]
ProteinModelPortaliQ9H1E1.
SMRiQ9H1E1. Positions 29-156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124179. 21 interactions.
STRINGi9606.ENSP00000298690.

PTM databases

iPTMnetiQ9H1E1.
PhosphoSiteiQ9H1E1.

Polymorphism and mutation databases

BioMutaiRNASE7.
DMDMi296452879.

Proteomic databases

MaxQBiQ9H1E1.
PaxDbiQ9H1E1.
PRIDEiQ9H1E1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298690; ENSP00000298690; ENSG00000165799.
ENST00000481538; ENSP00000431382; ENSG00000165799.
GeneIDi84659.
KEGGihsa:84659.
UCSCiuc001vzk.4. human.

Organism-specific databases

CTDi84659.
GeneCardsiRNASE7.
H-InvDBHIX0131226.
HGNCiHGNC:19278. RNASE7.
HPAiCAB062560.
CAB068225.
HPA005690.
MIMi612484. gene.
neXtProtiNX_Q9H1E1.
PharmGKBiPA134939592.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IXRT. Eukaryota.
ENOG4111AZ3. LUCA.
GeneTreeiENSGT00840000129759.
HOGENOMiHOG000276882.
HOVERGENiHBG008396.
InParanoidiQ9H1E1.
KOiK01172.
OMAiIVACKPP.
OrthoDBiEOG7J1826.
PhylomeDBiQ9H1E1.
TreeFamiTF333393.

Miscellaneous databases

EvolutionaryTraceiQ9H1E1.
GenomeRNAii84659.
PROiQ9H1E1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H1E1.
CleanExiHS_RNASE7.
GenevisibleiQ9H1E1. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin."
    Harder J., Schroeder J.M.
    J. Biol. Chem. 277:46779-46784(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANTS PRO-103 AND TYR-116.
  2. "Human RNase 7: a new cationic ribonuclease of the RNase A superfamily."
    Zhang J., Dyer K.D., Rosenberg H.F.
    Nucleic Acids Res. 31:602-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANTS PRO-103 AND TYR-116.
    Tissue: Kidney.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS PRO-103 AND TYR-116.
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS PRO-103 AND TYR-116.
  6. Harder J., Bartels J., Christophers E., Schroeder J.M.
    Submitted (MAR-1997) to UniProtKB
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 30-70.
    Tissue: Keratinocyte.
  7. "The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity."
    Huang Y.-C., Lin Y.-M., Chang T.-W., Wu S.-J., Lee Y.-S., Chang M.D.-S., Chen C., Wu S.-H., Liao Y.-D.
    J. Biol. Chem. 282:4626-4633(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 29-156, DISULFIDE BONDS, FUNCTION.

Entry informationi

Entry nameiRNAS7_HUMAN
AccessioniPrimary (citable) accession number: Q9H1E1
Secondary accession number(s): P80927, P83685, Q546N3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 19, 2001
Last sequence update: May 18, 2010
Last modified: June 8, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.