ID   RAB6B_MOUSE             Reviewed;         208 AA.
AC   P61294;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Ras-related protein Rab-6B;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:Q9NRW1};
GN   Name=Rab6b; Synonyms=D9Bwg0185e;
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=Cerebellum;
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=C57BL/6J; TISSUE=Brain;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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   [4]
RP   INTERACTION WITH BICDL1.
RX   PubMed=20360680; DOI=10.1038/emboj.2010.51;
RA   Schlager M.A., Kapitein L.C., Grigoriev I., Burzynski G.M., Wulf P.S.,
RA   Keijzer N., de Graaff E., Fukuda M., Shepherd I.T., Akhmanova A.,
RA   Hoogenraad C.C.;
RT   "Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-related
RT   protein 1 (BICDR-1) regulates neuritogenesis.";
RL   EMBO J. 29:1637-1651(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 active GTP-bound and inactive
CC       GDP-bound states. In their active state, drive transport of vesicular
CC       carriers from donor organelles to acceptor organelles to regulate the
CC       membrane traffic that maintains organelle identity and morphology.
CC       Recruits VPS13B to the Golgi membrane. Regulates the compacted
CC       morphology of the Golgi. Seems to have a role in retrograde membrane
CC       traffic at the level of the Golgi complex. May function in retrograde
CC       transport in neuronal cells. Plays a role in neuron projection
CC       development. {ECO:0000250|UniProtKB:Q9NRW1}.
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:Q9NRW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:Q9NRW1};
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC       (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC       activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC       and GDP dissociation inhibitors which inhibit the dissociation of the
CC       nucleotide from the GTPase. {ECO:0000250|UniProtKB:Q9NRW1}.
CC   -!- SUBUNIT: Interacts (GTP-bound) with BICD1 (via C-terminus); the
CC       interaction is direct. Interacts (GDP-bound) with DYNLRB1. Interacts
CC       (GTP-bound) with APBA1/MINT1 isoform 3, also called Mint1_826.
CC       Interacts (GTP-bound) with VPS13B. {ECO:0000250|UniProtKB:Q9NRW1}.
CC   -!- INTERACTION:
CC       P61294; A0JNT9: Bicdl1; NbExp=2; IntAct=EBI-529766, EBI-7893170;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q9NRW1}; Lipid-anchor {ECO:0000305}. Endoplasmic
CC       reticulum-Golgi intermediate compartment
CC       {ECO:0000250|UniProtKB:Q9NRW1}. Cytoplasmic vesicle
CC       {ECO:0000250|UniProtKB:Q9NRW1}. Note=Colocalizes with BICD1 at
CC       vesicular structures that align along microtubules.
CC       {ECO:0000250|UniProtKB:Q9NRW1}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AK035893; BAC29230.1; -; mRNA.
DR   EMBL; BC060618; AAH60618.1; -; mRNA.
DR   CCDS; CCDS23449.1; -.
DR   RefSeq; NP_776142.1; NM_173781.4.
DR   PDB; 8IJ9; X-ray; 2.04 A; A/B=8-176.
DR   PDBsum; 8IJ9; -.
DR   AlphaFoldDB; P61294; -.
DR   SMR; P61294; -.
DR   BioGRID; 234782; 16.
DR   IntAct; P61294; 13.
DR   MINT; P61294; -.
DR   STRING; 10090.ENSMUSP00000035155; -.
DR   GlyGen; P61294; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P61294; -.
DR   PhosphoSitePlus; P61294; -.
DR   SwissPalm; P61294; -.
DR   jPOST; P61294; -.
DR   PaxDb; 10090-ENSMUSP00000035155; -.
DR   PeptideAtlas; P61294; -.
DR   ProteomicsDB; 300383; -.
DR   Pumba; P61294; -.
DR   ABCD; P61294; 21 sequenced antibodies.
DR   Antibodypedia; 46687; 197 antibodies from 24 providers.
DR   DNASU; 270192; -.
DR   Ensembl; ENSMUST00000035155.8; ENSMUSP00000035155.7; ENSMUSG00000032549.8.
DR   GeneID; 270192; -.
DR   KEGG; mmu:270192; -.
DR   UCSC; uc009rgf.1; mouse.
DR   AGR; MGI:107283; -.
DR   CTD; 51560; -.
DR   MGI; MGI:107283; Rab6b.
DR   VEuPathDB; HostDB:ENSMUSG00000032549; -.
DR   eggNOG; KOG0094; Eukaryota.
DR   GeneTree; ENSGT00940000159656; -.
DR   HOGENOM; CLU_041217_10_2_1; -.
DR   InParanoid; P61294; -.
DR   OMA; TRFVYDH; -.
DR   OrthoDB; 5483572at2759; -.
DR   PhylomeDB; P61294; -.
DR   TreeFam; TF300803; -.
DR   Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
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; 270192; 0 hits in 76 CRISPR screens.
DR   ChiTaRS; Rab6b; mouse.
DR   PRO; PR:P61294; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P61294; Protein.
DR   Bgee; ENSMUSG00000032549; Expressed in substantia nigra and 223 other cell types or tissues.
DR   ExpressionAtlas; P61294; baseline and differential.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0098793; C:presynapse; ISO:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR   GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:1903292; P:protein localization to Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR   CDD; cd01861; Rab6; 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:SF66; RAS-RELATED PROTEIN RAB-6B 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.
DR   Genevisible; P61294; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..208
FT                   /note="Ras-related protein Rab-6B"
FT                   /id="PRO_0000121116"
FT   MOTIF           42..50
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         20..27
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         68..72
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         126..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         208
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           206
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           208
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   STRAND          11..19
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   HELIX           26..35
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   STRAND          47..57
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   STRAND          60..69
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   HELIX           73..78
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   HELIX           79..84
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   STRAND          87..94
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   HELIX           98..102
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   HELIX           104..115
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   STRAND          118..126
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   HELIX           138..147
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   STRAND          151..154
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   TURN            157..159
FT                   /evidence="ECO:0007829|PDB:8IJ9"
FT   HELIX           163..173
FT                   /evidence="ECO:0007829|PDB:8IJ9"
SQ   SEQUENCE   208 AA;  23462 MW;  E81C831996E2446D CRC64;
     MSAGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR
     TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNLNS FQQTSKWIDD VRTERGSDVI
     IMLVGNKTDL ADKRQITIEE GEQRAKELSV MFIETSAKTG YNVKQLFRRV ASALPGMENV
     QEKSKEGMID IKLDKPQEPP ASEGGCSC
//