RB11A_MOUSE
ID RB11A_MOUSE Reviewed; 216 AA.
AC P62492; P24410; Q3V1Z6; Q9JLX1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ras-related protein Rab-11A {ECO:0000303|PubMed:26506309};
DE Short=Rab-11 {ECO:0000303|PubMed:26506309};
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62491};
DE Flags: Precursor;
GN Name=Rab11a {ECO:0000312|MGI:MGI:1858202};
GN Synonyms=Rab11 {ECO:0000303|PubMed:10708602};
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 [GENOMIC DNA].
RX PubMed=10708602; DOI=10.1006/bbrc.2000.2334;
RA Bhartur S.G., Calhoun B.C., Woodrum J., Kurkjian J., Iyer S., Lai F.,
RA Goldenring J.R.;
RT "Genomic structure of murine rab11 family members.";
RL Biochem. Biophys. Res. Commun. 269:611-617(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [4]
RP PROTEIN SEQUENCE OF 14-24; 42-51 AND 83-95, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP INTERACTION WITH EXOC6.
RX PubMed=15292201; DOI=10.1074/jbc.m402264200;
RA Zhang X.-M., Ellis S., Sriratana A., Mitchell C.A., Rowe T.;
RT "Sec15 is an effector for the Rab11 GTPase in mammalian cells.";
RL J. Biol. Chem. 279:43027-43034(2004).
RN [6]
RP INTERACTION WITH SGSM1; SGSM2 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 small
RT G protein (RAP and RAB)-mediated signaling pathway.";
RL Genomics 90:249-260(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP INTERACTION WITH VIPAS39.
RX PubMed=20190753; DOI=10.1038/ng.538;
RA Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y.,
RA Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B.,
RA Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H., Matthews R.P.,
RA Thomas S.G., Rappoport J.Z., Arias I.M., Wolburg H., Knisely A.S.,
RA Kelly D.A., Muller F., Maher E.R., Gissen P.;
RT "Mutations in VIPAR cause an arthrogryposis, renal dysfunction and
RT cholestasis syndrome phenotype with defects in epithelial polarization.";
RL Nat. Genet. 42:303-312(2010).
RN [9]
RP FUNCTION IN MELANOSOME TRANSPORT.
RX PubMed=21291502; DOI=10.1111/j.1600-0854.2011.01172.x;
RA Beaumont K.A., Hamilton N.A., Moores M.T., Brown D.L., Ohbayashi N.,
RA Cairncross O., Cook A.L., Smith A.G., Misaki R., Fukuda M., Taguchi T.,
RA Sturm R.A., Stow J.L.;
RT "The recycling endosome protein Rab17 regulates melanocytic filopodia
RT formation and melanosome trafficking.";
RL Traffic 12:627-643(2011).
RN [10]
RP INTERACTION WITH SH3BP5.
RX PubMed=26506309; DOI=10.1016/j.devcel.2015.09.013;
RA Sakaguchi A., Sato M., Sato K., Gengyo-Ando K., Yorimitsu T., Nakai J.,
RA Hara T., Sato K., Sato K.;
RT "REI-1 is a guanine nucleotide exchange factor regulating RAB-11
RT localization and function in C. elegans embryos.";
RL Dev. Cell 35:211-221(2015).
RN [11]
RP INTERACTION WITH TBC1D12.
RX PubMed=28384198; DOI=10.1371/journal.pone.0174883;
RA Oguchi M.E., Noguchi K., Fukuda M.;
RT "TBC1D12 is a novel Rab11-binding protein that modulates neurite outgrowth
RT of PC12 cells.";
RL PLoS ONE 12:E0174883-E0174883(2017).
RN [12]
RP INTERACTION WITH RELCH, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A
RP COMPLEX WITH RECHL AND OSBP1.
