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 16-OCT-2019, entry version 165. DE RecName: Full=Ras-related protein Rap-2c; DE Flags: Precursor; GN Name=RAP2C; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Yu L.; RT "Cloning and characterization of the human gene RAP2C, a novel member RT of 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA 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., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA 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., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA 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., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA 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., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT member of 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., RA Buerckstuemmer T., 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., RA Ayoub D., 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- CC bound inactive and a GTP-bound active form. May play a role in CC cytoskeletal rearrangements and regulate cell spreading through CC activation of the effector TNIK. May play a role in SRE-mediated CC gene transcription. {ECO:0000269|PubMed:17447155}. CC -!- INTERACTION: CC P52306-5:RAP1GDS1; NbExp=4; IntAct=EBI-2856617, EBI-12832744; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17447155}. CC Recycling endosome membrane {ECO:0000250}; Lipid-anchor CC {ECO:0000250}; 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 CC brain, kidney, pancreas, and bone marrow. Expressed in mononuclear CC leukocytes and megakaryocytes. {ECO:0000269|PubMed:16213650, CC ECO:0000269|PubMed:17447155}. CC -!- PTM: Palmitoylated. Palmitoylation is required for association CC with 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q9Y3L5; -. DR BioGrid; 121785; 23. DR IntAct; Q9Y3L5; 17. DR STRING; 9606.ENSP00000340274; -. DR iPTMnet; 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; Q9Y3L5; -. DR PeptideAtlas; Q9Y3L5; -. DR PRIDE; Q9Y3L5; -. DR ProteomicsDB; 86043; -. DR DNASU; 57826; -. DR Ensembl; ENST00000342983; ENSP00000340274; ENSG00000123728. DR Ensembl; ENST00000370874; ENSP00000359911; ENSG00000123728. DR GeneID; 57826; -. DR KEGG; hsa:57826; -. DR UCSC; uc004ewp.5; human. DR CTD; 57826; -. DR GeneCards; RAP2C; -. DR HGNC; HGNC:21165; RAP2C. DR neXtProt; NX_Q9Y3L5; -. DR OpenTargets; ENSG00000123728; -. DR PharmGKB; PA134899238; -. DR eggNOG; KOG0395; Eukaryota. DR eggNOG; COG1100; LUCA. DR GeneTree; ENSGT00940000157245; -. DR HOGENOM; HOG000233973; -. DR InParanoid; Q9Y3L5; -. DR KO; K07839; -. DR OMA; QQIYRIK; -. DR OrthoDB; 1353024at2759; -. DR PhylomeDB; Q9Y3L5; -. DR TreeFam; TF313014; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR ChiTaRS; RAP2C; human. DR GenomeRNAi; 57826; -. DR Pharos; Q9Y3L5; -. DR PRO; PR:Q9Y3L5; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; ENSG00000123728; Expressed in 227 organ(s), highest expression level in body of uterus. 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: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:0043312; P:neutrophil degranulation; TAS:Reactome. 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 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 SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51421; RAS; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Endosome; GTP-binding; Lipoprotein; KW Membrane; Methylation; Nucleotide-binding; Palmitate; Prenylation; KW Reference proteome. FT CHAIN 1 180 Ras-related protein Rap-2c. FT /FTId=PRO_0000030221. FT PROPEP 181 183 Removed in mature form. FT {ECO:0000250|UniProtKB:Q8BU31}. FT /FTId=PRO_0000030222. FT NP_BIND 10 17 GTP. {ECO:0000250}. FT NP_BIND 57 61 GTP. {ECO:0000250}. FT NP_BIND 116 119 GTP. {ECO:0000250}. FT MOTIF 32 40 Effector region. {ECO:0000305}. FT MOD_RES 180 180 Cysteine methyl ester. FT {ECO:0000250|UniProtKB:Q8BU31}. FT LIPID 176 176 S-palmitoyl cysteine. FT {ECO:0000250|UniProtKB:Q8BU31}. FT LIPID 177 177 S-palmitoyl cysteine. FT {ECO:0000250|UniProtKB:Q8BU31}. FT LIPID 180 180 S-geranylgeranyl cysteine. FT {ECO:0000250|UniProtKB:Q8BU31}. FT CONFLICT 135 135 A -> V (in Ref. 6; AAH03403). FT {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 //