RAB26_MOUSE
ID RAB26_MOUSE Reviewed; 260 AA.
AC Q504M8;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ras-related protein Rab-26;
GN Name=Rab26;
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 TISSUE=Pancreas;
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 [2]
RP INTERACTION WITH RIMS1.
RX PubMed=12578829; DOI=10.1074/jbc.m212341200;
RA Fukuda M.;
RT "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT Identification of a critical determinant of Rab3A/Rab27A recognition by
RT Rim2.";
RL J. Biol. Chem. 278:15373-15380(2003).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20038531; DOI=10.1128/mcb.01328-09;
RA Tian X., Jin R.U., Bredemeyer A.J., Oates E.J., Blazewska K.M.,
RA McKenna C.E., Mills J.C.;
RT "RAB26 and RAB3D are direct transcriptional targets of MIST1 that regulate
RT exocrine granule maturation.";
RL Mol. Cell. Biol. 30:1269-1284(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 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. Mediates transport of ADRA2A
CC and ADRA2B from the Golgi to the cell membrane. Plays a role in the
CC maturation of zymogenic granules and in pepsinogen secretion in the
CC stomach (By similarity). Plays a role in the secretion of amylase from
CC acinar granules in the parotid gland. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ADRA2B (By similarity). Interacts with RIMS1.
CC {ECO:0000250, ECO:0000269|PubMed:12578829}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000305|PubMed:20038531}; Lipid-anchor
CC {ECO:0000305|PubMed:20038531}; Cytoplasmic side
CC {ECO:0000305|PubMed:20038531}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9ULW5}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9ULW5}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9ULW5}. Note=Not localized at the plasma
CC membrane (By similarity). Inhibition of S-geranylgeranyl cysteine
CC formation abolishes membrane location. {ECO:0000250|UniProtKB:P51156}.
CC -!- TISSUE SPECIFICITY: Detected in zymogenic cells in the stomach.
CC {ECO:0000269|PubMed:20038531}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BC094931; AAH94931.1; -; mRNA.
DR CCDS; CCDS50016.1; -.
DR RefSeq; NP_796349.1; NM_177375.1.
DR AlphaFoldDB; Q504M8; -.
DR SMR; Q504M8; -.
DR BioGRID; 236652; 2.
DR IntAct; Q504M8; 3.
DR MINT; Q504M8; -.
DR STRING; 10090.ENSMUSP00000046089; -.
DR iPTMnet; Q504M8; -.
DR PhosphoSitePlus; Q504M8; -.
DR jPOST; Q504M8; -.
DR MaxQB; Q504M8; -.
DR PaxDb; Q504M8; -.
DR PRIDE; Q504M8; -.
DR ProteomicsDB; 300374; -.
DR Antibodypedia; 23581; 194 antibodies from 25 providers.
DR Ensembl; ENSMUST00000035797; ENSMUSP00000046089; ENSMUSG00000079657.
DR GeneID; 328778; -.
DR KEGG; mmu:328778; -.
DR UCSC; uc008awu.2; mouse.
DR CTD; 25837; -.
DR MGI; MGI:2443284; Rab26.
DR VEuPathDB; HostDB:ENSMUSG00000079657; -.
DR eggNOG; KOG0083; Eukaryota.
DR GeneTree; ENSGT00940000158558; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q504M8; -.
DR OMA; QEYAQDD; -.
DR OrthoDB; 1018397at2759; -.
DR PhylomeDB; Q504M8; -.
DR TreeFam; TF323428; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 328778; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Rab26; mouse.
DR PRO; PR:Q504M8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q504M8; protein.
DR Bgee; ENSMUSG00000079657; Expressed in dentate gyrus of hippocampal formation granule cell and 86 other tissues.
DR ExpressionAtlas; Q504M8; baseline and differential.
DR Genevisible; Q504M8; MM.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0030667; C:secretory granule membrane; IDA:UniProtKB.
DR GO; GO:0019002; F:GMP 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:0035272; P:exocrine system development; ISS:UniProtKB.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; ISS:UniProtKB.
DR GO; GO:0017157; P:regulation of exocytosis; ISS:UniProtKB.
DR GO; GO:0099575; P:regulation of protein catabolic process at presynapse, modulating synaptic transmission; ISO:MGI.
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 Cytoplasmic vesicle; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..260
FT /note="Ras-related protein Rab-26"
FT /id="PRO_0000121219"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 97..105
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 74..82
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 123..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 181..184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 211..213
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 257
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 258
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 260 AA; 28619 MW; 3657E725B1D004E8 CRC64;
MSRKKTPKSK GGSEPATSTL PAAAAATNGP RLAHPRTVRP GPEAPPNGPP QSIRPSLGST
GDFYDVAFKV MLVGDSGVGK TCLLVRFKDG AFLAGTFIST VGIDFRNKVL DVDGMKVKLQ
IWDTAGQERF RSVTHAYYRD AHALLLLYDI TNKDSFDNIQ AWLTEIQEYA QQDVVLMLLG
NKVDSTQDRV VKREDGEKLA KEYGLPFMET SARTGLNVDL AFTAIAKELK QRSAKAPSEP
RFRLHDYVKR EGRGVSCCRL
