RAP2C_MOUSE
ID RAP2C_MOUSE Reviewed; 183 AA.
AC Q8BU31; Q504Q0; Q6P1Y7; Q810J4; Q8R2P4;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Ras-related protein Rap-2c;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P10114};
DE Flags: Precursor;
GN Name=Rap2c;
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, and NOD;
RC TISSUE=Embryonic heart, Embryonic liver, and Thymus;
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=Embryo, Eye, Limb, 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 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Liver, Lung, Pancreas, 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. May play a role in cytoskeletal
CC rearrangements and regulate cell spreading through activation of the
CC effector TNIK. May play a role in SRE-mediated gene transcription.
CC {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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Recycling endosome
CC membrane {ECO:0000269|PubMed:19061864}; Lipid-anchor
CC {ECO:0000269|PubMed:19061864}; Cytoplasmic side
CC {ECO:0000269|PubMed:19061864}.
CC -!- PTM: Palmitoylated. Palmitoylation is required for association with
CC recycling endosome membranes and activation of TNIK.
CC {ECO:0000269|PubMed:19061864}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; AK087971; BAC40066.1; -; mRNA.
DR EMBL; AK146057; BAE26866.1; -; mRNA.
DR EMBL; AK146956; BAE27564.1; -; mRNA.
DR EMBL; AK147015; BAE27609.1; -; mRNA.
DR EMBL; BC027363; AAH27363.3; -; mRNA.
DR EMBL; BC050056; AAH50056.2; -; mRNA.
DR EMBL; BC064814; AAH64814.2; -; mRNA.
DR EMBL; BC094890; AAH94890.1; -; mRNA.
DR CCDS; CCDS30121.1; -.
DR RefSeq; NP_766001.1; NM_172413.2.
DR RefSeq; XP_006541608.1; XM_006541545.2.
DR RefSeq; XP_006541609.1; XM_006541546.2.
DR AlphaFoldDB; Q8BU31; -.
DR SMR; Q8BU31; -.
DR BioGRID; 215127; 2.
DR STRING; 10090.ENSMUSP00000058391; -.
DR iPTMnet; Q8BU31; -.
DR PhosphoSitePlus; Q8BU31; -.
DR SwissPalm; Q8BU31; -.
DR EPD; Q8BU31; -.
DR jPOST; Q8BU31; -.
DR MaxQB; Q8BU31; -.
DR PaxDb; Q8BU31; -.
DR PeptideAtlas; Q8BU31; -.
DR PRIDE; Q8BU31; -.
DR ProteomicsDB; 254984; -.
DR Antibodypedia; 56035; 127 antibodies from 24 providers.
DR DNASU; 72065; -.
DR Ensembl; ENSMUST00000053593; ENSMUSP00000058391; ENSMUSG00000050029.
DR GeneID; 72065; -.
DR KEGG; mmu:72065; -.
DR UCSC; uc009tds.1; mouse.
DR CTD; 57826; -.
DR MGI; MGI:1919315; Rap2c.
DR VEuPathDB; HostDB:ENSMUSG00000050029; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000157245; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q8BU31; -.
DR OMA; QFTGINE; -.
DR OrthoDB; 1353024at2759; -.
DR PhylomeDB; Q8BU31; -.
DR TreeFam; TF313014; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 72065; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Rap2c; mouse.
DR PRO; PR:Q8BU31; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BU31; protein.
DR Bgee; ENSMUSG00000050029; Expressed in embryonic post-anal tail and 251 other tissues.
DR Genevisible; Q8BU31; 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:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA: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:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA: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 Cytoplasm; Endosome; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Palmitate; Prenylation;
KW Reference proteome.
FT CHAIN 1..180
FT /note="Ras-related protein Rap-2c"
FT /id="PRO_0000030223"
FT PROPEP 181..183
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:19061864"
FT /id="PRO_0000030224"
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: Loss of association with the recycling
FT endosome membranes and loss of TNIK activation; when
FT associated with C-177."
FT /evidence="ECO:0000269|PubMed:19061864"
FT MUTAGEN 177
FT /note="C->G: Loss of association with the recycling
FT endosome membranes and loss of TNIK activation; when
FT associated with C-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"
FT CONFLICT 83
FT /note="S -> N (in Ref. 2; AAH27363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 183 AA; 20745 MW; 6763385F76638324 CRC64;
MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI VRVKRYEKVP LILVGNKVDL
EPEREVMSSE GRALAQEWGC PFMETSAKSK SMVDELFAEI VRQMNYSSLP EKQDQCCTTC
VVQ
