RIT2_RAT
ID RIT2_RAT Reviewed; 217 AA.
AC Q5BJQ5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=GTP-binding protein Rit2;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P70425};
GN Name=Rit2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Binds and exchanges GTP and GDP. {ECO:0000250}.
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:0000250|UniProtKB:P70425};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AFDN, the C-terminal domain of RALGDS and RLF,
CC but not with RIN1 and PIK3CA. RLF binds exclusively to the active GTP-
CC bound form. Binds calmodulin. Interacts with PLXNB3 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q5BJQ5; Q01959: SLC6A3; Xeno; NbExp=2; IntAct=EBI-11686902, EBI-6661445;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P70425}. Cell
CC membrane {ECO:0000250|UniProtKB:P70425}. Note=Colocalizes with PLXNB3
CC at the plasma membrane. {ECO:0000250|UniProtKB:Q99578}.
CC -!- MISCELLANEOUS: Shows rapid uncatalyzed guanine nucleotide dissociation
CC rates, which are much faster than those of most Ras subfamily members.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; BC091382; AAH91382.1; -; mRNA.
DR RefSeq; NP_001013078.1; NM_001013060.1.
DR AlphaFoldDB; Q5BJQ5; -.
DR SMR; Q5BJQ5; -.
DR IntAct; Q5BJQ5; 2.
DR STRING; 10116.ENSRNOP00000023871; -.
DR PaxDb; Q5BJQ5; -.
DR PRIDE; Q5BJQ5; -.
DR Ensembl; ENSRNOT00000023874; ENSRNOP00000023871; ENSRNOG00000017568.
DR GeneID; 291713; -.
DR KEGG; rno:291713; -.
DR UCSC; RGD:1307654; rat.
DR CTD; 6014; -.
DR RGD; 1307654; Rit2.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000161402; -.
DR HOGENOM; CLU_041217_9_5_1; -.
DR InParanoid; Q5BJQ5; -.
DR OMA; QFVSHRF; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; Q5BJQ5; -.
DR TreeFam; TF315072; -.
DR PRO; PR:Q5BJQ5; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000017568; Expressed in cerebellum and 10 other tissues.
DR Genevisible; Q5BJQ5; RN.
DR GO; GO:0044297; C:cell body; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0097447; C:dendritic tree; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005516; F:calmodulin binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
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; ISS:ParkinsonsUK-UCL.
DR GO; GO:0003924; F:GTPase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030215; F:semaphorin receptor binding; ISO:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0032507; P:maintenance of protein location in cell; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISO:RGD.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:RGD.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IGI:ParkinsonsUK-UCL.
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_0000233261"
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"
SQ SEQUENCE 217 AA; 24761 MW; 4D12C7B0D3F46903 CRC64;
MEAENEAHCC PGSSSGGSRE YKVVMLGAGG VGKSAVTMQF ISHQFPDYHD PTIEDAYKTQ
VRIDNEPAYL DILDTAGQAE FTAMREQYMR GGEGFIICYS VTDRQSFQEA AKFKELIFQV
RHTYEIPLVL VGNKIDLEQF RQVSTEEGMT LARDYNCAFF ETSAALRFGI DDAFQGLVRE
IRRKESMLSL VERKLKRKDS LWKKIKASLK KKRENMI
