ID RAB5A_MOUSE Reviewed; 215 AA. AC Q9CQD1; Q9DCN5; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 02-MAR-2010, entry version 85. DE RecName: Full=Ras-related protein Rab-5A; GN Name=Rab5a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Embryonic stem cell, Head, and Small intestine; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP PROTEIN SEQUENCE OF 23-33; 82-110 AND 184-195, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP INTERACTION WITH SGSM1 AND SGSM3. RX PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013; RA Yang H., Sasaki T., Minoshima S., Shimizu N.; RT "Identification of three novel proteins (SGSM1, 2, 3) which modulate RT small G protein (RAP and RAB)-mediated signaling pathway."; RL Genomics 90:249-260(2007). CC -!- FUNCTION: Required for the fusion of plasma membranes and early CC endosomes. CC -!- ENZYME REGULATION: Regulated by guanine nucleotide exchange CC factors (GEFs) which promote the exchange of bound GDP for free CC GTP. CC -!- SUBUNIT: Binds EEA1. Interacts with ALS2CL, UNC84B, ZFYVE20 and CC RUFY1. Interacts with RIN1 and GAPVD1, which regulate its pathway, CC probably by acting as a GEF (By similarity). Interacts with SGSM1 CC and SGSM3. CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic CC side (By similarity). Early endosome membrane; Lipid-anchor (By CC similarity). Melanosome (By similarity). CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK002631; BAB22245.1; -; mRNA. DR EMBL; AK008198; BAB25527.1; -; mRNA. DR EMBL; AK010495; BAB26985.1; -; mRNA. DR EMBL; AK081999; BAC38391.1; -; mRNA. DR EMBL; BC004842; AAH04842.1; -; mRNA. DR EMBL; BC034370; AAH34370.1; -; mRNA. DR IPI; IPI00132410; -. DR RefSeq; NP_080163.1; -. DR UniGene; Mm.329123; -. DR SMR; Q9CQD1; 15-184. DR IntAct; Q9CQD1; 1. DR STRING; Q9CQD1; -. DR PhosphoSite; Q9CQD1; -. DR PRIDE; Q9CQD1; -. DR Ensembl; ENSMUST00000017975; ENSMUSP00000017975; ENSMUSG00000017831; Mus musculus. DR GeneID; 271457; -. DR KEGG; mmu:271457; -. DR UCSC; uc008czn.1; mouse. DR CTD; 271457; -. DR MGI; MGI:105926; Rab5a. DR HOGENOM; HBG745225; -. DR HOVERGEN; HBG009351; -. DR InParanoid; Q9CQD1; -. DR OMA; PTRNQCC; -. DR OrthoDB; EOG9M3CV3; -. DR PhylomeDB; Q9CQD1; -. DR NextBio; 393462; -. DR ArrayExpress; Q9CQD1; -. DR Bgee; Q9CQD1; -. DR CleanEx; MM_RAB5A; -. DR Genevestigator; Q9CQD1; -. DR GermOnline; ENSMUSG00000017831; Mus musculus. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030139; C:endocytic vesicle; IDA:MGI. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0045121; C:membrane raft; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0001726; C:ruffle; IDA:MGI. DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB. DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR InterPro; IPR003579; GTPase_Rab. DR InterPro; IPR015599; Rab5-like. DR InterPro; IPR013753; Ras. DR InterPro; IPR001806; Ras_GTPase. DR InterPro; IPR005225; Small_GTP_bd. DR InterPro; IPR020851; Small_GTPase. DR PANTHER; PTHR11708:SF254; Rab5_like; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51419; RAB; 1. PE 1: Evidence at protein level; KW Acetylation; Cell membrane; Direct protein sequencing; Endosome; KW GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; KW Phosphoprotein; Prenylation; Protein transport; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 215 Ras-related protein Rab-5A. FT /FTId=PRO_0000121106. FT NP_BIND 27 35 GTP (By similarity). FT NP_BIND 75 79 GTP (By similarity). FT NP_BIND 133 136 GTP (By similarity). FT NP_BIND 163 165 GTP (By similarity). FT MOTIF 49 57 Effector region (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 202 202 Phosphothreonine (By similarity). FT LIPID 212 212 S-geranylgeranyl cysteine (By FT similarity). FT LIPID 213 213 S-geranylgeranyl cysteine (By FT similarity). FT CONFLICT 119 119 Q -> R (in Ref. 1; BAB22245). SQ SEQUENCE 215 AA; 23599 MW; 9CDE2FD9B37C261A CRC64; MANRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE STIGAAFLTQ TVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNEESFAR AKNWVKELQR QASPNIVIAL SGNKADLANK RAVDFQEAQS YADDNSLLFM ETSAKTSMNV NEIFMAIAKK LPKNEPQNPG ANSARGRGVD LTEPAQPARS QCCSN //