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Protein

Ran GTPase-activating protein 1

Gene

rna1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTPase activator for the nuclear Ras-related regulatory protein spi1 (Ran), converting it to the putatively inactive GDP-bound state.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei74 – 741Critical residue for GTP hydrolysis

GO - Molecular functioni

  • GTPase activator activity Source: PomBase

GO - Biological processi

  • chromatin silencing at centromere Source: PomBase
  • kinetochore organization Source: PomBase
  • mitotic sister chromatid segregation Source: PomBase
  • nucleocytoplasmic transport Source: PomBase
  • positive regulation of protein export from nucleus Source: PomBase
  • regulation of GTPase activity Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Ran GTPase-activating protein 1
Short name:
Protein rna1
Gene namesi
Name:rna1
ORF Names:SPAC22E12.07
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC22E12.07.
PomBaseiSPAC22E12.07. rna1.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric region Source: GOC
  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nuclear membrane Source: PomBase
  • nucleus Source: PomBase
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386Ran GTPase-activating protein 1PRO_0000056741Add
BLAST

Proteomic databases

MaxQBiP41391.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi278353. 16 interactions.
IntActiP41391. 1 interaction.
MINTiMINT-4690066.

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi12 – 154Combined sources
Helixi19 – 224Combined sources
Helixi23 – 253Combined sources
Helixi26 – 305Combined sources
Beta strandi36 – 383Combined sources
Beta strandi42 – 443Combined sources
Helixi46 – 549Combined sources
Turni55 – 584Combined sources
Beta strandi64 – 663Combined sources
Helixi76 – 783Combined sources
Helixi80 – 9011Combined sources
Beta strandi98 – 1003Combined sources
Turni108 – 1103Combined sources
Helixi111 – 12010Combined sources
Beta strandi126 – 1283Combined sources
Helixi135 – 15622Combined sources
Beta strandi163 – 1653Combined sources
Helixi173 – 1753Combined sources
Helixi176 – 18510Combined sources
Beta strandi191 – 1933Combined sources
Helixi201 – 2099Combined sources
Helixi212 – 2143Combined sources
Beta strandi220 – 2223Combined sources
Helixi229 – 23911Combined sources
Helixi240 – 2423Combined sources
Beta strandi248 – 2503Combined sources
Helixi258 – 26912Combined sources
Beta strandi278 – 2803Combined sources
Helixi288 – 30114Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi313 – 3153Combined sources
Helixi320 – 33213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5DX-ray2.70C/F/I/L1-386[»]
1K5GX-ray3.10C/F/I/L1-386[»]
1YRGX-ray2.66A/B2-386[»]
2CA6X-ray2.20A/B1-386[»]
ProteinModelPortaliP41391.
SMRiP41391. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41391.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati23 – 4826LRR 1Add
BLAST
Repeati85 – 11228LRR 2Add
BLAST
Repeati113 – 14129LRR 3Add
BLAST
Repeati179 – 20628LRR 4Add
BLAST
Repeati207 – 23529LRR 5Add
BLAST
Repeati236 – 26429LRR 6Add
BLAST
Repeati265 – 29329LRR 7Add
BLAST
Repeati294 – 32229LRR 8Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi323 – 37452Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the RNA1 family.Curated
Contains 8 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

HOGENOMiHOG000195026.
InParanoidiP41391.
KOiK14319.
OMAiWANIQEL.
OrthoDBiEOG71ZPB0.
PhylomeDBiP41391.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR027038. RanGap.
[Graphical view]
PANTHERiPTHR24113. PTHR24113. 1 hit.

Sequencei

Sequence statusi: Complete.

P41391-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRFSIEGKS LKLDAITTED EKSVFAVLLE DDSVKEIVLS GNTIGTEAAR
60 70 80 90 100
WLSENIASKK DLEIAEFSDI FTGRVKDEIP EALRLLLQAL LKCPKLHTVR
110 120 130 140 150
LSDNAFGPTA QEPLIDFLSK HTPLEHLYLH NNGLGPQAGA KIARALQELA
160 170 180 190 200
VNKKAKNAPP LRSIICGRNR LENGSMKEWA KTFQSHRLLH TVKMVQNGIR
210 220 230 240 250
PEGIEHLLLE GLAYCQELKV LDLQDNTFTH LGSSALAIAL KSWPNLRELG
260 270 280 290 300
LNDCLLSARG AAAVVDAFSK LENIGLQTLR LQYNEIELDA VRTLKTVIDE
310 320 330 340 350
KMPDLLFLEL NGNRFSEEDD VVDEIREVFS TRGRGELDEL DDMEELTDEE
360 370 380
EEDEEEEAES QSPEPETSEE EKEDKELADE LSKAHI
Length:386
Mass (Da):43,236
Last modified:November 1, 1995 - v1
Checksum:i8E1C9C506988A7F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69882 Genomic DNA. Translation: CAA49509.1.
CU329670 Genomic DNA. Translation: CAA93894.1.
PIRiS37691.
RefSeqiNP_594833.1. NM_001020262.2.

Genome annotation databases

EnsemblFungiiSPAC22E12.07.1; SPAC22E12.07.1:pep; SPAC22E12.07.
GeneIDi2541863.
KEGGispo:SPAC22E12.07.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69882 Genomic DNA. Translation: CAA49509.1.
CU329670 Genomic DNA. Translation: CAA93894.1.
PIRiS37691.
RefSeqiNP_594833.1. NM_001020262.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5DX-ray2.70C/F/I/L1-386[»]
1K5GX-ray3.10C/F/I/L1-386[»]
1YRGX-ray2.66A/B2-386[»]
2CA6X-ray2.20A/B1-386[»]
ProteinModelPortaliP41391.
SMRiP41391. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278353. 16 interactions.
IntActiP41391. 1 interaction.
MINTiMINT-4690066.

Proteomic databases

MaxQBiP41391.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC22E12.07.1; SPAC22E12.07.1:pep; SPAC22E12.07.
GeneIDi2541863.
KEGGispo:SPAC22E12.07.

Organism-specific databases

EuPathDBiFungiDB:SPAC22E12.07.
PomBaseiSPAC22E12.07. rna1.

Phylogenomic databases

HOGENOMiHOG000195026.
InParanoidiP41391.
KOiK14319.
OMAiWANIQEL.
OrthoDBiEOG71ZPB0.
PhylomeDBiP41391.

Miscellaneous databases

EvolutionaryTraceiP41391.
PROiP41391.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR027038. RanGap.
[Graphical view]
PANTHERiPTHR24113. PTHR24113. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A functional homologue of the RNA1 gene product in Schizosaccharomyces pombe: purification, biochemical characterization, and identification of a leucine-rich repeat motif."
    Melchior F., Weber K., Gerke V.
    Mol. Biol. Cell 4:569-581(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport."
    Bischoff F.R., Krebber H., Kempf T., Hermes I., Ponstingl H.
    Proc. Natl. Acad. Sci. U.S.A. 92:1749-1753(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE.
    Strain: 972 / ATCC 24843.
  4. "The crystal structure of rna1p: a new fold for a GTPase-activating protein."
    Hillig R.C., Renault L., Vetter I.R., Drell T. IV, Wittinghofer A., Becker J.
    Mol. Cell 3:781-791(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS).

Entry informationi

Entry nameiRNA1_SCHPO
AccessioniPrimary (citable) accession number: P41391
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.