RAB7B_MOUSE
ID RAB7B_MOUSE Reviewed; 199 AA.
AC Q8VEA8; Q0PD09; Q8BJT0; Q8BZB1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ras-related protein Rab-7b;
GN Name=Rab7b;
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 [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=16923123; DOI=10.1111/j.1365-2443.2006.00997.x;
RA Itoh T., Satoh M., Kanno E., Fukuda M.;
RT "Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing
RT proteins based on their Rab-binding activity.";
RL Genes Cells 11:1023-1037(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Blood vessel, Cerebellum, and Head;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17395780; DOI=10.1182/blood-2007-01-066027;
RA Wang Y., Chen T., Han C., He D., Liu H., An H., Cai Z., Cao X.;
RT "Lysosome-associated small Rab GTPase Rab7b negatively regulates TLR4
RT signaling in macrophages by promoting lysosomal degradation of TLR4.";
RL Blood 110:962-971(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, 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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19587007; DOI=10.4049/jimmunol.0900249;
RA Yao M., Liu X., Li D., Chen T., Cai Z., Cao X.;
RT "Late endosome/lysosome-localized Rab7b suppresses TLR9-initiated
RT proinflammatory cytokine and type I IFN production in macrophages.";
RL J. Immunol. 183:1751-1758(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Controls vesicular trafficking from endosomes to the trans-
CC Golgi network (TGN). Acts as a negative regulator of TLR9 signaling and
CC can suppress TLR9-triggered TNFA, IL6, and IFNB production in
CC macrophages by promoting TLR9 lysosomal degradation. Also negatively
CC regulates TLR4 signaling in macrophages by promoting lysosomal
CC degradation of TLR4. Promotes megakaryocytic differentiation by
CC increasing NF-kappa-B-dependent IL6 production and subsequently
CC enhancing the association of STAT3 with GATA1. Not involved in the
CC regulation of the EGF- and EGFR degradation pathway.
CC {ECO:0000269|PubMed:17395780, ECO:0000269|PubMed:19587007}.
CC -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:19587007}.
CC Lysosome {ECO:0000269|PubMed:17395780, ECO:0000269|PubMed:19587007}.
CC Golgi apparatus {ECO:0000250|UniProtKB:Q96AH8}. Golgi apparatus, trans-
CC Golgi network {ECO:0000250|UniProtKB:Q96AH8}. Cytoplasmic vesicle,
CC phagosome {ECO:0000250|UniProtKB:Q96AH8}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305};
CC Cytoplasmic side {ECO:0000305}. Note=Recruited to phagosomes containing
CC S.aureus or Mycobacterium. {ECO:0000250|UniProtKB:Q96AH8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VEA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VEA8-2; Sequence=VSP_011108;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AB232641; BAF02903.1; -; mRNA.
DR EMBL; AK030688; BAC27078.1; -; mRNA.
DR EMBL; AK036056; BAC29291.1; -; mRNA.
DR EMBL; AK079999; BAC37802.1; -; mRNA.
DR EMBL; CH466520; EDL39704.1; -; Genomic_DNA.
DR CCDS; CCDS15272.1; -. [Q8VEA8-1]
DR CCDS; CCDS78677.1; -. [Q8VEA8-2]
DR RefSeq; NP_001298025.1; NM_001311096.1. [Q8VEA8-2]
DR RefSeq; NP_663484.1; NM_145509.3. [Q8VEA8-1]
DR RefSeq; XP_006529493.1; XM_006529430.2. [Q8VEA8-1]
DR AlphaFoldDB; Q8VEA8; -.
DR SMR; Q8VEA8; -.
DR BioGRID; 230511; 1.
DR STRING; 10090.ENSMUSP00000065456; -.
DR iPTMnet; Q8VEA8; -.
DR PhosphoSitePlus; Q8VEA8; -.
DR SwissPalm; Q8VEA8; -.
DR jPOST; Q8VEA8; -.
DR MaxQB; Q8VEA8; -.
DR PaxDb; Q8VEA8; -.
DR PRIDE; Q8VEA8; -.
DR ProteomicsDB; 253152; -. [Q8VEA8-1]
DR ProteomicsDB; 253153; -. [Q8VEA8-2]
DR Antibodypedia; 72889; 143 antibodies from 19 providers.
DR DNASU; 226421; -.
DR Ensembl; ENSMUST00000064664; ENSMUSP00000066452; ENSMUSG00000052688. [Q8VEA8-2]
DR Ensembl; ENSMUST00000064679; ENSMUSP00000065456; ENSMUSG00000052688. [Q8VEA8-1]
DR GeneID; 226421; -.
DR KEGG; mmu:226421; -.
DR UCSC; uc007cnp.1; mouse. [Q8VEA8-1]
DR CTD; 338382; -.
DR MGI; MGI:2442295; Rab7b.
DR VEuPathDB; HostDB:ENSMUSG00000052688; -.
DR eggNOG; KOG0394; Eukaryota.
DR GeneTree; ENSGT00940000161943; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; Q8VEA8; -.
DR OMA; ASSWCKE; -.
DR OrthoDB; 1172019at2759; -.
DR PhylomeDB; Q8VEA8; -.
DR TreeFam; TF326442; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 226421; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Rab7b; mouse.
DR PRO; PR:Q8VEA8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VEA8; protein.
DR Bgee; ENSMUSG00000052688; Expressed in stroma of bone marrow and 172 other tissues.
DR ExpressionAtlas; Q8VEA8; baseline and differential.
DR Genevisible; Q8VEA8; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0034499; P:late endosome to Golgi transport; ISS:UniProtKB.
DR GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; IMP:UniProtKB.
DR GO; GO:0034164; P:negative regulation of toll-like receptor 9 signaling pathway; IMP:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; IBA:GO_Central.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Alternative splicing; Cytoplasmic vesicle; Endosome; Golgi apparatus;
KW GTP-binding; Lipoprotein; Lysosome; Membrane; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..199
FT /note="Ras-related protein Rab-7b"
FT /id="PRO_0000121126"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 34..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 154..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT LIPID 198
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 199
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 133..174
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011108"
FT CONFLICT 187
FT /note="I -> V (in Ref. 2; BAC29291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 22502 MW; 33353842079CF6FC CRC64;
MNPRKKVDLK LIIVGALGVG KTSLLHQYVH KTFFEEYQTT LGASILSKII ILDDTTLKLQ
IWDTGGQERF RSMVSTFYKG SDGCILAFDV TDPESFEALD IWRDDVLAKI IPMEQSYPMV
VLGNKIDLED RKVSQEVVHG WCKEKDMPYF EVSAKNDINV VQAFEVLASR ALLRYQGTAE
NHLIDSIKLS PGQPKSRCC
