RAB9A_HUMAN
ID RAB9A_HUMAN Reviewed; 201 AA.
AC P51151; A8K390; Q6ICN1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Ras-related protein Rab-9A;
GN Name=RAB9A; Synonyms=RAB9;
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].
RX PubMed=9126495; DOI=10.1006/geno.1997.4644;
RA Davies J.P., Cotter P.D., Ioannou Y.A.;
RT "Cloning and mapping of human Rab7 and Rab9 cDNA sequences and
RT identification of a Rab9 pseudogene.";
RL Genomics 41:131-134(1997).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 SUBCELLULAR LOCATION.
RX PubMed=16176980; DOI=10.1091/mbc.e05-03-0189;
RA Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M.;
RT "The oxysterol-binding protein homologue ORP1L interacts with Rab7 and
RT alters functional properties of late endocytic compartments.";
RL Mol. Biol. Cell 16:5480-5492(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION BY
RP 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 [9]
RP INTERACTION WITH GCC2.
RX PubMed=16885419; DOI=10.1091/mbc.e06-02-0153;
RA Reddy J.V., Burguete A.S., Sridevi K., Ganley I.G., Nottingham R.M.,
RA Pfeffer S.R.;
RT "A functional role for the GCC185 golgin in mannose 6-phosphate receptor
RT recycling.";
RL Mol. Biol. Cell 17:4353-4363(2006).
RN [10]
RP INTERACTION WITH GCC2.
RX PubMed=18243103; DOI=10.1016/j.cell.2007.11.048;
RA Burguete A.S., Fenn T.D., Brunger A.T., Pfeffer S.R.;
RT "Rab and Arl GTPase family members cooperate in the localization of the
RT golgin GCC185.";
RL Cell 132:286-298(2008).
RN [11]
RP IDENTIFICATION BY 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 [12]
RP INTERACTION WITH HPS4 AND BLOC-3 COMPLEX, ABSENCE OF INTERACTION WITH HPS1,
RP AND MUTAGENESIS OF ILE-40; PHE-44; TRP-61 AND GLN-66.
RX PubMed=20048159; DOI=10.1074/jbc.m109.069088;
RA Kloer D.P., Rojas R., Ivan V., Moriyama K., van Vlijmen T., Murthy N.,
RA Ghirlando R., van der Sluijs P., Hurley J.H., Bonifacino J.S.;
RT "Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-
RT 3) and its interaction with Rab9.";
RL J. Biol. Chem. 285:7794-7804(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP INTERACTION WITH SGSM2.
RX PubMed=21808068; DOI=10.1074/jbc.m111.261115;
RA Nottingham R.M., Ganley I.G., Barr F.A., Lambright D.G., Pfeffer S.R.;
RT "RUTBC1 protein, a Rab9A effector that activates GTP hydrolysis by Rab32
RT and Rab33B proteins.";
RL J. Biol. Chem. 286:33213-33222(2011).
RN [16]
RP 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 [17]
RP INTERACTION WITH SGSM1.
RX PubMed=22637480; DOI=10.1074/jbc.m112.362558;
RA Nottingham R.M., Pusapati G.V., Ganley I.G., Barr F.A., Lambright D.G.,
RA Pfeffer S.R.;
RT "RUTBC2 protein, a Rab9A effector and GTPase-activating protein for
RT Rab36.";
RL J. Biol. Chem. 287:22740-22748(2012).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-187, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
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 [22]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1-177 IN COMPLEX WITH GDP ANALOG.
RX PubMed=15263003; DOI=10.1074/jbc.m407114200;
RA Chen L., DiGiammarino E., Zhou X.E., Wang Y., Toh D., Hodge T.W.,
RA Meehan E.J.;
RT "High resolution crystal structure of human Rab9 GTPase: a novel antiviral
RT drug target.";
RL J. Biol. Chem. 279:40204-40208(2004).
CC -!- FUNCTION: Involved in the transport of proteins between the endosomes
CC and the trans Golgi network. Involved in the recruitment of SGSM2 to
CC melanosomes and is required for the proper trafficking of melanogenic
CC enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes.
