ID   RAB31_MOUSE             Reviewed;         195 AA.
AC   Q921E2; Q8BKP0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2024, sequence version 2.
DT   27-MAR-2024, entry version 157.
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-36, 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=AAH13063.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK051270; BAC34585.1; -; mRNA.
DR   EMBL; BC013063; AAH13063.1; ALT_INIT; 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   SwissPalm; Q921E2; -.
DR   EPD; Q921E2; -.
DR   MaxQB; Q921E2; -.
DR   PaxDb; 10090-ENSMUSP00000068195; -.
DR   ProteomicsDB; 300377; -.
DR   Pumba; Q921E2; -.
DR   DNASU; 106572; -.
DR   Ensembl; ENSMUST00000070673.9; ENSMUSP00000068195.8; ENSMUSG00000056515.10.
DR   GeneID; 106572; -.
DR   KEGG; mmu:106572; -.
DR   AGR; MGI:1914603; -.
DR   CTD; 11031; -.
DR   MGI; MGI:1914603; Rab31.
DR   eggNOG; KOG0092; Eukaryota.
DR   GeneTree; ENSGT00940000155702; -.
DR   InParanoid; Q921E2; -.
DR   OMA; KQDTFHT; -.
DR   OrthoDB; 5483572at2759; -.
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 78 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:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0001891; C:phagocytic cup; IDA: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; 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   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_0000121233"
FT   REGION          168..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007744|PubMed:19144319"
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        50
FT                   /note="C -> W (in Ref. 1; BAC34585)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   195 AA;  21463 MW;  D7E3AFC1EDA7ADAD CRC64;
     MMAIRELKVC LLGDTGVGKS SIVCRFVQDH FDHNISPTIG ASFMTKTVPC GNELHKFLIW
     DTAGQERFHS LAPMYYRGSA AAVIVYDITK QDSFHTLKKW VKELKEHGPE NIVMAIAGNK
     CDLSDIREVP LKDAKEYAES IGAIVVETSA KNAINIEELF QGISRQIPPL GPQENGNSGG
     IKLGNQSLQA SRRCC
//