RB33B_MOUSE
ID RB33B_MOUSE Reviewed; 229 AA.
AC O35963; Q3TWI8;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Ras-related protein Rab-33B;
GN Name=Rab33b;
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 [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=9512502; DOI=10.1242/jcs.111.8.1061;
RA Zheng J.Y., Koda T., Fujiwara T., Kishi M., Ikehara Y., Kakinuma M.;
RT "A novel Rab GTPase, Rab33B, is ubiquitously expressed and localized to the
RT medial Golgi cisternae.";
RL J. Cell Sci. 111:1061-1069(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, Liver, and Thymus;
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 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 [4]
RP PROTEIN SEQUENCE OF 84-94, 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 FUNCTION, INTERACTION WITH ATG16L1, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF THR-47 AND GLN-92.
RX PubMed=18448665; DOI=10.1091/mbc.e07-12-1231;
RA Itoh T., Fujita N., Kanno E., Yamamoto A., Yoshimori T., Fukuda M.;
RT "Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates
RT autophagosome formation.";
RL Mol. Biol. Cell 19:2916-2925(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
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 X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 30-202 IN COMPLEX WITH GTP
RP ANALOG.
RX PubMed=16034420; DOI=10.1038/nature03798;
RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.";
RL Nature 436:415-419(2005).
RN [8]
RP INTERACTION WITH ATG16L2.
RX PubMed=22082872; DOI=10.4161/auto.7.12.18025;
RA Ishibashi K., Fujita N., Kanno E., Omori H., Yoshimori T., Itoh T.,
RA Fukuda M.;
RT "Atg16L2, a novel isoform of mammalian Atg16L that is not essential for
RT canonical autophagy despite forming an Atg12-5-16L2 complex.";
RL Autophagy 7:1500-1513(2011).
CC -!- FUNCTION: Protein transport. Acts, in coordination with RAB6A, to
CC regulate intra-Golgi retrograde trafficking (By similarity). It is
CC involved in autophagy, acting as a modulator of autophagosome
CC formation. {ECO:0000250, ECO:0000269|PubMed:18448665}.
CC -!- ACTIVITY REGULATION: Regulated by a guanine nucleotide-exchange factor
CC (GEF) and a GTPase-activating protein (GAP) and alternates between an
CC inactive GDP-bound and an active GTP-bound form. In vitro, SGSM2 acts
CC as its GAP and inactivates it by stimulating its GTPase activity.
CC {ECO:0000250|UniProtKB:Q9H082}.
CC -!- SUBUNIT: Interacts with RIC1 (via C-terminus domain); the interaction
CC is direct with a preference for RAB33B-GTP. Interacts with RGP1 (By
CC similarity). Interacts with ATG16L1; the interaction is important for
CC autophagosome formation (PubMed:18448665). Interacts with ATG16L2;
CC however interaction is approximately hundred times lower than for
CC ATG16L1 (PubMed:22082872). {ECO:0000250|UniProtKB:Q9H082,
CC ECO:0000269|PubMed:18448665, ECO:0000269|PubMed:22082872}.
CC -!- INTERACTION:
CC O35963; Q08484: GYP1; Xeno; NbExp=3; IntAct=EBI-6379521, EBI-8005;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18448665, ECO:0000269|PubMed:9512502}; Lipid-anchor
CC {ECO:0000305}. Golgi apparatus, cis-Golgi network
CC {ECO:0000269|PubMed:18448665}. Note=Under starvation conditions
CC punctate RAB33B-positive structures are often observed in the cytoplasm
CC (PubMed:18448665). {ECO:0000269|PubMed:18448665}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9512502}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AB004665; BAA22655.1; -; mRNA.
DR EMBL; AB004664; BAA22654.1; -; Genomic_DNA.
DR EMBL; AK004974; BAB23710.1; -; mRNA.
DR EMBL; AK087967; BAC40064.1; -; mRNA.
DR EMBL; AK139821; BAE24147.1; -; mRNA.
DR EMBL; AK159674; BAE35278.1; -; mRNA.
DR EMBL; BC065076; AAH65076.1; -; mRNA.
DR CCDS; CCDS38427.1; -.
DR RefSeq; NP_058554.1; NM_016858.2.
