RAB5A_MOUSE
ID RAB5A_MOUSE Reviewed; 215 AA.
AC Q9CQD1; Q3UCX7; Q4VAA1; Q9DCN5;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ras-related protein Rab-5A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P20339};
GN Name=Rab5a; Synonyms=nnyRab5a;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11773082; DOI=10.1074/jbc.m112414200;
RA Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.;
RT "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2
RT functions as a novel Rab27A binding domain.";
RL J. Biol. Chem. 277:9212-9218(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=16923123; DOI=10.1111/j.1365-2443.2006.00997.x;
RA Itoh T., Satoh M., Kanno E., Fukuda M.;
RT "Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing
RT proteins based on their Rab-binding activity.";
RL Genes Cells 11:1023-1037(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, 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., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PROTEIN SEQUENCE OF 23-33; 82-110 AND 184-195, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
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 small
RT G protein (RAP and RAB)-mediated signaling pathway.";
RL Genomics 90:249-260(2007).
RN [8]
RP FUNCTION, INTERACTION WITH PIK3C3 AND DYN2, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF SER-34 AND GLN-79.
RX PubMed=18425118; DOI=10.1038/ncb1718;
RA Kinchen J.M., Doukoumetzidis K., Almendinger J., Stergiou L.,
RA Tosello-Trampont A., Sifri C.D., Hengartner M.O., Ravichandran K.S.;
RT "A pathway for phagosome maturation during engulfment of apoptotic cells.";
RL Nat. Cell Biol. 10:556-566(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH PIK3CB.
RX PubMed=21059846; DOI=10.1083/jcb.201006056;
RA Dou Z., Chattopadhyay M., Pan J.-A., Guerriero J.L., Jiang Y.-P.,
RA Ballou L.M., Yue Z., Lin R.Z., Zong W.-X.;
RT "The class IA phosphatidylinositol 3-kinase p110-beta subunit is a positive
RT regulator of autophagy.";
RL J. Cell Biol. 191:827-843(2010).
RN [11]
RP SUBCELLULAR LOCATION, INTERACTION WITH OCRL AND INPP5F, AND MUTAGENESIS OF
RP SER-34 AND GLN-79.
RX PubMed=25869668; DOI=10.1083/jcb.201409064;
RA Nakatsu F., Messa M., Nandez R., Czapla H., Zou Y., Strittmatter S.M.,
RA De Camilli P.;
RT "Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic
RT pathway.";
RL J. Cell Biol. 209:85-95(2015).
RN [12]
RP INTERACTION WITH APPL2.
RX PubMed=25568335; DOI=10.1091/mbc.e14-10-1457;
RA Yeo J.C., Wall A.A., Luo L., Stow J.L.;
RT "Rab31 and APPL2 enhance FcgammaR-mediated phagocytosis through PI3K/Akt
RT signaling in macrophages.";
RL Mol. Biol. Cell 26:952-965(2015).
CC -!- FUNCTION: Small GTPase which cycles between active GTP-bound and
CC inactive GDP-bound states. In its active state, binds to a variety of
CC effector proteins to regulate cellular responses such as of
CC intracellular membrane trafficking, from the formation of transport
CC vesicles to their fusion with membranes. Active GTP-bound form is able
CC to recruit to membranes different sets of downstream effectors directly
CC responsible for vesicle formation, movement, tethering and fusion.
CC RAB5A is required for the fusion of plasma membranes and early
CC endosomes. Contributes to the regulation of filopodia extension.
CC Required for the exosomal release of SDCBP, CD63, PDCD6IP and syndecan
CC (By similarity). Regulates maturation of apoptotic cell-containing
CC phagosomes, probably downstream of DYN2 and PIK3C3 (PubMed:18425118).
CC {ECO:0000250|UniProtKB:P18066, ECO:0000250|UniProtKB:P20339,
CC ECO:0000269|PubMed:18425118}.
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:P20339};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P20339};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP.
CC {ECO:0000250|UniProtKB:P18066}.
CC -!- SUBUNIT: Interacts with GDI1; this promotes dissociation from
CC membranes; phosphorylation at Ser-84 disrupts this interaction (By
CC similarity). Interacts with GDI2; phosphorylation at Ser-84 disrupts
CC the interaction (By similarity). Interacts with EEA1. Interacts with
CC RIN1 and GAPVD1, which regulate its pathway, probably by acting as a
CC GEF. Interacts with RINL. Interacts with ALS2CL, SUN2, ZFYVE20 and
CC RUFY1. Interacts with RABEP1; one RABEP1 homodimer binds two RAB5A
CC chains, but at opposite sides of the dimer (By similarity). Interacts
CC with SGSM1 and SGSM3 (PubMed:17509819). Interacts with PIK3CB
CC (PubMed:21059846). Interacts with OCRL and INPP5F (PubMed:25869668).
CC May be a component of a complex composed of RAB5A, DYN2 and PIK3C3
CC (PubMed:18425118). Does not interact with BLOC-3 complex (heterodimer
CC of HPS1 and HPS4). Interacts with CLN5 (By similarity). Interacts with
CC APPL2 (PubMed:25568335). Interacts with F8A1/F8A2/F8A3 (By similarity).
CC Found in a complex with F8A1/F8A2/F8A3, HTT and RAB5A; mediates the
CC recruitment of HTT by RAB5A onto early endosomes (By similarity).
