RAB31_RAT
ID RAB31_RAT Reviewed; 194 AA.
AC Q6GQP4; Q9JK74;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ras-related protein Rab-31;
DE AltName: Full=GTP-binding protein Rab0;
GN Name=Rab31;
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 [MRNA].
RA Rodriguez-Gabin A.G., Cammer M., Almazan G., Charron M.J., Larocca J.N.;
RT "Visualization in living cells of formation and transport of vesicles:
RT participation of Rab0, an oligodendrocyte protein.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3]
RP FUNCTION.
RX PubMed=11746448; DOI=10.1002/jnr.1253;
RA Rodriguez-Gabin A.G., Cammer M., Almazan G., Charron M., Larocca J.N.;
RT "Role of rRAB22b, an oligodendrocyte protein, in regulation of transport of
RT vesicles from trans Golgi to endocytic compartments.";
RL J. Neurosci. Res. 66:1149-1160(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17678623; DOI=10.1016/j.bbrc.2007.07.076;
RA Ng E.L., Wang Y., Tang B.L.;
RT "Rab22B's role in trans-Golgi network membrane dynamics.";
RL Biochem. Biophys. Res. Commun. 361:751-757(2007).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=19725050; DOI=10.1002/jcp.21911;
RA Ng E.L., Ng J.J., Liang F., Tang B.L.;
RT "Rab22B is expressed in the CNS astroglia lineage and plays a role in
RT epidermal growth factor receptor trafficking in A431 cells.";
RL J. Cell. Physiol. 221:716-728(2009).
RN [6]
RP FUNCTION, AND INTERACTION WITH OCRL.
RX PubMed=19795375; DOI=10.1002/jnr.22236;
RA Rodriguez-Gabin A.G., Ortiz E., Demoliner K., Si Q., Almazan G.,
RA Larocca J.N.;
RT "Interaction of Rab31 and OCRL-1 in oligodendrocytes: its role in transport
RT of mannose 6-phosphate receptors.";
RL J. Neurosci. Res. 88:589-604(2010).
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. Required for the integrity
CC and for normal function of the Golgi apparatus and the trans-Golgi
CC network. Plays a role in insulin-stimulated translocation of GLUT4 to
CC the cell membrane. Plays a role in the maturation of phagosomes that
CC engulf pathogens, such as S.aureus and Mycobacterium (By similarity).
CC Plays a role in M6PR transport from the trans-Golgi network to
CC endosomes. Plays a role in the internalization of EGFR from the cell
CC membrane into endosomes. {ECO:0000250, ECO:0000269|PubMed:11746448,
CC ECO:0000269|PubMed:19795375}.
CC -!- SUBUNIT: Interacts (in GDP-bound form) with RIN3 and GAPVD1, which
CC function as guanine exchange factors (GEF). Interacts (in GTP-bound
CC form) with EEA1. Interacts with NGFR. Interacts with EGFR (By
CC similarity). Interacts with OCRL. Interacts (in GTP-bound form) with
CC APPL2; interaction contributes to or enhances recruitment of APPL2 to
CC the phagosomes; interaction enhances Fc-gamma receptor-mediated
CC phagocytosis through PI3K/Akt signaling in macrophages (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q921E2,
CC ECO:0000269|PubMed:19795375}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q13636}.
CC Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q13636}.
CC Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Lipid-
CC anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic
CC vesicle, phagosome {ECO:0000250|UniProtKB:Q13636}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305};
CC Cytoplasmic side {ECO:0000305}. Note=Rapidly recruited to phagosomes
CC containing S.aureus or M.tuberculosis. {ECO:0000250|UniProtKB:Q13636}.
CC -!- TISSUE SPECIFICITY: Detected in brain astrocytes, spleen and intestine
CC (at protein level). {ECO:0000269|PubMed:17678623,
CC ECO:0000269|PubMed:19725050}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72698.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF254800; AAF67746.1; -; mRNA.
DR EMBL; BC072698; AAH72698.1; ALT_INIT; mRNA.
DR RefSeq; NP_659562.2; NM_145094.2.
DR AlphaFoldDB; Q6GQP4; -.
DR SMR; Q6GQP4; -.
DR IntAct; Q6GQP4; 1.
DR STRING; 10116.ENSRNOP00000063486; -.
DR jPOST; Q6GQP4; -.
DR PaxDb; Q6GQP4; -.
DR PRIDE; Q6GQP4; -.
DR GeneID; 246324; -.
DR KEGG; rno:246324; -.
DR CTD; 11031; -.
DR RGD; 628598; Rab31.
DR eggNOG; KOG0092; Eukaryota.
DR InParanoid; Q6GQP4; -.
DR OMA; CMHGGKP; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; Q6GQP4; -.
DR TreeFam; TF331262; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:Q6GQP4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0036186; C:early phagosome membrane; ISS:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0048193; P:Golgi vesicle transport; IMP:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0090382; P:phagosome maturation; ISS:UniProtKB.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; ISS: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 Cytoplasmic vesicle; Endosome; Golgi apparatus; GTP-binding; Lipoprotein;
KW Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Reference proteome.
FT CHAIN 1..194
FT /note="Ras-related protein Rab-31"
FT /id="PRO_0000121234"
FT MOTIF 34..42
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13636"
FT LIPID 193
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 194
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 106
FT /note="H -> Y (in Ref. 1; AAF67746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 21368 MW; D48C9C68E4476205 CRC64;
MAIRELKVCL LGDTGVGKSS IVCRFVQDHF DHNISPTIGA SFMTKTVPCG NELHKFLIWD
TAGQERFHSL APMYYRGSAA AVIVYDITKQ DSFHTLKKWV KELKEHGPEN IVMAIAGNKC
DLSDIREVPL KDAKEYAESI GALVVETSAK NAINIEELFQ GISRQIPPLD PHENGNSGGI
KLGNQSLQAG RRCC
