ID   RAB10_DIPOM             Reviewed;         200 AA.
AC   P22127;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Ras-related protein Rab-10;
DE            Short=ORA1;
OS   Diplobatis ommata (Ocellated electric ray) (Discopyge ommata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Narcinidae; Diplobatis.
OX   NCBI_TaxID=1870830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Electric lobe;
RX   PubMed=1899244; DOI=10.1016/s0021-9258(18)52297-3;
RA   Ngsee J.K., Elferink L.A., Scheller R.H.;
RT   "A family of ras-like GTP-binding proteins expressed in electromotor
RT   neurons.";
RL   J. Biol. Chem. 266:2675-2680(1991).
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. That Rab is mainly involved
CC       in the biosynthetic transport of proteins from the Golgi to the plasma
CC       membrane. Also plays a specific role in asymmetric protein transport to
CC       the plasma membrane within the polarized neuron and epithelial cells.
CC       In neurons, it is involved in axonogenesis through regulation of
CC       vesicular membrane trafficking toward the axonal plasma membrane while
CC       in epithelial cells, it regulates transport from the Golgi to the
CC       basolateral membrane. Moreover, may play a role in the basolateral
CC       recycling pathway and in phagosome maturation. Finally, may play a role
CC       in endoplasmic reticulum dynamics and morphology controlling tubulation
CC       along microtubules and tubules fusion (By similarity). {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC       exchange factor (GEF), while inactivation through hydrolysis of bound
CC       GTP is catalyzed by a GTPase activating protein (GAP). That Rab is
CC       activated by the DENND4C guanine exchange factor (GEF) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305};
CC       Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi
CC       apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P24409}.
CC       Endosome membrane {ECO:0000250|UniProtKB:P61026}. Recycling endosome
CC       membrane {ECO:0000250|UniProtKB:P24409}. Cytoplasmic vesicle, phagosome
CC       membrane {ECO:0000250|UniProtKB:P24409}. Cell projection, cilium
CC       {ECO:0000250|UniProtKB:P61027}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P61027}. Note=Associates with SLC2A4/GLUT4
CC       storage vesicles (By similarity). Localizes to the base of the cilium
CC       (By similarity). Transiently associates with phagosomes (By
CC       similarity). Localizes to the endoplasmic reticulum at domains of new
CC       tubule growth (By similarity). {ECO:0000250|UniProtKB:P24409,
CC       ECO:0000250|UniProtKB:P61026, ECO:0000250|UniProtKB:P61027}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {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; M38390; AAA49230.1; -; mRNA.
DR   PIR; A38625; A38625.
DR   AlphaFoldDB; P22127; -.
DR   SMR; P22127; -.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0071782; C:endoplasmic reticulum tubular network; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR   GO; GO:0071786; P:endoplasmic reticulum tubular network organization; ISS:UniProtKB.
DR   GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR   GO; GO:0045200; P:establishment of neuroblast polarity; ISS:UniProtKB.
DR   GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; ISS:UniProtKB.
DR   GO; GO:0030859; P:polarized epithelial cell differentiation; ISS:UniProtKB.
DR   GO; GO:1903361; P:protein localization to basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
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 projection; Cytoplasmic vesicle; Endoplasmic reticulum; Endosome;
KW   Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW   Prenylation; Protein transport; Transport.
FT   CHAIN           1..200
FT                   /note="Ras-related protein Rab-10"
FT                   /id="PRO_0000121149"
FT   REGION          181..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         16..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..68
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         122..125
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           198
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           199
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   200 AA;  22623 MW;  41D38E3D760519C5 CRC64;
     MAKKTYDLLF KLLLIGDSGV GKTCVLFRFS DDAFNTTFIS TIGIDFKIKT VELHGKKIKL
     QIWDTAGQER FHTITTSYYR GAMGIMLVYD ITNAKSFENI SKWLRNIDEH ANEDVERMLL
     GNKCDMEDKR VVLKSKGEQI AREHAIRFFE TSAKANINIE KAFLTLAEDI LQKTPVKEPD
     RENVDISTTG GGTGLKKCCS