CC {ECO:0000250|UniProtKB:P24408, ECO:0000250|UniProtKB:Q9R0M6}.
CC -!- SUBUNIT: Interacts (preferentially in its GTP-bound form) with GCC2
CC (via its GRIP domain) (PubMed:18243103, PubMed:16885419). Interacts
CC (GTP-bound form) with SGSM1; the GDP-bound form has much lower affinity
CC for SGSM1 (PubMed:22637480). Interacts with SGSM2 (PubMed:21808068).
CC The GTP-bound form but not the GDP-bound form interacts with HPS4 and
CC BLOC-3 complex (heterodimer of HPS1 and HPS4) but does not interact
CC with HPS1 alone (PubMed:20048159). {ECO:0000269|PubMed:16885419,
CC ECO:0000269|PubMed:18243103, ECO:0000269|PubMed:20048159,
CC ECO:0000269|PubMed:21808068, ECO:0000269|PubMed:22637480}.
CC -!- INTERACTION:
CC P51151; Q9Y2I1: NISCH; NbExp=8; IntAct=EBI-4401353, EBI-2688731;
CC P51151; Q8IWE5: PLEKHM2; NbExp=4; IntAct=EBI-4401353, EBI-726484;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum
CC membrane {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}. Late
CC endosome {ECO:0000269|PubMed:16176980}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9R0M6}. Melanosome
CC {ECO:0000250|UniProtKB:Q9R0M6}. Note=Colocalizes with OSBPL1A at the
CC late endosome (PubMed:16176980). Recruited to phagosomes containing
CC S.aureus or M.tuberculosis (PubMed:21255211).
CC {ECO:0000269|PubMed:16176980, ECO:0000269|PubMed:21255211}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; U44103; AAC51200.1; -; mRNA.
DR EMBL; AF498944; AAM21092.1; -; mRNA.
DR EMBL; CR450362; CAG29358.1; -; mRNA.
DR EMBL; AK290505; BAF83194.1; -; mRNA.
DR EMBL; CH471074; EAW98826.1; -; Genomic_DNA.
DR EMBL; BC017265; AAH17265.1; -; mRNA.
DR CCDS; CCDS14156.1; -.
DR PIR; G02361; G02361.
DR RefSeq; NP_001182257.1; NM_001195328.1.
DR RefSeq; NP_004242.1; NM_004251.4.
DR RefSeq; XP_016885453.1; XM_017029964.1.
DR PDB; 1WMS; X-ray; 1.25 A; A/B=1-177.
DR PDB; 7E1T; X-ray; 2.45 A; A/B=1-201.
DR PDBsum; 1WMS; -.
DR PDBsum; 7E1T; -.
DR AlphaFoldDB; P51151; -.
DR SMR; P51151; -.
DR BioGRID; 114768; 587.
DR CORUM; P51151; -.
DR DIP; DIP-46409N; -.
DR IntAct; P51151; 168.
DR MINT; P51151; -.
DR STRING; 9606.ENSP00000420127; -.
DR ChEMBL; CHEMBL1293294; -.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR iPTMnet; P51151; -.
DR PhosphoSitePlus; P51151; -.
DR BioMuta; RAB9A; -.
DR DMDM; 1710003; -.
DR EPD; P51151; -.
DR jPOST; P51151; -.
DR MassIVE; P51151; -.
DR MaxQB; P51151; -.
DR PaxDb; P51151; -.
DR PeptideAtlas; P51151; -.
DR PRIDE; P51151; -.
DR ProteomicsDB; 56285; -.
DR Antibodypedia; 513; 289 antibodies from 35 providers.
DR DNASU; 9367; -.
DR Ensembl; ENST00000464506.2; ENSP00000420127.1; ENSG00000123595.8.
DR Ensembl; ENST00000618931.2; ENSP00000480777.1; ENSG00000123595.8.
DR GeneID; 9367; -.
DR KEGG; hsa:9367; -.
