RAB43_HUMAN
ID RAB43_HUMAN Reviewed; 212 AA.
AC Q86YS6; A8K4P9; E9PBQ0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Ras-related protein Rab-43;
DE AltName: Full=Ras-related protein Rab-41;
GN Name=RAB43; Synonyms=RAB41;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=15018353; DOI=10.1080/10425170310001617902;
RA Guo J.H., Chen L., Chen S., Liu X., Saiyin H., Deng Q., Zhuang Y., Wan B.,
RA Yu L., Zhao S.Y.;
RT "Isolation, expression pattern of a novel human RAB gene RAB41 and
RT characterization of its intronless homolog RAB41P.";
RL DNA Seq. 14:431-435(2003).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17562788; DOI=10.1083/jcb.200612068;
RA Fuchs E., Haas A.K., Spooner R.A., Yoshimura S., Lord J.M., Barr F.A.;
RT "Specific Rab GTPase-activating proteins define the Shiga toxin and
RT epidermal growth factor uptake pathways.";
RL J. Cell Biol. 177:1133-1143(2007).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF THR-32.
RX PubMed=17684057; DOI=10.1242/jcs.014225;
RA Haas A.K., Yoshimura S., Stephens D.J., Preisinger C., Fuchs E., Barr F.A.;
RT "Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs
RT required to maintain a functional Golgi complex in human cells.";
RL J. Cell Sci. 120:2997-3010(2007).
RN [8]
RP FUNCTION, MUTAGENESIS OF THR-32, AND SUBCELLULAR LOCATION.
RX PubMed=18664496; DOI=10.1242/jcs.021808;
RA Dejgaard S.Y., Murshid A., Erman A., Kizilay O., Verbich D., Lodge R.,
RA Dejgaard K., Ly-Hartig T.B., Pepperkok R., Simpson J.C., Presley J.F.;
RT "Rab18 and Rab43 have key roles in ER-Golgi trafficking.";
RL J. Cell Sci. 121:2768-2781(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP 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 [11]
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 [12]
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 [13]
RP INTERACTION WITH GDI1; GDI2; CHM AND CHML, PHOSPHORYLATION AT THR-82, AND
RP MUTAGENESIS OF THR-82.
RX PubMed=29125462; DOI=10.7554/elife.31012;
RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA Mann M.;
RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT establishes a connection to ciliogenesis.";
RL Elife 6:0-0(2017).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 9-190 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human RAB43 in complex with GDP.";
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. The low intrinsic GTPase
CC activity of RAB43 is activated by USP6NL. Involved in retrograde
CC transport from the endocytic pathway to the Golgi apparatus. Involved
CC in the transport of Shiga toxin from early and recycling endosomes to
CC the trans-Golgi network. Required for the structural integrity of the
CC Golgi complex. Plays a role in the maturation of phagosomes that engulf
CC pathogens, such as S.aureus and M.tuberculosis.
CC {ECO:0000269|PubMed:17562788, ECO:0000269|PubMed:17684057,
CC ECO:0000269|PubMed:18664496, ECO:0000269|PubMed:21255211}.
CC -!- SUBUNIT: Interacts with GDI1, GDI2, CHM and CHML; phosphorylation at
CC Thr-82 disrupts these interactions. {ECO:0000269|PubMed:29125462}.
CC -!- INTERACTION:
CC Q86YS6; P04792: HSPB1; NbExp=2; IntAct=EBI-4401730, EBI-352682;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Golgi apparatus {ECO:0000269|PubMed:17562788,
CC ECO:0000269|PubMed:18664496}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus,
CC trans-Golgi network {ECO:0000269|PubMed:17562788}. Note=Recruited to
CC phagosomes containing S.aureus or M.tuberculosis (PubMed:21255211).
CC {ECO:0000269|PubMed:21255211}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86YS6-1; Sequence=Displayed;
CC Name=2; Synonyms=ISY1-RAB43;
CC IsoId=Q9ULR0-1; Sequence=External;
CC Name=3;
CC IsoId=Q86YS6-2; Sequence=VSP_054030, VSP_054031;
CC -!- TISSUE SPECIFICITY: Widely expressed in brain, testis, lung, heart,
CC ovary, colon, kidney, uterus and spleen but not in liver.
CC {ECO:0000269|PubMed:15018353}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AY166852; AAO17291.1; -; mRNA.
DR EMBL; AK291014; BAF83703.1; -; mRNA.
DR EMBL; AC108673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79283.1; -; Genomic_DNA.
DR EMBL; BC062319; AAH62319.1; -; mRNA.
DR CCDS; CCDS33850.1; -. [Q86YS6-1]
DR CCDS; CCDS56275.1; -. [Q86YS6-2]
DR RefSeq; NP_001191812.1; NM_001204883.1. [Q86YS6-1]
DR RefSeq; NP_001191813.1; NM_001204884.1. [Q86YS6-1]
DR RefSeq; NP_001191814.1; NM_001204885.1. [Q86YS6-1]
DR RefSeq; NP_001191815.1; NM_001204886.1. [Q86YS6-1]
DR RefSeq; NP_001191816.1; NM_001204887.1. [Q86YS6-2]
DR RefSeq; NP_940892.1; NM_198490.2. [Q86YS6-1]
DR PDB; 2HUP; X-ray; 2.05 A; A/B=9-190.
DR PDBsum; 2HUP; -.
DR AlphaFoldDB; Q86YS6; -.
DR SMR; Q86YS6; -.
