RAB35_MOUSE
ID RAB35_MOUSE Reviewed; 201 AA.
AC Q6PHN9;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Ras-related protein Rab-35;
GN Name=Rab35;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP PROTEIN SEQUENCE OF 11-21; 59-69 AND 129-137, 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 [3]
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 [4]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH DENND1A, AND MUTAGENESIS OF
RP SER-22 AND GLN-67.
RX PubMed=20159556; DOI=10.1016/j.molcel.2009.12.037;
RA Allaire P.D., Marat A.L., Dall'Armi C., Di Paolo G., McPherson P.S.,
RA Ritter B.;
RT "The Connecdenn DENN domain: a GEF for Rab35 mediating cargo-specific exit
RT from early endosomes.";
RL Mol. Cell 37:370-382(2010).
RN [5]
RP FUNCTION.
RX PubMed=22762500; DOI=10.1111/j.1600-0854.2012.01397.x;
RA Davey J.R., Humphrey S.J., Junutula J.R., Mishra A.K., Lambright D.G.,
RA James D.E., Stoeckli J.;
RT "TBC1D13 is a RAB35 specific GAP that plays an important role in GLUT4
RT trafficking in adipocytes.";
RL Traffic 13:1429-1441(2012).
RN [6]
RP FUNCTION IN NEURITE OUTGROWTH, INTERACTION WITH ACAP2; EHD1 AND MICALL1,
RP AND MUTAGENESIS OF SER-22.
RX PubMed=23572513; DOI=10.1242/jcs.117846;
RA Kobayashi H., Fukuda M.;
RT "Rab35 establishes the EHD1-association site by coordinating two distinct
RT effectors during neurite outgrowth.";
RL J. Cell Sci. 126:2424-2435(2013).
RN [7]
RP INTERACTION WITH DENND1B, AND ACTIVITY REGULATION.
RX PubMed=26774822; DOI=10.1016/j.cell.2015.11.052;
RA Yang C.W., Hojer C.D., Zhou M., Wu X., Wuster A., Lee W.P., Yaspan B.L.,
RA Chan A.C.;
RT "Regulation of T cell receptor signaling by DENND1B in TH2 cells and
RT allergic disease.";
RL Cell 164:141-155(2016).
RN [8]
RP PHOSPHORYLATION AT THR-72.
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).
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 sets of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. That Rab is involved in the
CC process of endocytosis and is an essential rate-limiting regulator of
CC the fast recycling pathway back to the plasma membrane. During
CC cytokinesis, required for the postfurrowing terminal steps, namely for
CC intercellular bridge stability and abscission, possibly by controlling
CC phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at
CC the intercellular bridge. May indirectly regulate neurite outgrowth.
CC Together with TBC1D13 may be involved in regulation of insulin-induced
CC glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane
CC in adipocytes. {ECO:0000269|PubMed:20159556,
CC ECO:0000269|PubMed:22762500, ECO:0000269|PubMed:23572513}.
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP) (By similarity).
CC That Rab is activated by the guanine exchange factors DENND1A, DENND1B
CC and DENND1C (PubMed:20159556, PubMed:26774822).
CC {ECO:0000250|UniProtKB:Q15286, ECO:0000269|PubMed:20159556,
CC ECO:0000269|PubMed:26774822}.
CC -!- SUBUNIT: Interacts with DENND1A and DENND1B; in a nucleotide-dependent
CC manner (PubMed:20159556, PubMed:26774822). Interacts with DENND1C; weak
CC interaction which is nucleotide-independent (By similarity). Interacts
CC (GTP-bound form) with ACAP2 and MICALL1; the interaction is direct and
CC probably recruits ACAP2 and MICALL1 to membranes (PubMed:23572513).
CC Interacts with EHD1; the interaction is indirect through MICALL1 and
CC probably recruits EHD1 to membranes (PubMed:23572513). Interacts with
CC GDI1, GDI2, CHM and CHML; phosphorylation at Thr-72 disrupts these
CC interactions (By similarity). {ECO:0000250|UniProtKB:Q15286,
CC ECO:0000269|PubMed:20159556, ECO:0000269|PubMed:23572513,
CC ECO:0000269|PubMed:26774822}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15286};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Membrane,
CC clathrin-coated pit {ECO:0000250|UniProtKB:Q15286}. Cytoplasmic
CC vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q15286}.