CC {ECO:0000250|UniProtKB:P18066, ECO:0000250|UniProtKB:P20339,
CC ECO:0000250|UniProtKB:Q0IIG7, ECO:0000269|PubMed:17509819,
CC ECO:0000269|PubMed:21059846, ECO:0000269|PubMed:25568335,
CC ECO:0000269|PubMed:25869668, ECO:0000305|PubMed:18425118}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20339};
CC Lipid-anchor {ECO:0000250|UniProtKB:P20339}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P18066}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P20339}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P20339}. Melanosome
CC {ECO:0000269|PubMed:25869668}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:P20339}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:P18066}. Membrane
CC {ECO:0000250|UniProtKB:P20339}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P20339}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000269|PubMed:18425118}. Endosome membrane
CC {ECO:0000250|UniProtKB:P20339}. Note=Enriched in stage I melanosomes.
CC Alternates between membrane-bound and cytosolic forms.
CC {ECO:0000250|UniProtKB:P20339}.
CC -!- PTM: Phosphorylation of Ser-84 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including RAB GDP
CC dissociation inhibitors GDI1 and GDI2. {ECO:0000250|UniProtKB:P20339}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AB232593; BAF02855.1; -; mRNA.
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; AK150296; BAE29448.1; -; mRNA.
DR EMBL; AK150346; BAE29485.1; -; mRNA.
DR EMBL; AK150405; BAE29531.1; -; mRNA.
DR EMBL; AK151066; BAE30082.1; -; mRNA.
DR EMBL; AK153131; BAE31744.1; -; mRNA.
DR EMBL; AK159706; BAE35305.1; -; mRNA.
DR EMBL; CH466559; EDL23663.1; -; Genomic_DNA.
DR EMBL; BC004842; AAH04842.1; -; mRNA.
DR EMBL; BC034370; AAH34370.1; -; mRNA.
DR EMBL; BC096481; AAH96481.1; -; mRNA.
DR CCDS; CCDS28879.1; -.
DR RefSeq; NP_080163.1; NM_025887.4.
DR AlphaFoldDB; Q9CQD1; -.
DR SMR; Q9CQD1; -.
DR BioGRID; 234840; 30.
DR IntAct; Q9CQD1; 11.
DR MINT; Q9CQD1; -.
DR STRING; 10090.ENSMUSP00000017975; -.
DR iPTMnet; Q9CQD1; -.
DR PhosphoSitePlus; Q9CQD1; -.
DR SwissPalm; Q9CQD1; -.
DR EPD; Q9CQD1; -.
DR jPOST; Q9CQD1; -.
DR MaxQB; Q9CQD1; -.
DR PaxDb; Q9CQD1; -.
DR PeptideAtlas; Q9CQD1; -.
DR PRIDE; Q9CQD1; -.
DR ProteomicsDB; 300381; -.
DR Antibodypedia; 3882; 780 antibodies from 41 providers.
DR DNASU; 271457; -.
DR Ensembl; ENSMUST00000017975; ENSMUSP00000017975; ENSMUSG00000017831.
DR GeneID; 271457; -.
DR KEGG; mmu:271457; -.
DR UCSC; uc008czn.1; mouse.
DR CTD; 5868; -.
DR MGI; MGI:105926; Rab5a.
DR VEuPathDB; HostDB:ENSMUSG00000017831; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000154337; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; Q9CQD1; -.
DR OMA; DGIDCAE; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; Q9CQD1; -.
DR TreeFam; TF300199; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 271457; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Rab5a; mouse.
DR PRO; PR:Q9CQD1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CQD1; protein.
DR Bgee; ENSMUSG00000017831; Expressed in esophagus and 66 other tissues.
DR Genevisible; Q9CQD1; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0030424; C:axon; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043679; C:axon terminus; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0098559; C:cytoplasmic side of early endosome membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0032009; C:early phagosome; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0098842; C:postsynaptic early endosome; ISO:MGI.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0036477; C:somatodendritic compartment; ISS:ParkinsonsUK-UCL.
DR GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043195; C:terminal bouton; ISS:ParkinsonsUK-UCL.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
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; IDA:MGI.
DR GO; GO:0019001; F:guanyl nucleotide binding; IDA:MGI.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; ISO:MGI.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IDA:MGI.
DR GO; GO:0007032; P:endosome organization; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0044788; P:modulation by host of viral process; ISO:MGI.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:2000286; P:receptor internalization involved in canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR GO; GO:0051036; P:regulation of endosome size; ISO:MGI.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISO:MGI.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0036465; P:synaptic vesicle recycling; 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 Cell membrane; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Endocytosis; Endosome; GTP-binding; Hydrolase;
KW Lipoprotein; Membrane; Nucleotide-binding; Phagocytosis; Phosphoprotein;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..215
FT /note="Ras-related protein Rab-5A"
FT /id="PRO_0000121106"
FT REGION 181..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 49..57
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 27..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT BINDING 46..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT BINDING 163..165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT LIPID 212
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT MUTAGEN 34
FT /note="S->N: Inhibits endosome localization. Disrupts
FT interaction of RAB5A and OCRL with INPP5F. Prevents its
FT localization to apoptotic cell corpse-containing early
FT phagosomes. Maturation of apoptotic cell-containing
FT phagosome into acidic phagosomes is decreased. Interacts
FT with PIK3C3."
FT /evidence="ECO:0000269|PubMed:18425118,
FT ECO:0000269|PubMed:25869668"
FT MUTAGEN 79
FT /note="Q->L: Induces the formation of larger endosomes. No
FT effect on interaction with INPP5F. Prevents interaction
FT with DYN2 without affecting the interaction with PIK3C3."
FT /evidence="ECO:0000269|PubMed:18425118,
FT ECO:0000269|PubMed:25869668"
FT CONFLICT 13
FT /note="N -> D (in Ref. 3; BAE29485)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="Q -> R (in Ref. 3; BAB22245)"
FT /evidence="ECO:0000305"
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