RX PubMed=29514919; DOI=10.1083/jcb.201709123;
RA Sobajima T., Yoshimura S.I., Maeda T., Miyata H., Miyoshi E., Harada A.;
RT "The Rab11-binding protein RELCH/KIAA1468 controls intracellular
RT cholesterol distribution.";
RL J. Cell Biol. 217:1777-1796(2018).
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different set of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. The small Rab GTPase RAB11A
CC regulates endocytic recycling. Acts as a major regulator of membrane
CC delivery during cytokinesis. Together with MYO5B and RAB8A participates
CC in epithelial cell polarization. Together with RAB3IP, RAB8A, the
CC exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes
CC transcytosis of PODXL to the apical membrane initiation sites (AMIS),
CC apical surface formation and lumenogenesis. Together with MYO5B
CC participates in CFTR trafficking to the plasma membrane and TF
CC (Transferrin) recycling in nonpolarized cells. Required in a complex
CC with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma
CC membrane. Participates in the sorting and basolateral transport of CDH1
CC from the Golgi apparatus to the plasma membrane. Regulates the
CC recycling of FCGRT (receptor of Fc region of monomeric Ig G) to
CC basolateral membranes (By similarity). May also play a role in
CC melanosome transport and release from melanocytes (PubMed:21291502).
CC {ECO:0000250|UniProtKB:P62491, ECO:0000269|PubMed:21291502}.
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:P62491};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P62491};
CC -!- SUBUNIT: Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 (via its C-
CC terminus) and RAB11FIP4 (By similarity). Interacts with EVI5; EVI5 and
CC RAB11FIP3 may be mutually exclusive and compete for binding RAB11A (By
CC similarity). Interacts with RAB11FIP5 (By similarity). Interacts with
CC STXBP6 (By similarity). Interacts (GDP-bound form) with ZFYVE27 (By
CC similarity). Interacts with SGSM1, SGSM2, SGSM3 and VIPAS39
CC (PubMed:17509819, PubMed:20190753). Interacts with EXOC6 in a GTP-
CC dependent manner (PubMed:15292201). Interacts with BIRC6/bruce (By
CC similarity). May interact with TBC1D14 (By similarity). Interacts with
CC UNC119; in a cell cycle-dependent manner (By similarity). GDP-bound and
CC nucleotide-free forms interact with SH3BP5 (PubMed:26506309). Interacts
CC (GDP-bound form) with KIF5A in a ZFYVE27-dependent manner (By
CC similarity). Interacts (GDP-bound form) with RELCH (PubMed:29514919).
CC Found in a complex composed of RELCH, OSBP1 and RAB11A
CC (PubMed:29514919). Interacts with TBC1D12 (PubMed:28384198). Interacts
CC with DEF6 (By similarity). {ECO:0000250|UniProtKB:P62491,
CC ECO:0000250|UniProtKB:P62494, ECO:0000269|PubMed:15292201,
CC ECO:0000269|PubMed:17509819, ECO:0000269|PubMed:26506309,
CC ECO:0000269|PubMed:28384198, ECO:0000269|PubMed:29514919}.
CC -!- INTERACTION:
CC P62492; P59016: Vps33b; NbExp=3; IntAct=EBI-770256, EBI-2656383;
CC P62492; Q62739: Rab3ip; Xeno; NbExp=4; IntAct=EBI-770256, EBI-2028671;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P62491};
CC Lipid-anchor {ECO:0000305}. Recycling endosome membrane
CC {ECO:0000269|PubMed:29514919}; Lipid-anchor {ECO:0000305}. Cleavage
CC furrow {ECO:0000250|UniProtKB:P62491}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:P62491}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P62491}. Note=Translocates with RAB11FIP2 from
CC the vesicles of the endocytic recycling compartment (ERC) to the plasma
CC membrane. Localizes to the cleavage furrow. Colocalizes with PARD3,
CC PRKCI, EXOC5, OCLN, PODXL and RAB8A in apical membrane initiation sites
CC (AMIS) during the generation of apical surface and lumenogenesis.