CC Endosome {ECO:0000250|UniProtKB:Q15286}. Melanosome
CC {ECO:0000250|UniProtKB:Q15286}. Note=Present on sorting endosomes and
CC recycling endosome tubules. Tends to be enriched in PIP2-positive cell
CC membrane domains. During mitosis, associated with the plasma membrane
CC and present at the ingressing furrow during early cytokinesis as well
CC as at the intercellular bridge later during cytokinesis. Identified in
CC stage I to stage IV melanosomes. {ECO:0000250|UniProtKB:Q15286}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BC056466; AAH56466.1; -; mRNA.
DR CCDS; CCDS19596.1; -.
DR RefSeq; NP_937806.1; NM_198163.1.
DR AlphaFoldDB; Q6PHN9; -.
DR SMR; Q6PHN9; -.
DR BioGRID; 218674; 8.
DR DIP; DIP-38238N; -.
DR IntAct; Q6PHN9; 19.
DR MINT; Q6PHN9; -.
DR STRING; 10090.ENSMUSP00000031492; -.
DR ChEMBL; CHEMBL4523349; -.
DR iPTMnet; Q6PHN9; -.
DR PhosphoSitePlus; Q6PHN9; -.
DR SwissPalm; Q6PHN9; -.
DR EPD; Q6PHN9; -.
DR jPOST; Q6PHN9; -.
DR MaxQB; Q6PHN9; -.
DR PaxDb; Q6PHN9; -.
DR PRIDE; Q6PHN9; -.
DR ProteomicsDB; 255065; -.
DR Antibodypedia; 45490; 308 antibodies from 32 providers.
DR DNASU; 77407; -.
DR Ensembl; ENSMUST00000031492; ENSMUSP00000031492; ENSMUSG00000029518.
DR GeneID; 77407; -.
DR KEGG; mmu:77407; -.
DR UCSC; uc008zei.1; mouse.
DR CTD; 11021; -.
DR MGI; MGI:1924657; Rab35.
DR VEuPathDB; HostDB:ENSMUSG00000029518; -.
DR eggNOG; KOG0079; Eukaryota.
DR GeneTree; ENSGT00940000158557; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q6PHN9; -.
DR OMA; FMAITRQ; -.
DR OrthoDB; 1149105at2759; -.
DR PhylomeDB; Q6PHN9; -.
DR TreeFam; TF105954; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 77407; 12 hits in 72 CRISPR screens.
DR ChiTaRS; Rab35; mouse.
DR PRO; PR:Q6PHN9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6PHN9; protein.
DR Bgee; ENSMUSG00000029518; Expressed in granulocyte and 63 other tissues.
DR ExpressionAtlas; Q6PHN9; baseline and differential.
DR Genevisible; Q6PHN9; MM.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0031253; C:cell projection membrane; ISO:MGI.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; ISO:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:MGI.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0048227; P:plasma membrane to endosome transport; ISO:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0036010; P:protein localization to endosome; ISS: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:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04110; Rab35; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041815; Rab35.
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; Coated pit; Cytoplasmic vesicle; Direct protein sequencing;
KW Endosome; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..201
FT /note="Ras-related protein Rab-35"
FT /id="PRO_0000121246"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 150..152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 72
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29125462"
FT MOD_RES 75
FT /note="O-(2-cholinephosphoryl)serine"
FT /evidence="ECO:0000250|UniProtKB:Q15286"
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 22
FT /note="S->N: Loss of interaction with MICALL1."
FT /evidence="ECO:0000269|PubMed:20159556,
FT ECO:0000269|PubMed:23572513"
FT MUTAGEN 67
FT /note="Q->L: Loss of GTPase activity. Increased fast
FT recycling."
FT /evidence="ECO:0000269|PubMed:20159556"
SQ SEQUENCE 201 AA; 23025 MW; 31EB15D6D42E076E CRC64;
MARDYDHLFK LLIIGDSGVG KSSLLLRFAD NTFSGSYITT IGVDFKIRTV EINGEKVKLQ
IWDTAGQERF RTITSTYYRG THGVIVVYDV TSAESFVNVK RWLHEINQNC DDVCRILVGN
KNDDPERKVV ETEDAYKFAG QMGIQLFETS AKENVNVEEM FNCITELVLR AKKDNLAKQQ
QQQQNDVVKL TKNSKRKKRC C
