RAP2B_MOUSE
ID RAP2B_MOUSE Reviewed; 183 AA.
AC P61226; P17964; Q96EG5; Q9CXG0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ras-related protein Rap-2b;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P10114};
DE Flags: Precursor;
GN Name=Rap2b;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Cerebellum, and Mammary gland;
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 [3]
RP PROTEIN SEQUENCE OF 6-16; 43-68 AND 151-162, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP INTERACTION WITH RUNDC3A, AND DOMAIN.
RX PubMed=9523700; DOI=10.1046/j.1432-1327.1998.2520290.x;
RA Janoueix-Lerosey I., Pasheva E., de Tand M.-F., Tavitian A.,
RA de Gunzburg J.;
RT "Identification of a specific effector of the small GTP-binding protein
RT Rap2.";
RL Eur. J. Biochem. 252:290-298(1998).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-180, METHYLATION AT
RP CYS-180, PALMITOYLATION AT CYS-176 AND CYS-177, AND MUTAGENESIS OF CYS-176;
RP CYS-177 AND CYS-180.
RX PubMed=19061864; DOI=10.1016/j.bbrc.2008.11.107;
RA Uechi Y., Bayarjargal M., Umikawa M., Oshiro M., Takei K., Yamashiro Y.,
RA Asato T., Endo S., Misaki R., Taguchi T., Kariya K.;
RT "Rap2 function requires palmitoylation and recycling endosome
RT localization.";
RL Biochem. Biophys. Res. Commun. 378:732-737(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC Testis;
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: Small GTP-binding protein which cycles between a GDP-bound
CC inactive and a GTP-bound active form. Involved in EGFR and CHRM3
CC signaling pathways through stimulation of PLCE1. May play a role in
CC cytoskeletal rearrangements and regulate cell spreading through
CC activation of the effector TNIK. May regulate membrane vesiculation in
CC red blood cells. {ECO:0000269|PubMed:19061864}.
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:P10114};
CC -!- SUBUNIT: Interacts with PLCE1. Interacts with SGSM1, SGSM2 and SGSM3
CC (By similarity). The GTP-bound form of RAP2B interacts with RUNDC3A.
CC {ECO:0000250, ECO:0000269|PubMed:9523700}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000269|PubMed:19061864}; Lipid-anchor
CC {ECO:0000269|PubMed:19061864}; Cytoplasmic side
CC {ECO:0000269|PubMed:19061864}. Note=Associated with red blood cells-
CC released vesicles. {ECO:0000250}.
CC -!- DOMAIN: The effector domain mediates the interaction with RUNDC3A.
CC {ECO:0000269|PubMed:9523700}.
CC -!- PTM: Palmitoylated. Unlike RAP2A and RAP2C, palmitoylation of RAP2B is
CC not required for association with recycling endosome membranes and
CC activation of TNIK. {ECO:0000269|PubMed:19061864}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; AK014462; BAB29368.1; -; mRNA.
DR EMBL; BC032168; AAH32168.1; -; mRNA.
DR EMBL; BC046528; AAH46528.1; -; mRNA.
DR CCDS; CCDS17378.1; -.
DR RefSeq; NP_082988.1; NM_028712.4.
DR AlphaFoldDB; P61226; -.
DR SMR; P61226; -.
DR BioGRID; 216422; 6.
DR IntAct; P61226; 2.
DR STRING; 10090.ENSMUSP00000038841; -.
DR iPTMnet; P61226; -.
DR PhosphoSitePlus; P61226; -.
DR SwissPalm; P61226; -.
DR EPD; P61226; -.
DR jPOST; P61226; -.
DR PaxDb; P61226; -.
DR PeptideAtlas; P61226; -.
DR PRIDE; P61226; -.
DR ProteomicsDB; 254983; -.
DR Antibodypedia; 33622; 273 antibodies from 28 providers.
DR DNASU; 74012; -.
DR Ensembl; ENSMUST00000049064; ENSMUSP00000038841; ENSMUSG00000036894.
DR GeneID; 74012; -.
DR KEGG; mmu:74012; -.
DR UCSC; uc008pjl.1; mouse.
DR CTD; 5912; -.
DR MGI; MGI:1921262; Rap2b.
DR VEuPathDB; HostDB:ENSMUSG00000036894; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000160283; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P61226; -.
DR OMA; IEDCFRT; -.
DR OrthoDB; 1353024at2759; -.
DR PhylomeDB; P61226; -.
DR TreeFam; TF313014; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 74012; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Rap2b; mouse.
DR PRO; PR:P61226; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P61226; protein.
DR Bgee; ENSMUSG00000036894; Expressed in aortic valve and 238 other tissues.
DR ExpressionAtlas; P61226; baseline and differential.
DR Genevisible; P61226; MM.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IDA:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:MGI.
DR GO; GO:0030168; P:platelet activation; ISO:MGI.
DR GO; GO:0070527; P:platelet aggregation; ISO:MGI.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:MGI.
DR GO; GO:0032486; P:Rap protein signal transduction; IDA:UniProtKB.
DR GO; GO:0061097; P:regulation of protein tyrosine kinase activity; IDA:UniProtKB.
DR CDD; cd04176; Rap2; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041840; Rap2.
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 Direct protein sequencing; Endosome; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Palmitate; Prenylation;
KW Reference proteome.
FT CHAIN 1..180
FT /note="Ras-related protein Rap-2b"
FT /id="PRO_0000030217"
FT PROPEP 181..183
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:19061864"
FT /id="PRO_0000030218"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 180
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305|PubMed:19061864"
FT LIPID 176
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:19061864"
FT LIPID 177
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:19061864"
FT LIPID 180
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:19061864"
FT MUTAGEN 176
FT /note="C->G: No reduction of association with the recycling
FT endosome membranes and does activate TNIK; when associated
FT with G-177."
FT /evidence="ECO:0000269|PubMed:19061864"
FT MUTAGEN 177
FT /note="C->G: No reduction of association with the recycling
FT endosome membranes and does activate TNIK; when associated
FT with G-176."
FT /evidence="ECO:0000269|PubMed:19061864"
FT MUTAGEN 180
FT /note="C->A: Loss of association with membranes."
FT /evidence="ECO:0000269|PubMed:19061864"
SQ SEQUENCE 183 AA; 20504 MW; A1139C2D5E7F5865 CRC64;
MREYKVVVLG SGGVGKSALT VQFVTGSFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYERVP MILVGNKVDL
EGEREVSYGE GKALAEEWSC PFMETSAKNK ASVDELFAEI VRQMNYAAQP NGDEGCCSAC
VIL
