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RIT1_MOUSE
ID   RIT1_MOUSE              Reviewed;         219 AA.
AC   P70426;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=GTP-binding protein Rit1;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:Q92963};
DE   AltName: Full=Ras-like protein expressed in many tissues;
DE   AltName: Full=Ras-like without CAAX protein 1;
GN   Name=Rit1; Synonyms=Rit;
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].
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
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   [4]
RP   INTERACTION WITH RGL3.
RX   PubMed=10869344; DOI=10.1074/jbc.m002241200;
RA   Shao H., Andres D.A.;
RT   "A novel RalGEF-like protein, RGL3, as a candidate effector for rit and
RT   Ras.";
RL   J. Biol. Chem. 275:26914-26924(2000).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
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).
CC   -!- FUNCTION: Plays a crucial role in coupling NGF stimulation to the
CC       activation of both EPHB2 and MAPK14 signaling pathways and in NGF-
CC       dependent neuronal differentiation. Involved in ELK1 transactivation
CC       through the Ras-MAPK signaling cascade that mediates a wide variety of
CC       cellular functions, including cell proliferation, survival, and
CC       differentiation (By similarity). {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:Q92963};
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. Strongly interacts with BRAF, but only weakly with RAF1.
CC       BARF and RAF1 association is dependent upon the GTP-bound state (By
CC       similarity). Interacts with RGL3. {ECO:0000250,
CC       ECO:0000269|PubMed:10869344}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane.
CC   -!- TISSUE SPECIFICITY: Expressed in many tissues.
CC   -!- MISCELLANEOUS: Stimulation of the NGF and EGF receptor signaling
CC       pathways results in rapid and prolonged activation. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Shows rapid uncatalyzed guanine nucleotide dissociation
CC       rates, which are very much 10-fold faster than those of most Ras
CC       subfamily members. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; U71205; AAB42215.1; -; mRNA.
DR   EMBL; AK005357; BAB23972.1; -; mRNA.
DR   EMBL; AK014126; BAB29168.1; -; mRNA.
DR   EMBL; BC012694; AAH12694.1; -; mRNA.
DR   CCDS; CCDS17484.1; -.
DR   RefSeq; NP_033095.1; NM_009069.4.
DR   RefSeq; XP_006501223.1; XM_006501160.3.
DR   AlphaFoldDB; P70426; -.
DR   SMR; P70426; -.
DR   BioGRID; 202897; 2.
DR   IntAct; P70426; 1.
DR   STRING; 10090.ENSMUSP00000029692; -.
DR   iPTMnet; P70426; -.
DR   PhosphoSitePlus; P70426; -.
DR   EPD; P70426; -.
DR   MaxQB; P70426; -.
DR   PaxDb; P70426; -.
DR   PeptideAtlas; P70426; -.
DR   PRIDE; P70426; -.
DR   ProteomicsDB; 255154; -.
DR   Antibodypedia; 20423; 251 antibodies from 30 providers.
DR   DNASU; 19769; -.
DR   Ensembl; ENSMUST00000029692; ENSMUSP00000029692; ENSMUSG00000028057.
DR   GeneID; 19769; -.
DR   KEGG; mmu:19769; -.
DR   UCSC; uc008pwh.2; mouse.
DR   CTD; 6016; -.
DR   MGI; MGI:108053; Rit1.
DR   VEuPathDB; HostDB:ENSMUSG00000028057; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000160132; -.
DR   InParanoid; P70426; -.
DR   OMA; AQSREYK; -.
DR   OrthoDB; 1259506at2759; -.
DR   PhylomeDB; P70426; -.
DR   TreeFam; TF315072; -.
DR   BioGRID-ORCS; 19769; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Rit1; mouse.
DR   PRO; PR:P70426; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P70426; protein.
DR   Bgee; ENSMUSG00000028057; Expressed in granulocyte and 269 other tissues.
DR   ExpressionAtlas; P70426; baseline and differential.
DR   Genevisible; P70426; MM.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
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:MGI.
DR   GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR   GO; GO:0007265; P:Ras protein signal transduction; 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   Cell membrane; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..219
FT                   /note="GTP-binding protein Rit1"
FT                   /id="PRO_0000082726"
FT   BINDING         28..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         75..79
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         134..137
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   219 AA;  25169 MW;  3041ED75190C65AC CRC64;
     MESGARPIGS SCSSPAALSR EYKLVMLGAG GVGKSAMTMQ FISHRFPEDH DPTIEDAYKI
     RIRIDDEPAN LDILDTAGQA EFTAMRDQYM RAGEGFIICY SITDRRSFHE VREFKQLIYR
     VRRTDDTPVV LVGNKSDLKQ LRQVSKEEGL SLAREFSCPF FETSAAYRYY IDDVFHALVR
     EIRKKEKELV LAMEKKAKPK NSVWKRLKSP FRRKKDSVT
 
 
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