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P70425 (RIT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP-binding protein Rit2
Alternative name(s):
Ras-like protein expressed in neurons
Ras-like without CAAX protein 2
Gene names
Name:Rit2
Synonyms:Rin, Roc2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds and exchanges GTP and GDP.

Enzyme regulation

Alternates between an inactive form bound to GDP and an active form bound to GTP.

Subunit structure

Interacts with PLXNB3 By similarity. Interacts with MLLT4, the C-terminal domain of RALGDS and RLF, but not with RIN1 and PIK3CA. RLF binds exclusively to the active GTP-bound form. Binds calmodulin. Ref.2

Subcellular location

Nucleus By similarity. Cell membrane. Note: Colocalizes with PLXNB3 at the plasma membrane By similarity.

Tissue specificity

Neuron-specific.

Miscellaneous

Shows rapid uncatalyzed guanine nucleotide dissociation rates, which are much faster than those of most Ras subfamily members.

Sequence similarities

Belongs to the small GTPase superfamily. Ras family.

Sequence caution

The sequence BAE23581.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RLFQ131292EBI-2649620,EBI-958266From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217GTP-binding protein Rit2
PRO_0000082728

Regions

Nucleotide binding27 – 348GTP By similarity
Nucleotide binding74 – 785GTP By similarity
Nucleotide binding133 – 1364GTP By similarity

Experimental info

Mutagenesis341S → N: Dominant negative. Loss of interaction with MLLT4, RLF and RALGDS. Ref.2
Mutagenesis521T → A: Loss of interaction with MLLT4, RLF and RALGDS; when associated with L-78. Ref.2
Mutagenesis781Q → L: Constitutively active. Dramatic reduction of the rate of GTP hydrolysis. Ref.2
Sequence conflict31V → A in AAD13022. Ref.2
Sequence conflict1501N → T in AAD13022. Ref.2
Sequence conflict1761G → S in BAC32750. Ref.3
Sequence conflict2171L → I in AAD13022. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P70425 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 189AA6DCCE75034F

FASTA21724,802
        10         20         30         40         50         60 
MEVENEAHCC PGSSSGGSRE YKVVMLGAGG VGKSAVTMQF ISHQFPDYHD PTIEDAYKTQ 

        70         80         90        100        110        120 
VRIDNEPAYL DILDTAGQAE FTAMREQYMR GGEGFIICYS VTDRQSFQEA AKFKELIFQV 

       130        140        150        160        170        180 
RHTYEIPLVL VGNKIDLEQF RQVSTEEGMN LARDYNCAFF ETSAALRFGI DDAFQGLVRE 

       190        200        210 
IRRKESMLSL VERKLKRKDS LWKKIKASLK KKRENML 

« Hide

References

« Hide 'large scale' references
[1]"Rin, a neuron-specific and calmodulin-binding small G-protein, and Rit define a novel subfamily of ras proteins."
Lee C.H.J., Della N.G., Chew C.E., Zack D.J.
J. Neurosci. 16:6784-6794(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Tissue: Retina.
[2]"Biochemical characterization of the Ras-related GTPases Rit and Rin."
Shao H., Kadono-Okuda K., Finlin B.S., Andres D.A.
Arch. Biochem. Biophys. 371:207-219(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INTERACTION WITH MLLT4; RP RALGDS AND RLF, MUTAGENESIS OF SER-34; THR-52 AND GLN-78.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Blood vessel, Brain cortex, Corpora quadrigemina, Corpus striatum, Hypothalamus and Spinal cord.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Retina.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U71202 mRNA. Translation: AAB42212.1.
AF084463 mRNA. Translation: AAD13022.1.
AK040743 mRNA. Translation: BAC30690.1.
AK046425 mRNA. Translation: BAC32724.1.
AK046484 mRNA. Translation: BAC32750.1.
AK138206 mRNA. Translation: BAE23581.1. Different initiation.
AK139394 mRNA. Translation: BAE23992.1.
AK140133 mRNA. Translation: BAE24250.1.
AK140726 mRNA. Translation: BAE24457.1.
AK162862 mRNA. Translation: BAE37088.1.
AK162953 mRNA. Translation: BAE37131.1.
BC018267 mRNA. Translation: AAH18267.1.
CCDSCCDS29108.1.
RefSeqNP_033091.1. NM_009065.2.
UniGeneMm.5163.

3D structure databases

ProteinModelPortalP70425.
SMRP70425. Positions 33-183.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202893. 1 interaction.
IntActP70425. 3 interactions.

Proteomic databases

PaxDbP70425.
PRIDEP70425.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000153060; ENSMUSP00000114323; ENSMUSG00000057455.
GeneID19762.
KEGGmmu:19762.
UCSCuc008ehx.1. mouse.

Organism-specific databases

CTD6014.
MGIMGI:108054. Rit2.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00750000117416.
HOVERGENHBG009351.
InParanoidP70425.
KOK07833.
OMAVYKIVIL.
PhylomeDBP70425.
TreeFamTF315072.

Gene expression databases

ArrayExpressP70425.
BgeeP70425.
CleanExMM_RIT2.
GenevestigatorP70425.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERPTHR24070. PTHR24070. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRIT2. mouse.
NextBio297208.
PROP70425.
SOURCESearch...

Entry information

Entry nameRIT2_MOUSE
AccessionPrimary (citable) accession number: P70425
Secondary accession number(s): Q3UST1 expand/collapse secondary AC list , Q3UUP4, Q8BQT5, Q9QWX5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot