RAB31_MOUSE
ID RAB31_MOUSE Reviewed; 194 AA.
AC Q921E2; Q8BKP0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ras-related protein Rab-31;
GN Name=Rab31;
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=Spinal ganglion;
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 [2]
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 [3]
RP FUNCTION.
RX PubMed=19345684; DOI=10.1016/j.yexcr.2009.03.020;
RA Rodriguez-Gabin A.G., Yin X., Si Q., Larocca J.N.;
RT "Transport of mannose-6-phosphate receptors from the trans-Golgi network to
RT endosomes requires Rab31.";
RL Exp. Cell Res. 315:2215-2230(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, 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 [7]
RP FUNCTION, AND INTERACTION WITH EEA1 AND NGFR.
RX PubMed=22460790; DOI=10.1073/pnas.1103638109;
RA Baeza-Raja B., Li P., Le Moan N., Sachs B.D., Schachtrup C., Davalos D.,
RA Vagena E., Bridges D., Kim C., Saltiel A.R., Olefsky J.M., Akassoglou K.;
RT "p75 neurotrophin receptor regulates glucose homeostasis and insulin
RT sensitivity.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5838-5843(2012).
RN [8]
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: 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:19345684,
CC ECO:0000269|PubMed:22460790}.
CC -!- SUBUNIT: Interacts with OCRL. Interacts (in GDP-bound form) with RIN3
CC and GAPVD1, which function as guanine exchange factors (GEF). Interacts
CC with EGFR (By similarity). Interacts with NGFR. Interacts (in GTP-bound
CC form) with EEA1. Interacts (in GTP-bound form) with APPL2; interaction
CC contributes to or enhances recruitment of APPL2 to the phagosomes;
CC interaction enhances Fc-gamma receptor-mediated phagocytosis through
CC PI3K/Akt signaling in macrophages (PubMed:25568335). {ECO:0000250,
CC ECO:0000269|PubMed:22460790, ECO:0000269|PubMed:25568335}.
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 (at protein level).
CC {ECO:0000269|PubMed:19725050}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC34585.1; Type=Erroneous initiation; 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; AK051270; BAC34585.1; ALT_INIT; mRNA.
DR EMBL; BC013063; AAH13063.1; -; mRNA.
DR RefSeq; NP_598446.2; NM_133685.2.
DR AlphaFoldDB; Q921E2; -.
DR SMR; Q921E2; -.
DR BioGRID; 223081; 1.
DR IntAct; Q921E2; 10.
DR STRING; 10090.ENSMUSP00000068195; -.
DR iPTMnet; Q921E2; -.
DR PhosphoSitePlus; Q921E2; -.
DR EPD; Q921E2; -.
DR MaxQB; Q921E2; -.
DR PaxDb; Q921E2; -.
DR PRIDE; Q921E2; -.
DR ProteomicsDB; 300377; -.
DR DNASU; 106572; -.
DR GeneID; 106572; -.
DR KEGG; mmu:106572; -.
DR CTD; 11031; -.
DR MGI; MGI:1914603; Rab31.
DR eggNOG; KOG0092; Eukaryota.
DR InParanoid; Q921E2; -.
DR OMA; CMHGGKP; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; Q921E2; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 106572; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Rab31; mouse.
DR PRO; PR:Q921E2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q921E2; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0036186; C:early phagosome membrane; IDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
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; ISO:MGI.
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; IMP: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_0000121233"
FT REGION 167..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007744|PubMed:19144319"
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 49
FT /note="C -> W (in Ref. 1; BAC34585)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 21331 MW; 4EBCAF6E2431AD02 CRC64;
MAIRELKVCL LGDTGVGKSS IVCRFVQDHF DHNISPTIGA SFMTKTVPCG NELHKFLIWD
TAGQERFHSL APMYYRGSAA AVIVYDITKQ DSFHTLKKWV KELKEHGPEN IVMAIAGNKC
DLSDIREVPL KDAKEYAESI GAIVVETSAK NAINIEELFQ GISRQIPPLG PQENGNSGGI
KLGNQSLQAS RRCC
