RIT2_MOUSE
ID RIT2_MOUSE Reviewed; 217 AA.
AC P70425; Q3UST1; Q3UUP4; Q8BQT5; Q9QWX5;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=GTP-binding protein Rit2;
DE EC=3.6.5.2 {ECO:0000269|PubMed:10545207};
DE AltName: Full=Ras-like protein expressed in neurons;
DE AltName: Full=Ras-like without CAAX protein 2;
GN Name=Rit2; Synonyms=Rin, Roc2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=8824319; DOI=10.1523/jneurosci.16-21-06784.1996;
RA Lee C.H.J., Della N.G., Chew C.E., Zack D.J.;
RT "Rin, a neuron-specific and calmodulin-binding small G-protein, and Rit
RT define a novel subfamily of ras proteins.";
RL J. Neurosci. 16:6784-6794(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, INTERACTION WITH AFDN;
RP RALGDS AND RLF, AND MUTAGENESIS OF SER-34; THR-52 AND GLN-78.
RX PubMed=10545207; DOI=10.1006/abbi.1999.1448;
RA Shao H., Kadono-Okuda K., Finlin B.S., Andres D.A.;
RT "Biochemical characterization of the Ras-related GTPases Rit and Rin.";
RL Arch. Biochem. Biophys. 371:207-219(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Blood vessel, Brain cortex, Corpora quadrigemina, Corpus striatum,
RC Hypothalamus, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH POU4F1, AND MUTAGENESIS OF GLN-78.
RX PubMed=12934100; DOI=10.1038/sj.onc.1206635;
RA Calissano M., Latchman D.S.;
RT "Functional interaction between the small GTP-binding protein Rin and the
RT N-terminal of Brn-3a transcription factor.";
RL Oncogene 22:5408-5414(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=23805044;
RA Zhang L., Wahlin K., Li Y., Masuda T., Yang Z., Zack D.J., Esumi N.;
RT "RIT2, a neuron-specific small guanosine triphosphatase, is expressed in
RT retinal neuronal cells and its promoter is modulated by the POU4
RT transcription factors.";
RL Mol. Vis. 19:1371-1386(2013).
CC -!- FUNCTION: Binds and exchanges GTP and GDP. Binds and modulates the
CC activation of POU4F1 as gene expression regulator.
CC {ECO:0000269|PubMed:12934100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000269|PubMed:10545207};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP.
CC -!- SUBUNIT: Interacts with PLXNB3 (By similarity). Interacts with AFDN,
CC the C-terminal domain of RALGDS and RLF, but not with RIN1 and PIK3CA.
CC RLF binds exclusively to the active GTP-bound form. Binds calmodulin.
CC Interacts with POU4F1 (via N-terminus); the interaction controls POU4F1
CC transactivation activity on some neuronal target genes
CC (PubMed:12934100). {ECO:0000250|UniProtKB:Q99578,
CC ECO:0000269|PubMed:10545207, ECO:0000269|PubMed:12934100}.
CC -!- INTERACTION:
CC P70425; Q13129: RLF; Xeno; NbExp=2; IntAct=EBI-2649620, EBI-958266;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23805044}. Cell
CC membrane {ECO:0000269|PubMed:23805044}. Note=Colocalizes with PLXNB3 at
CC the plasma membrane. {ECO:0000250|UniProtKB:Q99578}.
CC -!- TISSUE SPECIFICITY: Expressed in ganglion cell layer (GCL), inner
CC plexiform layer (IPL) and inner nuclear layer (INL) of the retina.
CC Expressed in retinal ganglion cells (RGCs). Expressed in horizontal,
CC bipolar and amacrine cells, but not Mueller glia, of the INL (at
CC protein level). Neuron-specific (PubMed:8824319). Expressed in ganglion
CC cell layer (GCL) and inner plexiform layer (IPL) (PubMed:23805044).
CC {ECO:0000269|PubMed:23805044, ECO:0000269|PubMed:8824319}.
CC -!- DEVELOPMENTAL STAGE: Expressed weakly in ganglion cell layer (GCL) and
CC inner neuroblastic layer (NBL) of the embryonic retina at 15.5 dpc.
CC Expression increases progressively in the retina from new borns at
CC postnatal day 2 (P2), P5, P15 to 8 week-old adult (at protein level).
CC {ECO:0000269|PubMed:23805044}.
CC -!- MISCELLANEOUS: Shows rapid uncatalyzed guanine nucleotide dissociation
CC rates, which are much faster than those of most Ras subfamily members.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE23581.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U71202; AAB42212.1; -; mRNA.
