P70425 (RIT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	217 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds and exchanges GTP and GDP.
Enzyme regulation	Alternate 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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Nucleus
Ligand	Calmodulin-binding GTP-binding Nucleotide-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RLF	Q13129	2	EBI-2649620,EBI-958266	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 217	217	GTP-binding protein Rit2		PRO_0000082728
Regions
	Nucleotide binding	27 – 34	8	GTP By similarity
	Nucleotide binding	74 – 78	5	GTP By similarity
	Nucleotide binding	133 – 136	4	GTP By similarity
Experimental info
	Mutagenesis	34	1	S → N: Dominant negative. Loss of interaction with MLLT4, RLF and RALGDS. Ref.2
	Mutagenesis	52	1	T → A: Loss of interaction with MLLT4, RLF and RALGDS; when associated with L-78. Ref.2
	Mutagenesis	78	1	Q → L: Constitutively active. Dramatic reduction of the rate of GTP hydrolysis. Ref.2
	Sequence conflict	3	1	V → A in AAD13022. Ref.2
	Sequence conflict	150	1	N → T in AAD13022. Ref.2
	Sequence conflict	176	1	G → S in BAC32750. Ref.3
	Sequence conflict	217	1	L → I in AAD13022. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P70425 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 189AA6DCCE75034F	FASTA	217	24,802
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00109248.
RefSeq	NP_033091.1. NM_009065.2.
UniGene	Mm.5163.
3D structure databases
ProteinModelPortal	P70425.
SMR	P70425. Positions 33-183.
ModBase	Search...
Protein-protein interaction databases
IntAct	P70425. 3 interactions.
Proteomic databases
PaxDb	P70425.
PRIDE	P70425.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000153060; ENSMUSP00000114323; ENSMUSG00000057455.
GeneID	19762.
KEGG	mmu:19762.
UCSC	uc008ehx.1. mouse.
Organism-specific databases
CTD	6014.
MGI	MGI:108054. Rit2.
Phylogenomic databases
eggNOG	COG1100.
GeneTree	ENSGT00700000104060.
HOVERGEN	HBG009351.
InParanoid	P70425.
KO	K07833.
OMA	VYKIVIL.
OrthoDB	EOG4VDQ0C.
Gene expression databases
ArrayExpress	P70425.
Bgee	P70425.
CleanEx	MM_RIT2.
Genevestigator	P70425.
GermOnline	ENSMUSG00000057455. Mus musculus.
Family and domain databases
InterPro	IPR027417. P-loop_NTPase. IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR020849. Small_GTPase_Ras. [Graphical view]
PANTHER	PTHR24070. PTHR24070. 1 hit.
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00173. RAS. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51421. RAS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RIT2. mouse.
NextBio	297208.
SOURCE	Search...

Entry information

Entry name

RIT2_MOUSE

Accession

Primary (citable) accession number: P70425
Secondary accession number(s): Q3UST1 , Q3UUP4, Q8BQT5, Q9QWX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	February 1, 1997
Last modified:	May 29, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program