DR BioGRID; 130830; 41.
DR IntAct; Q86YS6; 6.
DR MINT; Q86YS6; -.
DR STRING; 9606.ENSP00000319781; -.
DR iPTMnet; Q86YS6; -.
DR PhosphoSitePlus; Q86YS6; -.
DR BioMuta; RAB43; -.
DR DMDM; 74727944; -.
DR EPD; Q86YS6; -.
DR jPOST; Q86YS6; -.
DR MassIVE; Q86YS6; -.
DR MaxQB; Q86YS6; -.
DR PaxDb; Q86YS6; -.
DR PeptideAtlas; Q86YS6; -.
DR PRIDE; Q86YS6; -.
DR ProteomicsDB; 19270; -.
DR ProteomicsDB; 70463; -. [Q86YS6-1]
DR Antibodypedia; 34842; 103 antibodies from 24 providers.
DR DNASU; 339122; -.
DR Ensembl; ENST00000315150.10; ENSP00000319781.6; ENSG00000172780.17. [Q86YS6-1]
DR Ensembl; ENST00000393304.5; ENSP00000376981.1; ENSG00000172780.17. [Q86YS6-1]
DR Ensembl; ENST00000393305.5; ENSP00000376982.1; ENSG00000172780.17. [Q86YS6-1]
DR Ensembl; ENST00000393307.5; ENSP00000376984.1; ENSG00000172780.17. [Q86YS6-1]
DR Ensembl; ENST00000393308.5; ENSP00000376985.1; ENSG00000172780.17. [Q86YS6-1]
DR Ensembl; ENST00000476465.5; ENSP00000427632.1; ENSG00000172780.17. [Q86YS6-2]
DR Ensembl; ENST00000615093.1; ENSP00000481399.1; ENSG00000172780.17. [Q86YS6-2]
DR GeneID; 339122; -.
DR KEGG; hsa:339122; -.
DR MANE-Select; ENST00000315150.10; ENSP00000319781.6; NM_198490.3; NP_940892.1.
DR UCSC; uc003eln.3; human. [Q86YS6-1]
DR CTD; 339122; -.
DR DisGeNET; 339122; -.
DR GeneCards; RAB43; -.
DR HGNC; HGNC:19983; RAB43.
DR HPA; ENSG00000172780; Tissue enhanced (liver).
DR neXtProt; NX_Q86YS6; -.
DR OpenTargets; ENSG00000172780; -.
DR PharmGKB; PA134968262; -.
DR VEuPathDB; HostDB:ENSG00000172780; -.
DR eggNOG; KOG0084; Eukaryota.
DR GeneTree; ENSGT00940000161980; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q86YS6; -.
DR OMA; MFVMETS; -.
DR PhylomeDB; Q86YS6; -.
DR TreeFam; TF300097; -.
DR PathwayCommons; Q86YS6; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q86YS6; -.
DR BioGRID-ORCS; 339122; 41 hits in 1041 CRISPR screens.
DR EvolutionaryTrace; Q86YS6; -.
DR GenomeRNAi; 339122; -.
DR Pharos; Q86YS6; Tbio.
DR PRO; PR:Q86YS6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q86YS6; protein.
DR Bgee; ENSG00000172780; Expressed in blood and 94 other tissues.
DR ExpressionAtlas; Q86YS6; baseline and differential.
DR Genevisible; Q86YS6; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; 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:0035526; P:retrograde transport, plasma membrane to Golgi; IMP:UniProtKB.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR GO; GO:0019068; P:virion assembly; 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; Alternative splicing; Cytoplasmic vesicle; Golgi apparatus;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..212
FT /note="Ras-related protein Rab-43"
FT /id="PRO_0000244615"
FT MOTIF 47..55
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 25..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 73..77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 163..164
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CG50"
FT MOD_RES 82
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29125462"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 212
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 210
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 212
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 130..155
FT /note="GNKSDLSELREVSLAEAQSLAEHYDI -> EMQSCYVAQADLELLASSNPPA
FT STSK (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054030"
FT VAR_SEQ 156..212
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054031"
FT MUTAGEN 32
FT /note="T->N: Abolishes activity. Disrupts Golgi structure."
FT /evidence="ECO:0000269|PubMed:17684057,
FT ECO:0000269|PubMed:18664496"
FT MUTAGEN 82
FT /note="T->A: Loss of phosphorylation. No effect on binding
FT of GDI1 and GDI2."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 82
FT /note="T->E: Phosphomimetic mutant. Loss of binding to
FT GDI1, GDI2, CHM and CHML."
FT /evidence="ECO:0000269|PubMed:29125462"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:2HUP"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:2HUP"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:2HUP"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:2HUP"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2HUP"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:2HUP"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:2HUP"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:2HUP"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:2HUP"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:2HUP"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2HUP"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:2HUP"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2HUP"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:2HUP"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:2HUP"
SQ SEQUENCE 212 AA; 23339 MW; 087EE3802B7159C9 CRC64;
MAGPGPGPGD PDEQYDFLFK LVLVGDASVG KTCVVQRFKT GAFSERQGST IGVDFTMKTL
EIQGKRVKLQ IWDTAGQERF RTITQSYYRS ANGAILAYDI TKRSSFLSVP HWIEDVRKYA
GSNIVQLLIG NKSDLSELRE VSLAEAQSLA EHYDILCAIE TSAKDSSNVE EAFLRVATEL
IMRHGGPLFS EKSPDHIQLN SKDIGEGWGC GC
