ID RAP2C_HUMAN Reviewed; 183 AA.
AC Q9Y3L5; B3KWD6; Q5H9H9; Q9BTS0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 187.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=17447155; DOI=10.1007/s11033-006-9023-9;
RA Guo Z., Yuan J., Tang W., Chen X., Gu X., Luo K., Wang Y., Wan B., Yu L.;
RT "Cloning and characterization of the human gene RAP2C, a novel member of
RT Ras family, which activates transcriptional activities of SRE.";
RL Mol. Biol. Rep. 34:137-144(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Rhodes S., Huckle E.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [7]
RP GTP-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=16213650; DOI=10.1016/j.biochi.2005.08.007;
RA Paganini S., Guidetti G.F., Catricala S., Trionfini P., Panelli S.,
RA Balduini C., Torti M.;
RT "Identification and biochemical characterization of Rap2C, a new member of
RT the Rap family of small GTP-binding proteins.";
RL Biochimie 88:285-295(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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:17447155}.
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 -!- INTERACTION:
CC Q9Y3L5; P52306-5: RAP1GDS1; NbExp=3; IntAct=EBI-2856617, EBI-12832744;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17447155}.
CC Recycling endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, skeletal muscle, prostate,
CC uterus, rectum, stomach, and bladder and to a lower extent in brain,
CC kidney, pancreas, and bone marrow. Expressed in mononuclear leukocytes
CC and megakaryocytes. {ECO:0000269|PubMed:16213650,
CC ECO:0000269|PubMed:17447155}.
CC -!- PTM: Palmitoylated. Palmitoylation is required for association with
CC recycling endosome membranes and activation of TNIK.
CC {ECO:0000250|UniProtKB:Q8BU31}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; AY298955; AAP55684.1; -; mRNA.
DR EMBL; AL049685; CAB41256.1; -; mRNA.
DR EMBL; AK124801; BAG54098.1; -; mRNA.
DR EMBL; Z78022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471107; EAX11782.1; -; Genomic_DNA.
DR EMBL; BC003403; AAH03403.1; -; mRNA.
DR CCDS; CCDS14632.1; -.
DR RefSeq; NP_001258115.1; NM_001271186.1.
DR RefSeq; NP_001258116.1; NM_001271187.1.
DR RefSeq; NP_067006.3; NM_021183.4.
DR RefSeq; XP_011529678.1; XM_011531376.1.
DR AlphaFoldDB; Q9Y3L5; -.
DR SMR; Q9Y3L5; -.
DR BioGRID; 121785; 49.
DR IntAct; Q9Y3L5; 23.
DR MINT; Q9Y3L5; -.
DR STRING; 9606.ENSP00000359911; -.
DR iPTMnet; Q9Y3L5; -.
DR MetOSite; Q9Y3L5; -.
DR PhosphoSitePlus; Q9Y3L5; -.
DR SwissPalm; Q9Y3L5; -.
DR BioMuta; RAP2C; -.
DR DMDM; 47117343; -.
DR EPD; Q9Y3L5; -.
DR jPOST; Q9Y3L5; -.
DR MassIVE; Q9Y3L5; -.
DR MaxQB; Q9Y3L5; -.
DR PaxDb; 9606-ENSP00000340274; -.
DR PeptideAtlas; Q9Y3L5; -.
DR ProteomicsDB; 86043; -.
DR Pumba; Q9Y3L5; -.
DR Antibodypedia; 56035; 141 antibodies from 24 providers.
DR DNASU; 57826; -.
DR Ensembl; ENST00000342983.6; ENSP00000340274.2; ENSG00000123728.10.
DR Ensembl; ENST00000370874.2; ENSP00000359911.1; ENSG00000123728.10.
DR GeneID; 57826; -.
DR KEGG; hsa:57826; -.
DR MANE-Select; ENST00000370874.2; ENSP00000359911.1; NM_001271186.2; NP_001258115.1.
DR UCSC; uc004ewp.5; human.
DR AGR; HGNC:21165; -.
DR CTD; 57826; -.
DR DisGeNET; 57826; -.
DR GeneCards; RAP2C; -.
DR HGNC; HGNC:21165; RAP2C.
DR HPA; ENSG00000123728; Tissue enhanced (endometrium).
DR neXtProt; NX_Q9Y3L5; -.
DR OpenTargets; ENSG00000123728; -.
DR PharmGKB; PA134899238; -.
DR VEuPathDB; HostDB:ENSG00000123728; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000157245; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q9Y3L5; -.
DR OMA; NCDFVET; -.
DR OrthoDB; 8685at2759; -.
DR PhylomeDB; Q9Y3L5; -.
DR TreeFam; TF313014; -.
DR PathwayCommons; Q9Y3L5; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9Y3L5; -.
DR BioGRID-ORCS; 57826; 17 hits in 784 CRISPR screens.
DR ChiTaRS; RAP2C; human.
DR GenomeRNAi; 57826; -.
DR Pharos; Q9Y3L5; Tbio.
DR PRO; PR:Q9Y3L5; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9Y3L5; Protein.
DR Bgee; ENSG00000123728; Expressed in endothelial cell and 209 other cell types or tissues.
DR ExpressionAtlas; Q9Y3L5; baseline and differential.
DR Genevisible; Q9Y3L5; HS.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR GO; GO:0061097; P:regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR CDD; cd04176; Rap2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR24070; RAS, DI-RAS, AND RHEB FAMILY MEMBERS OF SMALL GTPASE SUPERFAMILY; 1.
DR PANTHER; PTHR24070:SF200; RAS-RELATED PROTEIN RAP-2C; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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_0000030221"
FT PROPEP 181..183
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q8BU31"
FT /id="PRO_0000030222"
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:0000250|UniProtKB:Q8BU31"
FT LIPID 176
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8BU31"
FT LIPID 177
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8BU31"
FT LIPID 180
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8BU31"
FT CONFLICT 135
FT /note="A -> V (in Ref. 6; AAH03403)"
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
//