DR MANE-Select; ENST00000464506.2; ENSP00000420127.1; NM_004251.5; NP_004242.1.
DR UCSC; uc004cvm.5; human.
DR CTD; 9367; -.
DR DisGeNET; 9367; -.
DR GeneCards; RAB9A; -.
DR HGNC; HGNC:9792; RAB9A.
DR HPA; ENSG00000123595; Low tissue specificity.
DR MIM; 300284; gene.
DR neXtProt; NX_P51151; -.
DR OpenTargets; ENSG00000123595; -.
DR PharmGKB; PA34152; -.
DR VEuPathDB; HostDB:ENSG00000123595; -.
DR eggNOG; KOG0394; Eukaryota.
DR GeneTree; ENSGT00940000158619; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; P51151; -.
DR OMA; FQNLGNW; -.
DR OrthoDB; 1172019at2759; -.
DR PhylomeDB; P51151; -.
DR TreeFam; TF326442; -.
DR PathwayCommons; P51151; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-HSA-9706019; RHOBTB3 ATPase cycle.
DR SignaLink; P51151; -.
DR SIGNOR; P51151; -.
DR BioGRID-ORCS; 9367; 18 hits in 705 CRISPR screens.
DR ChiTaRS; RAB9A; human.
DR EvolutionaryTrace; P51151; -.
DR GeneWiki; RAB9A; -.
DR GenomeRNAi; 9367; -.
DR Pharos; P51151; Tbio.
DR PRO; PR:P51151; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51151; protein.
DR Bgee; ENSG00000123595; Expressed in amniotic fluid and 206 other tissues.
DR ExpressionAtlas; P51151; baseline and differential.
DR Genevisible; P51151; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0030133; C:transport vesicle; 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; IDA:UniProtKB.
DR GO; GO:0052403; P:negative regulation by host of symbiont catalytic activity; IMP:AgBase.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0032880; P:regulation of protein localization; IMP:AgBase.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR CDD; cd04116; Rab9; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041824; Rab9.
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; Acetylation; Cell membrane; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Endosome; Golgi apparatus; GTP-binding; Lipoprotein;
KW Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..201
FT /note="Ras-related protein Rab-9A"
FT /id="PRO_0000121139"
FT MOTIF 36..44
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 14..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:15263003,
FT ECO:0007744|PDB:1WMS"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:15263003,
FT ECO:0007744|PDB:1WMS"
FT BINDING 155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:15263003,
FT ECO:0007744|PDB:1WMS"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 40
FT /note="I->L: Loss of interaction with HPS4; when associated
FT with L-66."
FT /evidence="ECO:0000269|PubMed:20048159"
FT MUTAGEN 44
FT /note="F->L: Loss of interaction with HPS4; when associated
FT with L-66."
FT /evidence="ECO:0000269|PubMed:20048159"
FT MUTAGEN 61
FT /note="W->L: Loss of interaction with HPS4; when associated
FT with L-66."
FT /evidence="ECO:0000269|PubMed:20048159"
FT MUTAGEN 66
FT /note="Q->L: Loss of interaction with HPS4; when associated
FT with L-40 or L-44 or L-61."
FT /evidence="ECO:0000269|PubMed:20048159"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:1WMS"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:1WMS"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:1WMS"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:1WMS"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1WMS"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:1WMS"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:1WMS"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1WMS"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:1WMS"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:1WMS"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1WMS"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1WMS"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:1WMS"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1WMS"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1WMS"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:1WMS"
SQ SEQUENCE 201 AA; 22838 MW; 65B502C21E97DB72 CRC64;
MAGKSSLFKV ILLGDGGVGK SSLMNRYVTN KFDTQLFHTI GVEFLNKDLE VDGHFVTMQI
WDTAGQERFR SLRTPFYRGS DCCLLTFSVD DSQSFQNLSN WKKEFIYYAD VKEPESFPFV
ILGNKIDISE RQVSTEEAQA WCRDNGDYPY FETSAKDATN VAAAFEEAVR RVLATEDRSD
HLIQTDTVNL HRKPKPSSSC C
