RAB31_HUMAN
ID RAB31_HUMAN Reviewed; 194 AA.
AC Q13636; B2RBT7; Q15770; Q9HC00;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Ras-related protein Rab-31;
DE AltName: Full=Ras-related protein Rab-22B;
GN Name=RAB31; Synonyms=RAB22B;
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].
RC TISSUE=Melanocyte;
RX PubMed=8863739; DOI=10.1016/0378-1119(96)00509-4;
RA Chen D., Guo J., Miki T., Tachibana M., Gahl W.A.;
RT "Molecular cloning of two novel rab genes from human melanocytes.";
RL Gene 174:129-134(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND MUTAGENESIS OF GLN-64.
RC TISSUE=Platelet;
RX PubMed=11784320; DOI=10.1046/j.0014-2956.2001.02645.x;
RA Bao X., Faris A.E., Jang E.K., Haslam R.J.;
RT "Molecular cloning, bacterial expression and properties of Rab31 and
RT Rab32.";
RL Eur. J. Biochem. 269:259-271(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Opdam F.J.M., van den Vorstenbosch R., Booltink E., Fransen J.A.M.;
RT "Small GTPase Rab22B is expressed in intestinal epithelial Caco-2 cells.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pheochromocytoma;
RA Peng Y., Gu Y., Tu Y., Xu S., Han Z., Fu G., Chen Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17678623; DOI=10.1016/j.bbrc.2007.07.076;
RA Ng E.L., Wang Y., Tang B.L.;
RT "Rab22B's role in trans-Golgi network membrane dynamics.";
RL Biochem. Biophys. Res. Commun. 361:751-757(2007).
RN [13]
RP FUNCTION, INTERACTION WITH GAPVD1 AND EEA1, AND SUBCELLULAR LOCATION.
RX PubMed=17189207; DOI=10.1016/j.cmet.2006.12.006;
RA Lodhi I.J., Chiang S.-H., Chang L., Vollenweider D., Watson R.T., Inoue M.,
RA Pessin J.E., Saltiel A.R.;
RT "Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates Glut4
RT trafficking in adipocytes.";
RL Cell Metab. 5:59-72(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EGFR AND EEA1.
RX PubMed=19725050; DOI=10.1002/jcp.21911;
RA Ng E.L., Ng J.J., Liang F., Tang B.L.;
RT "Rab22B is expressed in the CNS astroglia lineage and plays a role in
RT epidermal growth factor receptor trafficking in A431 cells.";
RL J. Cell. Physiol. 221:716-728(2009).
RN [16]
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 [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RIN3.
RX PubMed=21586568; DOI=10.1074/jbc.m110.172445;
RA Kajiho H., Sakurai K., Minoda T., Yoshikawa M., Nakagawa S., Fukushima S.,
RA Kontani K., Katada T.;
RT "Characterization of RIN3 as a guanine nucleotide exchange factor for the
RT Rab5 subfamily GTPase Rab31.";
RL J. Biol. Chem. 286:24364-24373(2011).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
RA Seto S., Tsujimura K., Koide Y.;
RT "Rab GTPases regulating phagosome maturation are differentially recruited
RT to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
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).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-174 IN COMPLEX WITH GTP ANALOG.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human RAB31 in complex with a GTP analogue.";
RL Submitted (FEB-2009) to the PDB data bank.
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. Required for the integrity
CC and for normal function of the Golgi apparatus and the trans-Golgi
CC network. Plays a role in insulin-stimulated translocation of GLUT4 to
CC the cell membrane. Plays a role in M6PR transport from the trans-Golgi
CC network to endosomes. Plays a role in the internalization of EGFR from
CC the cell membrane into endosomes. Plays a role in the maturation of
CC phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis.
CC {ECO:0000269|PubMed:17189207, ECO:0000269|PubMed:17678623,
CC ECO:0000269|PubMed:19725050, ECO:0000269|PubMed:21255211,
CC ECO:0000269|PubMed:21586568}.
CC -!- SUBUNIT: Interacts with OCRL. Interacts with NGFR (By similarity).
CC Interacts (in GDP-bound form) with RIN3 and GAPVD1, which function as
CC guanine exchange factors (GEF). Interacts (in GTP-bound form) with
CC EEA1. Interacts with EGFR. Interacts (in GTP-bound form) with APPL2;
CC interaction contributes to or enhances recruitment of APPL2 to the
CC phagosomes; interaction enhances Fc-gamma receptor-mediated
CC phagocytosis through PI3K/Akt signaling in macrophages (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q921E2,
CC ECO:0000269|PubMed:17189207, ECO:0000269|PubMed:19725050,
CC ECO:0000269|PubMed:21586568, ECO:0000269|Ref.21}.
CC -!- INTERACTION:
CC Q13636; Q60I27: ALS2CL; NbExp=3; IntAct=EBI-725987, EBI-12078276;
CC Q13636; P27797: CALR; NbExp=3; IntAct=EBI-725987, EBI-1049597;
CC Q13636; P36957: DLST; NbExp=3; IntAct=EBI-725987, EBI-351007;
CC Q13636; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-725987, EBI-1055945;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:17189207, ECO:0000269|PubMed:17678623,
CC ECO:0000269|PubMed:19725050, ECO:0000269|PubMed:21586568}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome
CC {ECO:0000269|PubMed:17189207, ECO:0000269|PubMed:21586568}. Cytoplasmic
CC vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305};
CC Cytoplasmic side {ECO:0000305}. Note=Rapidly recruited to phagosomes
CC containing S.aureus or M.tuberculosis (PubMed:21255211).
