Ribonuclease inhibitor - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Ribonuclease inhibitor
Alternative name(s):
    Ribonuclease/angiogenin inhibitor 1
      Short name=RAI
    Placental ribonuclease inhibitor
      Short name=RNase inhibitor
      Short name=RI

Gene names

Name:	RNH1
Synonyms:	PRI, RNH

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Inhibitor of pancreatic RNase and angiogenin. May also function in the modulation of cellular activities.
Subunit structure	Forms a tight one-to-one complex with the RNase.
Subcellular location	Cytoplasm.
Post-translational modification	The N-terminus is blocked. At least 30 of the 32 cysteine residues are in the reduced form.
Sequence similarities	Contains 15 LRR (leucine-rich) repeats.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Leucine-rich repeat Repeat
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	mRNA catabolic process Non-traceable author statement. Source: UniProtKB regulation of angiogenesis Inferred from direct assay. Source: UniProtKB
Cellular component	angiogenin-PRI complex Inferred from physical interaction. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB ribonuclease inhibitor activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed

Chain

2 – 461

460

Ribonuclease inhibitor

PRO_0000097343

Regions

Repeat

20 – 48

29

LRR 1

Repeat

49 – 76

28

LRR 2

Repeat

77 – 105

29

LRR 3

Repeat

106 – 133

28

LRR 4

Repeat

134 – 162

29

LRR 5

Repeat

163 – 190

28

LRR 6

Repeat

191 – 219

29

LRR 7

Repeat

220 – 247

28

LRR 8

Repeat

248 – 276

29

LRR 9

Repeat

277 – 304

28

LRR 10

Repeat

305 – 333

29

LRR 11

Repeat

334 – 361

28

LRR 12

Repeat

362 – 390

29

LRR 13

Repeat

391 – 418

28

LRR 14

Repeat

419 – 447

29

LRR 15

Region

2 – 11

10

2 X 5 AA tandem repeats of S-L-D-I-Q

Natural variations

Natural variant

170

1

P → L: dbSNP rs17585.

VAR_014726

Experimental info

Sequence conflict

423 – 424

2

RQ → SE in CAA32151 and AAA60249. Ref.2

Secondary structure

1

.

461

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P13489-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5E88CDAC95BAE5B3
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FASTA

461

49,973

        10         20         30         40         50         60 
MSLDIQSLDI QCEELSDARW AELLPLLQQC QVVRLDDCGL TEARCKDISS ALRVNPALAE 

        70         80         90        100        110        120 
LNLRSNELGD VGVHCVLQGL QTPSCKIQKL SLQNCCLTGA GCGVLSSTLR TLPTLQELHL 

       130        140        150        160        170        180 
SDNLLGDAGL QLLCEGLLDP QCRLEKLQLE YCSLSAASCE PLASVLRAKP DFKELTVSNN 

       190        200        210        220        230        240 
DINEAGVRVL CQGLKDSPCQ LEALKLESCG VTSDNCRDLC GIVASKASLR ELALGSNKLG 

       250        260        270        280        290        300 
DVGMAELCPG LLHPSSRLRT LWIWECGITA KGCGDLCRVL RAKESLKELS LAGNELGDEG 

       310        320        330        340        350        360 
ARLLCETLLE PGCQLESLWV KSCSFTAACC SHFSSVLAQN RFLLELQISN NRLEDAGVRE 

       370        380        390        400        410        420 
LCQGLGQPGS VLRVLWLADC DVSDSSCSSL AATLLANHSL RELDLSNNCL GDAGILQLVE 

       430        440        450        460 
SVRQPGCLLE QLVLYDIYWS EEMEDRLQAL EKDKPSLRVI S

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of human placental ribonuclease inhibitor." Lee F.S., Fox E.A., Zhou H.-M., Strydom D.J., Vallee B.L. Biochemistry 27:8545-8553(1988) [PubMed: 3219362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, OXIDATION STATE OF THE CYSTEINES. Tissue: Placenta.
[2]	"The primary structure of human ribonuclease/angiogenin inhibitor (RAI) discloses a novel highly diversified protein superfamily with a common repetitive module." Schneider R., Schneider-Scherzer E., Thurnher M., Auer B., Schweiger M. EMBO J. 7:4151-4156(1988) [PubMed: 3243277] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 444-462.
[3]	The German cDNA consortium Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Lymph and Ovary.
[5]	"Purification and characterization of human brain ribonuclease inhibitor." Nadano D., Yasuda T., Takeshita H., Uchide K., Kishi K. Arch. Biochem. Biophys. 312:421-428(1994) [PubMed: 8037455] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14. Tissue: Brain.
[6]	"Molecular recognition of human angiogenin by placental ribonuclease inhibitor -- an X-ray crystallographic study at 2.0-A resolution." Papageorgiou A.C., Shapiro R., Acharya K.R. EMBO J. 16:5162-5177(1997) [PubMed: 9311977] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH ANGIOGENIN.
+	Additional computationally mapped references.