RAB26_RAT
ID RAB26_RAT Reviewed; 257 AA.
AC P51156; Q6P6W7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Ras-related protein Rab-26;
GN Name=Rab26;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 63-257, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Pancreas;
RX PubMed=7864900; DOI=10.1006/bbrc.1995.1277;
RA Wagner A.C.C., Strowski M.Z., Goeke B., Williams J.A.;
RT "Molecular cloning of a new member of the Rab protein family, Rab 26, from
RT rat pancreas.";
RL Biochem. Biophys. Res. Commun. 207:950-956(1995).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Parotid gland;
RX PubMed=10857477; DOI=10.1007/s004180000130;
RA Yoshie S., Imai A., Nashida T., Shimomura H.;
RT "Expression, characterization, and localization of Rab26, a low molecular
RT weight GTP-binding protein, in the rat parotid gland.";
RL Histochem. Cell Biol. 113:259-263(2000).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16076461; DOI=10.1016/j.archoralbio.2005.06.005;
RA Nashida T., Imai A., Shimomura H.;
RT "Relation of Rab26 to the amylase release from rat parotid acinar cells.";
RL Arch. Oral Biol. 51:89-95(2006).
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 ECO:0000269|PubMed:10857477, ECO:0000269|PubMed:16076461}.
CC -!- SUBUNIT: Interacts with ADRA2B. Interacts with RIMS1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000269|PubMed:10857477, ECO:0000269|PubMed:16076461}; Lipid-
CC anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus
CC membrane {ECO:0000250|UniProtKB:Q9ULW5}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9ULW5}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9ULW5}. Note=Inhibition of S-geranylgeranyl
CC cysteine formation abolishes membrane location (By similarity).
CC Localized immediately around secretory granules in the acinar cells of
CC the parotid gland (PubMed:10857477). Not localized in plasma membranes
CC (PubMed:10857477). {ECO:0000250, ECO:0000269|PubMed:10857477}.
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, kidney, brain, submandibular
CC gland, and lung. {ECO:0000269|PubMed:7864900}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69955.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC061984; AAH61984.1; -; mRNA.
DR EMBL; U18771; AAA69955.1; ALT_INIT; mRNA.
DR PIR; JC2528; JC2528.
DR RefSeq; NP_598264.1; NM_133580.1.
DR AlphaFoldDB; P51156; -.
DR SMR; P51156; -.
DR STRING; 10116.ENSRNOP00000004249; -.
DR iPTMnet; P51156; -.
DR PhosphoSitePlus; P51156; -.
DR jPOST; P51156; -.
DR PaxDb; P51156; -.
DR PRIDE; P51156; -.
DR GeneID; 171111; -.
DR KEGG; rno:171111; -.
DR UCSC; RGD:620890; rat.
DR CTD; 25837; -.
DR RGD; 620890; Rab26.
DR VEuPathDB; HostDB:ENSRNOG00000042086; -.
DR eggNOG; KOG0083; Eukaryota.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P51156; -.
DR OMA; QEYAQDD; -.
DR OrthoDB; 1018397at2759; -.
DR PhylomeDB; P51156; -.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR PRO; PR:P51156; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000042086; Expressed in pancreas and 19 other tissues.
DR Genevisible; P51156; RN.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0030667; C:secretory granule membrane; ISS:UniProtKB.
DR GO; GO:0019002; F:GMP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0035272; P:exocrine system development; IDA: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; IDA:UniProtKB.
DR GO; GO:0099575; P:regulation of protein catabolic process at presynapse, modulating synaptic transmission; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:RGD.
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 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..257
FT /note="Ras-related protein Rab-26"
FT /id="PRO_0000121220"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 94..102
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 71..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 120..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 178..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 208..210
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 254
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 255
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 257 AA; 28203 MW; 3C4A12A2B8333474 CRC64;
MSRKKTPKSK GGSVPAASTL PAAANGPRLA HPRTARPGPE APPNGPPQSG RPSLGGTGDF
YDVAFKVMLV GDSGVGKTCL LVRFKDGAFL AGTFISTVGI DFRNKVLDVD GMKVKLQIWD
TAGQERFRSV THAYYRDAHA LLLLYDITNK DSFDNIQAWL TEIQEYAQQD VVLMLLGNKV
DSTQERVVKR EDGEKLAKEY GLPFMETSAK SGLNVDLAFT AIAKELKQRS TKAPSEPRFR
LHDYVKREGR GVSCCRL