DR PDB; 1Z06; X-ray; 1.81 A; A=30-202.
DR PDB; 2G77; X-ray; 2.26 A; B=14-202.
DR PDB; 6SUR; X-ray; 3.47 A; A/B/C/D/E/F=30-202.
DR PDBsum; 1Z06; -.
DR PDBsum; 2G77; -.
DR PDBsum; 6SUR; -.
DR AlphaFoldDB; O35963; -.
DR SMR; O35963; -.
DR BioGRID; 202543; 9.
DR DIP; DIP-60512N; -.
DR IntAct; O35963; 23.
DR MINT; O35963; -.
DR STRING; 10090.ENSMUSP00000063054; -.
DR iPTMnet; O35963; -.
DR PhosphoSitePlus; O35963; -.
DR jPOST; O35963; -.
DR PaxDb; O35963; -.
DR PeptideAtlas; O35963; -.
DR PRIDE; O35963; -.
DR ProteomicsDB; 300356; -.
DR Antibodypedia; 27146; 77 antibodies from 24 providers.
DR DNASU; 19338; -.
DR Ensembl; ENSMUST00000054387; ENSMUSP00000063054; ENSMUSG00000027739.
DR GeneID; 19338; -.
DR KEGG; mmu:19338; -.
DR UCSC; uc008pea.1; mouse.
DR CTD; 83452; -.
DR MGI; MGI:1330805; Rab33b.
DR VEuPathDB; HostDB:ENSMUSG00000027739; -.
DR eggNOG; KOG0084; Eukaryota.
DR GeneTree; ENSGT00940000157090; -.
DR HOGENOM; CLU_041217_10_3_1; -.
DR InParanoid; O35963; -.
DR OMA; QQFADSH; -.
DR OrthoDB; 1081271at2759; -.
DR PhylomeDB; O35963; -.
DR TreeFam; TF300097; -.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 19338; 4 hits in 75 CRISPR screens.
DR EvolutionaryTrace; O35963; -.
DR PRO; PR:O35963; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O35963; protein.
DR Bgee; ENSMUSG00000027739; Expressed in urinary bladder urothelium and 258 other tissues.
DR ExpressionAtlas; O35963; baseline and differential.
DR Genevisible; O35963; MM.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005796; C:Golgi lumen; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0000045; P:autophagosome assembly; IMP:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:1903434; P:negative regulation of constitutive secretory pathway; ISO:MGI.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:1903358; P:regulation of Golgi organization; ISO:MGI.
DR GO; GO:2000156; P:regulation of retrograde vesicle-mediated transport, Golgi to ER; ISS:UniProtKB.
DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:MGI.
DR CDD; cd04115; Rab33B_Rab33A; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041822; Rab33A/B.
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 3D-structure; Autophagy; Direct protein sequencing; Golgi apparatus;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..229
FT /note="Ras-related protein Rab-33B"
FT /id="PRO_0000121240"
FT BINDING 39..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 148..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 178..180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 229
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 227
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 229
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 47
FT /note="T->N: Affects interaction with ATG16L1."
FT /evidence="ECO:0000269|PubMed:18448665"
FT MUTAGEN 92
FT /note="Q->L: Does not affect interaction with ATG16L1.
FT Induces lipidation of LC3."
FT /evidence="ECO:0000269|PubMed:18448665"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1Z06"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:1Z06"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:1Z06"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1Z06"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:1Z06"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1Z06"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:1Z06"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1Z06"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:1Z06"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:1Z06"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2G77"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:1Z06"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1Z06"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:1Z06"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1Z06"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1Z06"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:1Z06"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:1Z06"
SQ SEQUENCE 229 AA; 25767 MW; EE2B3E482FC4365A CRC64;
MTSEMESSLE VSFSSSCAVS GASGCLPPAR SRIFKIIVIG DSNVGKTCLT YRFCAGRFPD
RTEATIGVDF RERAVDIDGE RIKIQLWDTA GQERFRKSMV QHYYRNVHAV VFVYDMTNMA
SFHSLPAWIE ECKQHLLAND IPRILVGNKC DLRSAIQVPT DLAQKFADTH SMPLFETSAK
NPNDNDHVEA IFMTLAHKLK SHKPLMLSQL PDNRISLKPE TKPAVTCWC