DR EMBL; AF084463; AAD13022.1; -; mRNA.
DR EMBL; AK040743; BAC30690.1; -; mRNA.
DR EMBL; AK046425; BAC32724.1; -; mRNA.
DR EMBL; AK046484; BAC32750.1; -; mRNA.
DR EMBL; AK138206; BAE23581.1; ALT_INIT; mRNA.
DR EMBL; AK139394; BAE23992.1; -; mRNA.
DR EMBL; AK140133; BAE24250.1; -; mRNA.
DR EMBL; AK140726; BAE24457.1; -; mRNA.
DR EMBL; AK162862; BAE37088.1; -; mRNA.
DR EMBL; AK162953; BAE37131.1; -; mRNA.
DR EMBL; BC018267; AAH18267.1; -; mRNA.
DR CCDS; CCDS29108.1; -.
DR RefSeq; NP_033091.1; NM_009065.2.
DR AlphaFoldDB; P70425; -.
DR SMR; P70425; -.
DR BioGRID; 202893; 1.
DR IntAct; P70425; 4.
DR MINT; P70425; -.
DR STRING; 10090.ENSMUSP00000114323; -.
DR PhosphoSitePlus; P70425; -.
DR SwissPalm; P70425; -.
DR MaxQB; P70425; -.
DR PaxDb; P70425; -.
DR PRIDE; P70425; -.
DR ProteomicsDB; 254888; -.
DR Antibodypedia; 8862; 287 antibodies from 29 providers.
DR DNASU; 19762; -.
DR Ensembl; ENSMUST00000153060; ENSMUSP00000114323; ENSMUSG00000057455.
DR GeneID; 19762; -.
DR KEGG; mmu:19762; -.
DR UCSC; uc008ehx.1; mouse.
DR CTD; 6014; -.
DR MGI; MGI:108054; Rit2.
DR VEuPathDB; HostDB:ENSMUSG00000057455; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000161402; -.
DR HOGENOM; CLU_041217_9_5_1; -.
DR InParanoid; P70425; -.
DR OMA; QFVSHRF; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; P70425; -.
DR TreeFam; TF315072; -.
DR BioGRID-ORCS; 19762; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Rit2; mouse.
DR PRO; PR:P70425; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P70425; protein.
DR Bgee; ENSMUSG00000057455; Expressed in ventral tegmental area and 117 other tissues.
DR ExpressionAtlas; P70425; baseline and differential.
DR Genevisible; P70425; MM.
DR GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0097447; C:dendritic tree; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005516; F:calmodulin binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003682; F:chromatin binding; IGI:ParkinsonsUK-UCL.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003924; F:GTPase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030215; F:semaphorin receptor binding; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0032507; P:maintenance of protein location in cell; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IGI:ParkinsonsUK-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:ParkinsonsUK-UCL.
DR GO; GO:0007265; P:Ras protein signal transduction; IDA:ARUK-UCL.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISO:MGI.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Cell membrane; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..217
FT /note="GTP-binding protein Rit2"
FT /id="PRO_0000082728"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 74..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MUTAGEN 34
FT /note="S->N: Dominant negative. Loss of interaction with
FT AFDN, RLF and RALGDS."
FT /evidence="ECO:0000269|PubMed:10545207"
FT MUTAGEN 52
FT /note="T->A: Loss of interaction with AFDN, RLF and RALGDS;
FT when associated with L-78."
FT /evidence="ECO:0000269|PubMed:10545207"
FT MUTAGEN 78
FT /note="Q->L: Constitutively active. Dramatic reduction of
FT the rate of GTP hydrolysis."
FT /evidence="ECO:0000269|PubMed:10545207"
FT CONFLICT 3
FT /note="V -> A (in Ref. 2; AAD13022)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="N -> T (in Ref. 2; AAD13022)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="G -> S (in Ref. 3; BAC32750)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="L -> I (in Ref. 2; AAD13022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 24802 MW; 189AA6DCCE75034F CRC64;
MEVENEAHCC PGSSSGGSRE YKVVMLGAGG VGKSAVTMQF ISHQFPDYHD PTIEDAYKTQ
VRIDNEPAYL DILDTAGQAE FTAMREQYMR GGEGFIICYS VTDRQSFQEA AKFKELIFQV
RHTYEIPLVL VGNKIDLEQF RQVSTEEGMN LARDYNCAFF ETSAALRFGI DDAFQGLVRE
IRRKESMLSL VERKLKRKDS LWKKIKASLK KKRENML
