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 27-MAR-2024, entry version 202. 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; 9. DR MINT; Q9ULW5; -. 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; 9606-ENSP00000210187; -. DR PeptideAtlas; Q9ULW5; -. DR ProteomicsDB; 3418; -. DR ProteomicsDB; 85142; -. [Q9ULW5-1] DR Antibodypedia; 23581; 213 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 AGR; HGNC:14259; -. DR CTD; 25837; -. DR DisGeNET; 25837; -. DR GeneCards; RAB26; -. DR HGNC; HGNC:14259; RAB26. DR HPA; ENSG00000167964; Tissue enhanced (brain, 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; 8685at2759; -. 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 1158 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 143 other cell types or tissues. DR ExpressionAtlas; Q9ULW5; baseline and differential. 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:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0030667; C:secretory granule membrane; ISS:UniProtKB. DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:SynGO. 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:0140251; P:regulation protein catabolic process at presynapse; IDA:SynGO. DR CDD; cd04112; Rab26; 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; PTHR47978; -; 1. DR PANTHER; PTHR47978:SF21; RAS-RELATED PROTEIN RAB-26; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00177; ARF; 1. 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; Q9ULW5; HS. 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 //