RAB26_HUMAN
ID RAB26_HUMAN Reviewed; 256 AA.
AC Q9ULW5; B2RAA6; Q3L6K5; Q6NXS7;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Ras-related protein Rab-26;
GN Name=RAB26;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Zhu N., Xu Y., Yang J., Li R.;
RT "Cloning, expression and characterization of human Ras-related oncogene
RT Rab26.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 66-256 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=11043516; DOI=10.1007/s100380070023;
RA Seki N., Yoshikawa T., Hattori A., Miyajima N., Muramatsu M., Saito T.;
RT "cDNA cloning of a human RAB26-related gene encoding a Ras-like GTP-binding
RT protein on chromosome 16p13.3 region.";
RL J. Hum. Genet. 45:309-314(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-256 (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, AND MUTAGENESIS OF THR-77.
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).
RN [9]
RP FUNCTION, INTERACTION WITH ADRA2B, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-77; GLN-123 AND ASN-177.
RX PubMed=23105096; DOI=10.1074/jbc.m112.410936;
RA Li C., Fan Y., Lan T.H., Lambert N.A., Wu G.;
RT "Rab26 modulates the cell surface transport of alpha2-adrenergic receptors
RT from the Golgi.";
RL J. Biol. Chem. 287:42784-42794(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 56-233 IN COMPLEX WITH GTP ANALOG.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human RAB26 in complex with a GTP analogue.";
RL Submitted (FEB-2009) to the PDB data bank.
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. Plays a role in the secretion of amylase from acinar granules
CC in the parotid gland. {ECO:0000269|PubMed:20038531,
CC ECO:0000269|PubMed:23105096}.
CC -!- SUBUNIT: Interacts with RIMS1 (By similarity). Interacts with ADRA2B.
CC {ECO:0000250, ECO:0000269|PubMed:23105096}.
CC -!- INTERACTION:
CC Q9ULW5; P18089: ADRA2B; NbExp=4; IntAct=EBI-958239, EBI-9077302;
CC Q9ULW5; Q5TD97: FHL5; NbExp=3; IntAct=EBI-958239, EBI-750641;
CC Q9ULW5; Q14525: KRT33B; NbExp=3; IntAct=EBI-958239, EBI-1049638;
CC Q9ULW5; O43482: OIP5; NbExp=3; IntAct=EBI-958239, EBI-536879;
CC Q9ULW5; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-958239, EBI-12817837;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:23105096}; Lipid-anchor
CC {ECO:0000269|PubMed:23105096}; Cytoplasmic side
CC {ECO:0000269|PubMed:23105096}. Cytoplasmic vesicle, secretory vesicle
CC membrane {ECO:0000305|PubMed:23105096}; Lipid-anchor
CC {ECO:0000305|PubMed:23105096}; Cytoplasmic side
CC {ECO:0000305|PubMed:23105096}. 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULW5-2; Sequence=VSP_056879;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA84707.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY646153; AAU88191.1; -; mRNA.
DR EMBL; AK314110; BAG36803.1; -; mRNA.
DR EMBL; AC009065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85552.1; -; Genomic_DNA.
DR EMBL; BC066913; AAH66913.1; -; mRNA.
DR EMBL; AB027137; BAA84707.1; ALT_INIT; mRNA.
DR EMBL; AF498952; AAM21100.1; -; mRNA.
DR CCDS; CCDS10460.1; -. [Q9ULW5-1]
DR CCDS; CCDS76806.1; -. [Q9ULW5-2]
DR RefSeq; NP_001294982.1; NM_001308053.1. [Q9ULW5-2]
DR RefSeq; NP_055168.2; NM_014353.4. [Q9ULW5-1]
DR PDB; 2G6B; X-ray; 2.00 A; A=56-233.
DR PDBsum; 2G6B; -.
DR AlphaFoldDB; Q9ULW5; -.
DR SMR; Q9ULW5; -.
DR BioGRID; 117364; 20.
DR IntAct; Q9ULW5; 8.
DR STRING; 9606.ENSP00000210187; -.
DR iPTMnet; Q9ULW5; -.
DR PhosphoSitePlus; Q9ULW5; -.
DR BioMuta; RAB26; -.
DR DMDM; 134044256; -.
DR jPOST; Q9ULW5; -.
DR MassIVE; Q9ULW5; -.
DR MaxQB; Q9ULW5; -.
DR PaxDb; Q9ULW5; -.
DR PeptideAtlas; Q9ULW5; -.
DR PRIDE; Q9ULW5; -.
DR ProteomicsDB; 3418; -.
DR ProteomicsDB; 85142; -. [Q9ULW5-1]
DR Antibodypedia; 23581; 194 antibodies from 25 providers.
