ID   RAB31_RAT               Reviewed;         195 AA.
AC   Q6GQP4; Q9JK74;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2024, sequence version 3.
DT   27-MAR-2024, entry version 130.
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=AAF67746.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF254800; AAF67746.1; ALT_INIT; mRNA.
DR   EMBL; BC072698; AAH72698.1; -; mRNA.
DR   RefSeq; NP_659562.2; NM_145094.2.
DR   AlphaFoldDB; Q6GQP4; -.
DR   SMR; Q6GQP4; -.
DR   IntAct; Q6GQP4; 1.
DR   STRING; 10116.ENSRNOP00000063486; -.
DR   PhosphoSitePlus; Q6GQP4; -.
DR   jPOST; Q6GQP4; -.
DR   PaxDb; 10116-ENSRNOP00000063486; -.
DR   Ensembl; ENSRNOT00000109162.1; ENSRNOP00000076689.1; ENSRNOG00000042189.3.
DR   GeneID; 246324; -.
DR   KEGG; rno:246324; -.
DR   AGR; RGD:628598; -.
DR   CTD; 11031; -.
DR   RGD; 628598; Rab31.
DR   eggNOG; KOG0092; Eukaryota.
DR   GeneTree; ENSGT00940000155702; -.
DR   InParanoid; Q6GQP4; -.
DR   OMA; KQDTFHT; -.
DR   OrthoDB; 5483572at2759; -.
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:0012505; C:endomembrane system; IBA:GO_Central.
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   CDD; cd01860; Rab5_related; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47977; RAS-RELATED PROTEIN RAB; 1.
DR   PANTHER; PTHR47977:SF13; RAS-RELATED PROTEIN RAB-31 ISOFORM X1; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..195
FT                   /note="Ras-related protein Rab-31"
FT                   /id="PRO_0000121234"
FT   MOTIF           35..43
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         13..20
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         61..65
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         119..122
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13636"
FT   LIPID           194
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           195
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        107
FT                   /note="H -> Y (in Ref. 1; AAF67746)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   195 AA;  21500 MW;  4DD39CC72DD162AA CRC64;
     MMAIRELKVC LLGDTGVGKS SIVCRFVQDH FDHNISPTIG ASFMTKTVPC GNELHKFLIW
     DTAGQERFHS LAPMYYRGSA AAVIVYDITK QDSFHTLKKW VKELKEHGPE NIVMAIAGNK
     CDLSDIREVP LKDAKEYAES IGALVVETSA KNAINIEELF QGISRQIPPL DPHENGNSGG
     IKLGNQSLQA GRRCC
//