CC {ECO:0000250|UniProtKB:P62491}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF127669; AAF36458.1; -; Genomic_DNA.
DR EMBL; AK014268; BAB29233.1; -; mRNA.
DR EMBL; AK132072; BAE20971.1; -; mRNA.
DR EMBL; AK132159; BAE21003.1; -; mRNA.
DR EMBL; AK147122; BAE27693.1; -; mRNA.
DR EMBL; BC010722; AAH10722.1; -; mRNA.
DR CCDS; CCDS23282.1; -.
DR RefSeq; NP_059078.2; NM_017382.5.
DR AlphaFoldDB; P62492; -.
DR SMR; P62492; -.
DR BioGRID; 207498; 17.
DR IntAct; P62492; 25.
DR MINT; P62492; -.
DR STRING; 10090.ENSMUSP00000129163; -.
DR iPTMnet; P62492; -.
DR PhosphoSitePlus; P62492; -.
DR SwissPalm; P62492; -.
DR jPOST; P62492; -.
DR PaxDb; P62492; -.
DR PeptideAtlas; P62492; -.
DR PRIDE; P62492; -.
DR ProteomicsDB; 255112; -.
DR TopDownProteomics; P62492; -.
DR Antibodypedia; 4588; 502 antibodies from 39 providers.
DR DNASU; 53869; -.
DR Ensembl; ENSMUST00000172298; ENSMUSP00000129163; ENSMUSG00000004771.
DR GeneID; 53869; -.
DR KEGG; mmu:53869; -.
DR UCSC; uc009qce.1; mouse.
DR CTD; 8766; -.
DR MGI; MGI:1858202; Rab11a.
DR VEuPathDB; HostDB:ENSMUSG00000004771; -.
DR eggNOG; KOG0087; Eukaryota.
DR GeneTree; ENSGT00940000154914; -.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; P62492; -.
DR OMA; SMKEDYY; -.
DR OrthoDB; 1133775at2759; -.
DR PhylomeDB; P62492; -.
DR TreeFam; TF300099; -.
DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 53869; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Rab11a; mouse.
DR PRO; PR:P62492; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P62492; protein.
DR Bgee; ENSMUSG00000004771; Expressed in lip and 261 other tissues.
DR ExpressionAtlas; P62492; baseline and differential.
DR Genevisible; P62492; MM.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005828; C:kinetochore microtubule; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0098837; C:postsynaptic recycling endosome; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; ISO:MGI.
DR GO; GO:0030953; P:astral microtubule organization; ISO:MGI.
DR GO; GO:0090150; P:establishment of protein localization to membrane; ISO:MGI.
DR GO; GO:0072594; P:establishment of protein localization to organelle; ISO:MGI.
DR GO; GO:0051650; P:establishment of vesicle localization; ISO:MGI.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:1990182; P:exosomal secretion; ISO:MGI.
DR GO; GO:0032402; P:melanosome transport; IMP:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:MGI.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI.
DR GO; GO:0036258; P:multivesicular body assembly; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; ISO:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:MGI.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0010796; P:regulation of multivesicular body size; ISO:MGI.
DR GO; GO:0051223; P:regulation of protein transport; ISO:MGI.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell membrane; Cytoplasmic vesicle;
KW Direct protein sequencing; Endosome; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT CHAIN 2..213
FT /note="Ras-related protein Rab-11A"
FT /id="PRO_0000121152"
FT PROPEP 214..216
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370808"
FT REGION 183..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 18..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 37..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT MOD_RES 213
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 212
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT CONFLICT 180
FT /note="Q -> H (in Ref. 1; AAF36458)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24394 MW; 76FC1E113A29B269 CRC64;
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI
KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM
LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF IETSALDSTN VEAAFQTILT EIYRIVSQKQ
MSDRRENDMS PSNNVVPIHV PPTTENKPKV QCCQNI