DR DNASU; 25837; -.
DR Ensembl; ENST00000210187.11; ENSP00000210187.6; ENSG00000167964.13. [Q9ULW5-1]
DR Ensembl; ENST00000541451.5; ENSP00000441580.1; ENSG00000167964.13. [Q9ULW5-2]
DR GeneID; 25837; -.
DR KEGG; hsa:25837; -.
DR MANE-Select; ENST00000210187.11; ENSP00000210187.6; NM_014353.5; NP_055168.2.
DR UCSC; uc002cou.4; human. [Q9ULW5-1]
DR CTD; 25837; -.
DR DisGeNET; 25837; -.
DR GeneCards; RAB26; -.
DR HGNC; HGNC:14259; RAB26.
DR HPA; ENSG00000167964; Tissue enhanced (brain, choroid plexus, liver, pancreas).
DR MIM; 605455; gene.
DR neXtProt; NX_Q9ULW5; -.
DR OpenTargets; ENSG00000167964; -.
DR PharmGKB; PA34116; -.
DR VEuPathDB; HostDB:ENSG00000167964; -.
DR eggNOG; KOG0083; Eukaryota.
DR GeneTree; ENSGT00940000158558; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q9ULW5; -.
DR OMA; QEYAQDD; -.
DR OrthoDB; 1018397at2759; -.
DR PhylomeDB; Q9ULW5; -.
DR TreeFam; TF323428; -.
DR PathwayCommons; Q9ULW5; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q9ULW5; -.
DR BioGRID-ORCS; 25837; 19 hits in 1080 CRISPR screens.
DR ChiTaRS; RAB26; human.
DR EvolutionaryTrace; Q9ULW5; -.
DR GeneWiki; RAB26; -.
DR GenomeRNAi; 25837; -.
DR Pharos; Q9ULW5; Tbio.
DR PRO; PR:Q9ULW5; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9ULW5; protein.
DR Bgee; ENSG00000167964; Expressed in right hemisphere of cerebellum and 141 other tissues.
DR ExpressionAtlas; Q9ULW5; baseline and differential.
DR Genevisible; Q9ULW5; HS.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO.
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; IDA:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0030667; C:secretory granule membrane; ISS:UniProtKB.
DR GO; GO:0019002; F:GMP binding; IMP:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IMP:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0035272; P:exocrine system development; IMP:UniProtKB.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; IMP: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; IDA:SynGO.
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 3D-structure; Alternative splicing; Cytoplasmic vesicle; Golgi apparatus;
KW GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..256
FT /note="Ras-related protein Rab-26"
FT /id="PRO_0000121218"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 93..101
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 7..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.10"
FT BINDING 119..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.10"
FT BINDING 177..180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.10"
FT BINDING 207..209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.10"
FT LIPID 253
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 254
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056879"
FT MUTAGEN 77
FT /note="T->N: Inactive, constitutively GDP-bound. Abolishes
FT location at Golgi membranes. Impairs transport of ADRA2A
FT and ADRA2B from the Golgi to the cell membrane."
FT /evidence="ECO:0000269|PubMed:20038531,
FT ECO:0000269|PubMed:23105096"
FT MUTAGEN 123
FT /note="Q->L: Constitutively activated."
FT /evidence="ECO:0000269|PubMed:23105096"
FT MUTAGEN 177
FT /note="N->I: Inactive, due to loss of GNP binding.
FT Abolishes location at Golgi membranes. Impairs transport of
FT ADRA2A and ADRA2B from the Golgi to the cell membrane."
FT /evidence="ECO:0000269|PubMed:23105096"
FT CONFLICT 227
FT /note="Q -> R (in Ref. 5; AAH66913)"
FT /evidence="ECO:0000305"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:2G6B"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:2G6B"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:2G6B"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:2G6B"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2G6B"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:2G6B"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:2G6B"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:2G6B"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:2G6B"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:2G6B"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2G6B"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:2G6B"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:2G6B"
SQ SEQUENCE 256 AA; 27900 MW; 575232F4B9E7FA7E CRC64;
MSRKKTPKSK GASTPAASTL PTANGARPAR SGTALSGPDA PPNGPLQPGR PSLGGGVDFY
DVAFKVMLVG DSGVGKTCLL VRFKDGAFLA GTFISTVGID FRNKVLDVDG VKVKLQMWDT
AGQERFRSVT HAYYRDAHAL LLLYDVTNKA SFDNIQAWLT EIHEYAQHDV ALMLLGNKVD
SAHERVVKRE DGEKLAKEYG LPFMETSAKT GLNVDLAFTA IAKELKQRSM KAPSEPRFRL
HDYVKREGRG ASCCRP
