RAB26_BOVIN
ID RAB26_BOVIN Reviewed; 256 AA.
AC Q29RR0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ras-related protein Rab-26;
GN Name=RAB26;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in exocrine secretion: regulates the secretion
CC of acinar granules in the parotid gland. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BC114066; AAI14067.1; -; mRNA.
DR RefSeq; NP_001039674.1; NM_001046209.1.
DR AlphaFoldDB; Q29RR0; -.
DR SMR; Q29RR0; -.
DR STRING; 9913.ENSBTAP00000000348; -.
DR PaxDb; Q29RR0; -.
DR PRIDE; Q29RR0; -.
DR Ensembl; ENSBTAT00000000348; ENSBTAP00000000348; ENSBTAG00000000279.
DR GeneID; 515675; -.
DR KEGG; bta:515675; -.
DR CTD; 25837; -.
DR VEuPathDB; HostDB:ENSBTAG00000000279; -.
DR VGNC; VGNC:33633; RAB26.
DR eggNOG; KOG0083; Eukaryota.
DR GeneTree; ENSGT00940000158558; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q29RR0; -.
DR OMA; QEYAQDD; -.
DR OrthoDB; 1018397at2759; -.
DR TreeFam; TF323428; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000000279; Expressed in adenohypophysis and 102 other tissues.
DR ExpressionAtlas; Q29RR0; baseline and differential.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0019002; F:GMP binding; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0035272; P:exocrine system development; ISS:UniProtKB.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IEA:Ensembl.
DR GO; GO:0045055; P:regulated exocytosis; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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 Cell membrane; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..256
FT /note="Ras-related protein Rab-26"
FT /id="PRO_0000239696"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 93..101
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 31..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 119..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 177..180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 207..209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 253
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 254
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 256 AA; 27802 MW; 8E0381BB86AAEC0E CRC64;
MSRKKTPKSK AGSAPATSAL PAANGPRPVR PGTARPGPEA PPNGPPQPGR SSVGGGGDFY
DVAFKVMLVG DSGVGKTCLL VRFKDGAFLA GTFISTVGID FRNKVVDVDG MKVKLQIWDT
AGQERFRSVT HAYYRDAHAL LLLYDVTNKA SFDSIQAWLT EIQEHAQDDV VLMLLGNKVD
SAQERAVKRE DAEKLAKDYG LPFMETSAKT GLNVDLAFTA IAKELKQRHT KAPSEPRFQL
HDYIKREGRG ASCCRP