RAB35_RAT
ID RAB35_RAT Reviewed; 201 AA.
AC Q5U316;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ras-related protein Rab-35;
GN Name=Rab35;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 INTERACTION WITH ACAP2; EHD1 AND MICALL1, AND SUBCELLULAR LOCATION.
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).
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 (By similarity). {ECO:0000250|UniProtKB:Q15286,
CC ECO:0000250|UniProtKB:Q6PHN9}.
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). That Rab is
CC activated by the guanine exchange factors DENND1A, DENND1B and DENND1C
CC (By similarity). {ECO:0000250|UniProtKB:Q15286}.
CC -!- SUBUNIT: Interacts with DENND1A and DENND1B; in a nucleotide-dependent
CC manner. Interacts with DENND1C; weak interaction which is nucleotide-
CC independent (By similarity). Interacts (GTP-bound form) with ACAP2 and
CC MICALL1; the interaction is direct and probably recruits ACAP2 and
CC MICALL1 to membranes (PubMed:23572513). Interacts with EHD1; the
CC interaction is indirect through MICALL1 and probably recruits EHD1 to
CC membranes (By similarity). Interacts with GDI1, GDI2 and CHM;
CC phosphorylation at Thr-72 disrupts these interactions (By similarity).
CC {ECO:0000250|UniProtKB:Q15286, ECO:0000269|PubMed:23572513}.
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:0000269|PubMed:23572513}. 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; BC085769; AAH85769.1; -; mRNA.
DR RefSeq; NP_001013064.1; NM_001013046.1.
DR AlphaFoldDB; Q5U316; -.
DR SMR; Q5U316; -.
DR STRING; 10116.ENSRNOP00000029070; -.
DR iPTMnet; Q5U316; -.
DR PhosphoSitePlus; Q5U316; -.
DR jPOST; Q5U316; -.
DR PaxDb; Q5U316; -.
DR PRIDE; Q5U316; -.
DR GeneID; 288700; -.
DR KEGG; rno:288700; -.
DR UCSC; RGD:1306362; rat.
DR CTD; 11021; -.
DR RGD; 1306362; Rab35.
DR VEuPathDB; HostDB:ENSRNOG00000022014; -.
DR eggNOG; KOG0079; Eukaryota.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q5U316; -.
DR OMA; FMAITRQ; -.
DR OrthoDB; 1149105at2759; -.
DR PhylomeDB; Q5U316; -.
DR TreeFam; TF105954; -.
DR Reactome; R-RNO-8854214; TBC/RABGAPs.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:Q5U316; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000022014; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5U316; RN.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO-UCL.
DR GO; GO:0031253; C:cell projection membrane; ISO:RGD.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; ISO:RGD.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA: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:RGD.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0048227; P:plasma membrane to endosome transport; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0036010; P:protein localization to endosome; 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: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; Endosome; GTP-binding;
KW Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..201
FT /note="Ras-related protein Rab-35"
FT /id="PRO_0000121247"
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"
FT /evidence="ECO:0000250|UniProtKB:Q15286"
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"
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
