ID   RAB5B_MOUSE             Reviewed;         215 AA.
AC   P61021; P35239; P35277;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Ras-related protein Rab-5B;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P20339};
GN   Name=Rab5b;
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], AND SUBCELLULAR LOCATION.
RC   TISSUE=Kidney;
RX   PubMed=7789520; DOI=10.1016/0014-5793(95)00477-q;
RA   Bucci C., Lutcke A., Steele Mortimer O., Olkkonen V.M., Dupree P.,
RA   Chiariello M., Bruni C.B., Simons K., Zerial M.;
RT   "Co-operative regulation of endocytosis by three Rab5 isoforms.";
RL   FEBS Lett. 366:65-71(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpus striatum;
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 [MRNA] OF 32-80.
RC   TISSUE=Kidney;
RX   PubMed=1555775; DOI=10.1016/0378-1119(92)90387-5;
RA   Chavrier P., Simons K., Zerial M.;
RT   "The complexity of the Rab and Rho GTP-binding protein subfamilies revealed
RT   by a PCR cloning approach.";
RL   Gene 112:261-264(1992).
RN   [4]
RP   PROTEIN SEQUENCE OF 82-110, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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).
CC   -!- FUNCTION: Protein transport (By similarity). Probably involved in
CC       vesicular traffic (By similarity). {ECO:0000250|UniProtKB:P20339}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:P20339};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P20339};
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC       (GEFs) which promote the exchange of bound GDP for free GTP.
CC       {ECO:0000250|UniProtKB:P18066}.
CC   -!- SUBUNIT: Binds EEA1. Interacts with RIN2 and RIN3, which probably
CC       regulate its pathway, possibly by acting as GEFs (By similarity).
CC       Interacts with GDI1, GDI2, CHML and CHM; phosphorylation at Ser-84
CC       disrupts this interaction (By similarity).
CC       {ECO:0000250|UniProtKB:P61020}.
CC   -!- INTERACTION:
CC       P61021; Q5S007: LRRK2; Xeno; NbExp=2; IntAct=EBI-8320093, EBI-5323863;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P61020};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P61020}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P61020}. Early endosome membrane
CC       {ECO:0000305|PubMed:7789520}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P61020}. Melanosome
CC       {ECO:0000250|UniProtKB:P61020}.
CC   -!- PTM: Phosphorylation of Ser-84 in the switch II region by LRRK2
CC       prevents the association of RAB regulatory proteins, including CHM,
CC       CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.
CC       {ECO:0000250|UniProtKB:P61020}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; X84239; CAA59016.1; -; mRNA.
DR   EMBL; AK081251; BAC38176.1; -; mRNA.
DR   EMBL; M79311; AAK14835.1; -; mRNA.
DR   CCDS; CCDS24287.1; -.
DR   PIR; JH0640; JH0640.
DR   PIR; S65932; S65932.
DR   RefSeq; NP_803130.1; NM_177411.4.
DR   RefSeq; XP_006513447.1; XM_006513384.3.
DR   AlphaFoldDB; P61021; -.
DR   SMR; P61021; -.
DR   BioGRID; 202548; 25.
DR   IntAct; P61021; 26.
DR   STRING; 10090.ENSMUSP00000000727; -.
DR   GlyGen; P61021; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P61021; -.
DR   PhosphoSitePlus; P61021; -.
DR   SwissPalm; P61021; -.
DR   EPD; P61021; -.
DR   jPOST; P61021; -.
DR   MaxQB; P61021; -.
DR   PaxDb; 10090-ENSMUSP00000000727; -.
DR   ProteomicsDB; 300382; -.
DR   Pumba; P61021; -.
DR   Antibodypedia; 4131; 197 antibodies from 33 providers.
DR   DNASU; 19344; -.
DR   Ensembl; ENSMUST00000000727.4; ENSMUSP00000000727.3; ENSMUSG00000000711.4.
DR   GeneID; 19344; -.
DR   KEGG; mmu:19344; -.
DR   UCSC; uc007hnv.2; mouse.
DR   AGR; MGI:105938; -.
DR   CTD; 5869; -.
DR   MGI; MGI:105938; Rab5b.
DR   VEuPathDB; HostDB:ENSMUSG00000000711; -.
DR   eggNOG; KOG0092; Eukaryota.
DR   GeneTree; ENSGT00940000160756; -.
DR   HOGENOM; CLU_041217_10_2_1; -.
DR   InParanoid; P61021; -.
DR   OMA; DEEGLMW; -.
DR   OrthoDB; 5483572at2759; -.
DR   PhylomeDB; P61021; -.
DR   TreeFam; TF300199; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR   Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   BioGRID-ORCS; 19344; 1 hit in 75 CRISPR screens.
DR   ChiTaRS; Rab5b; mouse.
DR   PRO; PR:P61021; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P61021; Protein.
DR   Bgee; ENSMUSG00000000711; Expressed in granulocyte and 183 other cell types or tissues.
DR   ExpressionAtlas; P61021; baseline and differential.
DR   GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
DR   GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR   GO; GO:0019882; P:antigen processing and presentation; ISO:MGI.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0007032; P:endosome organization; IDA:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0048227; P:plasma membrane to endosome transport; ISO:MGI.
DR   GO; GO:0030100; P:regulation of endocytosis; IDA:MGI.
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; PTHR47978; -; 1.
DR   PANTHER; PTHR47978:SF65; RAB43, MEMBER RAS ONCOGENE FAMILY; 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.
DR   Genevisible; P61021; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Direct protein sequencing; Endosome;
KW   GTP-binding; Hydrolase; Lipoprotein; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P61020"
FT   CHAIN           2..215
FT                   /note="Ras-related protein Rab-5B"
FT                   /id="PRO_0000121108"
FT   REGION          186..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           49..57
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        200..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         27..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         46..52
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         75..79
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         133..136
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         163..165
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P61020"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61020"
FT   LIPID           212
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   LIPID           213
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   CONFLICT        56
FT                   /note="A -> G (in Ref. 3; AAK14835)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   215 AA;  23707 MW;  D47AD834BCF8B591 CRC64;
     MTSRSTARPN GQPQASKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEYQE STIGAAFLTQ
     SVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNQETFAR AKTWVKELQR
     QASPSIVIAL AGNKADLANK RMVEYEEAQA YADDNSLLFM ETSAKTAMNV NDLFLAIAKK
     LPKSEPQNLG GAAGRSRGVD LHEQSQQNKS QCCSN
//