CC {ECO:0000269|PubMed:21255211}.
CC -!- TISSUE SPECIFICITY: Highest expression in placenta and brain with lower
CC levels in heart and lung. Not detected in liver, skeletal muscle,
CC kidney or pancreas. {ECO:0000269|PubMed:11784320}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09690.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH01148.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U57091; AAC50773.1; -; mRNA.
DR EMBL; U59877; AAB02832.1; -; mRNA.
DR EMBL; AF234995; AAG13847.1; -; mRNA.
DR EMBL; AF183421; AAG09690.1; ALT_INIT; mRNA.
DR EMBL; AF498957; AAM21105.1; -; mRNA.
DR EMBL; AK314809; BAG37334.1; -; mRNA.
DR EMBL; BT020027; AAV38830.1; -; mRNA.
DR EMBL; BT020028; AAV38831.1; -; mRNA.
DR EMBL; CR407659; CAG28587.1; -; mRNA.
DR EMBL; AC006238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001148; AAH01148.1; ALT_INIT; mRNA.
DR PIR; JC4961; JC4961.
DR RefSeq; NP_006859.2; NM_006868.3.
DR PDB; 2FG5; X-ray; 2.80 A; A=2-174.
DR PDBsum; 2FG5; -.
DR AlphaFoldDB; Q13636; -.
DR SMR; Q13636; -.
DR BioGRID; 116221; 47.
DR IntAct; Q13636; 20.
DR MINT; Q13636; -.
DR STRING; 9606.ENSP00000461945; -.
DR GlyGen; Q13636; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13636; -.
DR PhosphoSitePlus; Q13636; -.
DR BioMuta; RAB31; -.
DR DMDM; 2500069; -.
DR EPD; Q13636; -.
DR jPOST; Q13636; -.
DR MassIVE; Q13636; -.
DR MaxQB; Q13636; -.
DR PaxDb; Q13636; -.
DR PeptideAtlas; Q13636; -.
DR PRIDE; Q13636; -.
DR ProteomicsDB; 59631; -.
DR Antibodypedia; 21931; 195 antibodies from 27 providers.
DR DNASU; 11031; -.
DR Ensembl; ENST00000578921.6; ENSP00000461945.2; ENSG00000168461.13.
DR GeneID; 11031; -.
DR KEGG; hsa:11031; -.
DR UCSC; uc002kog.3; human.
DR CTD; 11031; -.
DR DisGeNET; 11031; -.
DR GeneCards; RAB31; -.
DR HGNC; HGNC:9771; RAB31.
DR HPA; ENSG00000168461; Low tissue specificity.
DR MIM; 605694; gene.
DR neXtProt; NX_Q13636; -.
DR PharmGKB; PA34122; -.
DR VEuPathDB; HostDB:ENSG00000168461; -.
DR eggNOG; KOG0092; Eukaryota.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; Q13636; -.
DR OMA; CMHGGKP; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; Q13636; -.
DR TreeFam; TF331262; -.
DR PathwayCommons; Q13636; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q13636; -.
DR BioGRID-ORCS; 11031; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; RAB31; human.
DR EvolutionaryTrace; Q13636; -.
DR GeneWiki; RAB31; -.
DR GenomeRNAi; 11031; -.
DR Pharos; Q13636; Tbio.
DR PRO; PR:Q13636; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q13636; protein.
DR Bgee; ENSG00000168461; Expressed in dorsal motor nucleus of vagus nerve and 212 other tissues.
DR ExpressionAtlas; Q13636; baseline and differential.
DR Genevisible; Q13636; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0036186; C:early phagosome membrane; ISS:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
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:0032869; P:cellular response to insulin stimulus; IMP:UniProtKB.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0090382; P:phagosome maturation; IMP:UniProtKB.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; IMP:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; IMP:UniProtKB.
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 3D-structure; Cytoplasmic vesicle; Endosome; Golgi apparatus; GTP-binding;
KW Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Reference proteome.
FT CHAIN 1..194
FT /note="Ras-related protein Rab-31"
FT /id="PRO_0000121232"
FT MOTIF 34..42
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT LIPID 193
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 194
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 64
FT /note="Q->L: No change in GTPase activity."
FT /evidence="ECO:0000269|PubMed:11784320"
FT CONFLICT 189
FT /note="A -> S (in Ref. 1; AAC50773)"
FT /evidence="ECO:0000305"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:2FG5"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:2FG5"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:2FG5"
FT STRAND 50..61
FT /evidence="ECO:0007829|PDB:2FG5"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:2FG5"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2FG5"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:2FG5"
FT HELIX 91..106
FT /evidence="ECO:0007829|PDB:2FG5"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:2FG5"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:2FG5"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:2FG5"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2FG5"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:2FG5"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:2FG5"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:2FG5"
SQ SEQUENCE 194 AA; 21569 MW; 19825648A9C214B9 CRC64;
MAIRELKVCL LGDTGVGKSS IVCRFVQDHF DHNISPTIGA SFMTKTVPCG NELHKFLIWD
TAGQERFHSL APMYYRGSAA AVIVYDITKQ DSFYTLKKWV KELKEHGPEN IVMAIAGNKC
DLSDIREVPL KDAKEYAESI GAIVVETSAK NAINIEELFQ GISRQIPPLD PHENGNNGTI
KVEKPTMQAS RRCC
